and Proteins

Biologically Active Peptides …………………………… 2
Biologically Active Proteins ………………………… 152–1 –Biologically Active Peptides

Biologically
ActivePeptidesand ProteinsBiologically Active Peptides
Biologically active peptides listed in this section are chemically synthesized and rigorously subjected toindependent purity testing. They are fully guaranteed according to our Purity Criteria on page IV (XVI).

Ac-Asp-Glu
CodeCompound

4167

Ac-Asp-Glu-20

(M.W. 304.25)

Price:Yen
Bulk
C11H16N2O8[3106-85-2]

25 mg
100 mg

4,800
13,500Endogenous Excitatory Neurotransmitter
1) K.L. Reichert and F. Fonnum, J. Neurochem., 16, 1409 (1969). (Original)
2) K.J. Koller and J.T. Coyle, Eur. J. Pharmacol., 98, 193 (1984). (Characterization of Receptor )3) K.J. Koller, R. Zaczek, and J.T. Coyle, J. Neurochem., 43, 1136 (1984). (Localization in Brain)
4) J.H. Neale, T. Bzdega, and B. Wroblewska, J. Neurochem., 75, 443 (2000). (Review)

Adjuvant Peptide
4031-v

Adjuvant Peptide-20

N-Ac-Mur-Ala-D-Glu-NH2(Mur: Muramic acid)(M.W. 492.48)

C19H32N4O11

0.5 mg

3,500

Bulk

25 mg

70,000[53678-77-6]

4031

Adjuvant Peptide-20

N-Ac-Mur-Ala-D-Glu-NH2 • 2H2O
(Mur: Muramic acid)(M.W. 492.48 • 36.03)

Vial

C19H32N4O11 • 2H2O

[53678-77-6]

Muramyl Dipeptide
1) F. Ellouz, A. Adam, R. Ciorbaru, and E. Lederer, Biochem. Biophys. Res. Commun., 59, 1317 (1974). (Original)
2) S. Kotani, Y. Watanabe, F. Kinoshita, T. Shimono, I. Morisaki, T. Shiba, S. Kusumoto, Y. Tarumi, and K. Ikenaka,
Biken J., 18, 105 (1975). (Chem. Synthesis & Immun. Activity)

Adrenocorticotropic Hormone (ACTH)
4109-v-20

ACTH (Human, 1-24)
Adrenocorticotropic Hormone (Human, 1-24)
Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-GlyLys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-ValLys-Val-Tyr-Pro(M.W. 2933.4)

C136H210N40O31S

Vial

0.5 mg18,000[16960-16-0]

1) B. Riniker, P. Sieber, W. Rittel, and H. Zuber, Nature (New Biol.), 235,114 (1972). (Original; Structure)–2 –Adrenomedullin and Related Peptides2) D.A. Schell, R.C. Vari, and W.K. Samson, Trends Endocrinol. Metab., 7, 7 (1996). (Review)Eur. J. Med. Chem., 40, 737 (2005). (Review)

Code

Compound4278-sAdrenomedullin (Human)*
Tyr-Arg-Gln-Ser-Met-Asn-Asn-Phe-Gln-GlyLeu-Arg-Ser-Phe-Gly-Cys-Arg-Phe-Gly-ThrCys-Thr-Val-Gln-Lys-Leu-Ala-His-Gln-IleTyr-Gln-Phe-Thr-Asp-Lys-Asp-Lys-Asp-AsnVal-Ala-Pro-Arg-Ser-Lys-Ile-Ser-Pro-GlnGly-Tyr-NH2-20

Price:Yen
Vial

0.1 mg28,000(Disulfide bond between Cys16-Cys21)(M.W. 6028.7)

C264H406N80O77S3[148498-78-6]

Hypotensive Peptide
1) K. Kitamura, K. Kangawa, M. Kawamoto, Y. Ichiki, S. Nakamura, H. Matsuo, and T. Eto, Biochem. Biophys. Res.
Commun., 192, 553 (1993). (Original)
2) K. Kitamura, J. Sakata, K. Kangawa, M. Kojima, H. Matsuo, and T. Eto, Biochem. Biophys. Res. Commun.,
194, 720 (1993). (Original; cDNA)• This product is distributed under the license of Shionogi & Co., Ltd. Its use for any purpose other than research isstrictly prohibited.

4325-v-20

Adrenomedullin (Human, 1-25)*
Tyr-Arg-Gln-Ser-Met-Asn-Asn-Phe-Gln-GlyLeu-Arg-Ser-Phe-Gly-Cys-Arg-Phe-Gly-ThrCys-Thr-Val-Gln-Lys

Vial

0.5 mg25,000(Disulfide bond between Cys16-Cys21)(M.W. 2927.3)

C125H192N40O36S3

Vasopressor Fragment of Human Adrenomedullin
1) T.X. Watanabe, Y. Itahara, T. Inui, K. Yoshizawa-Kumagaye, K. Nakajima, and S. Sakakibara, Biochem. Biophys. Res.
Commun., 219, 59 (1996). (Original)

4302-v-20

Adrenomedullin (Human, 22-52)
Thr-Val-Gln-Lys-Leu-Ala-His-Gln-Ile-TyrGln-Phe-Thr-Asp-Lys-Asp-Lys-Asp-Asn-ValAla-Pro-Arg-Ser-Lys-Ile-Ser-Pro-Gln-GlyTyr-NH2(M.W. 3576.0)

C159H252N46O48

Vial

0.5 mg25,000[159899-65-7]

Adrenomedullin Antagonist
1) S. Eguchi, Y. Hirata, H. Iwasaki, K. Sato, T.X. Watanabe, T. Inui, K. Nakajima, S. Sakakibara, and F. Marumo,
Endocrinology, 135, 2454 (1994). (Original)
2) J. Penchalaneni, S. J. Wimalawansa, and C. Yallampalli, Biol. Reprod., 71, 1475 (2004). (Pharmacol.)4281-s-20

Adrenomedullin (Rat)*
Tyr-Arg-Gln-Ser-Met-Asn-Gln-Gly-Ser-ArgSer-Thr-Gly-Cys-Arg-Phe-Gly-Thr-Cys-ThrMet-Gln-Lys-Leu-Ala-His-Gln-Ile-Tyr-GlnPhe-Thr-Asp-Lys-Asp-Lys-Asp-Gly-Met-AlaPro-Arg-Asn-Lys-Ile-Ser-Pro-Gln-Gly-Tyr-NH2

Vial

0.1 mg28,000(Disulfide bond between Cys14-Cys19)(M.W. 5729.4)

C242H381N77O75S5

Hypotensive Peptide
1) J. Sakata, T. Shimokubo, K. Kitamura, S. Nakamura, K. Kangawa, H. Matsuo, and T. Eto, Biochem. Biophys. Res.
Commun., 195, 921 (1993). (Original; cDNA & Biological Activity)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

–3 –and Proteins3) M. Julián, M. Cacho, M.A. Garc́a, S. Mart́n-Santamar́a, B. de Pascual-Teresa, A. Ramos, A. Mart́nez, and F. Cuttitta,

Biologically Active Peptides

1) K. Kitamura, K. Kangawa, H. Matsuo, and T. Eto, Drugs, 49, 485 (1995). (Review)Adrenomedullin and Related Peptides (continued)
Code

Compound4421-sAdrenomedullin 2 / Intermedin (Human)
Thr-Gln-Ala-Gln-Leu-Leu-Arg-Val-Gly-CysVal-Leu-Gly-Thr-Cys-Gln-Val-Gln-Asn-LeuSer-His-Arg-Leu-Trp-Gln-Leu-Met-Gly-ProAla-Gly-Arg-Gln-Asp-Ser-Ala-Pro-Val-AspPro-Ser-Ser-Pro-His-Ser-Tyr-NH2-20

Price:Yen
Vial

0.1 mg24,000(Disulfide bond between Cys10 and Cys15)(M.W. 5100.7)

C219H349N69O66S3

Cardiovascular and Renal Regulator / Suppressor for Food Intake and Gastric Emptying
4422-s-20

Adrenomedullin 2 / Intermedin (Rat)
Pro-His-Ala-Gln-Leu-Leu-Arg-Val-Gly-CysVal-Leu-Gly-Thr-Cys-Gln-Val-Gln-Asn-LeuSer-His-Arg-Leu-Trp-Gln-Leu-Val-Arg-ProSer-Gly-Arg-Arg-Asp-Ser-Ala-Pro-Val-AspPro-Ser-Ser-Pro-His-Ser-Tyr-NH2

Vial

0.1 mg24,000(Disulfide bond between Cys10 and Cys15)(M.W. 5216.9)

C226H361N75O64S2

Cardiovascular and Renal Regulator / Suppressor for Food Intake and Gastric Emptying
Five adrenomedullins (AM1-5) were cloned and identified from the pufferfish, Takifugu rubripes. Three ofthese [AM1/4/5] are counterparts of well-known mammalian adrenomedullins (AM) (Code 4278-s and 4281-s),
but the other two peptides [AM2/3] were unidentified in mammals 1) . Next, Takei and coworkers
attempted to detect cDNA encoding mammalian peptides corresponding to the already identified
adrenomedullins in pufferfish. As a result, they successfully discovered human and rat adrenomedullin 2 (AM2)
as a 47-residue peptide with 6 amino acid divergence2). Another group, Roh and coworkers, utilized aphylogenetic profiling approach to analyze GenBank databases, which led them to identify human and rat
intermedin (IMD); 47 amino acid peptides of these species (IMDL, named after long form of intermedin)3),
which is identical to AM2 . They also predicted IMDS (IMD short) as another possible product processed atsingle Arg-residue, located at 7 amino acid residue downstream of the amino-terminus of IMDL.
The synthetic cognate peptides of AM2 and two types of IMD showed the following biological activities: i)dose-dependent hypotensive effects at doses between 0.1-10 nmol/kg in mice (AM2) and at 10 and 50 nM in
normal and SHR rats (IMD), respectively, the efficacy of AM2 in mice seems to be higher than that of AM, ii)
antidiuretic and antinatriuretic activities in mice (AM2), and iii) anorexic activity in fasted mice through gastric
emptying suppression (IMD). It has been suggested that these activities may be regulated through its own
specific receptor or through shared calcitonin receptor-like receptor (CRLR) and related proteins, suchas receptor activity modifying protein (RAMP) complexes. The effects of AM2 on renal hemodynamics andurine formation in rats have been reported4). Later, the effects of AM2/IMD within central nervous system5) andimmunocytochemical localization in human6) were reported.
1) M. Ogoshi, K. Inoue, and Y. Takei, Biochem. Biophys. Res. Commun., 311, 1072 (2003). (Takifugu rubripes
Adrenomedullins)
2) Y. Takei, K. Inoue, M. Ogoshi, T. Kawahara, H. Bannai, and S. Miyano, FEBS Lett., 556, 53 (2004). (Original;
Adrenomedullin 2)
3) J. Roh, C.L. Chang, A. Bhalla, C. Klein, and S.Y.T. Hsu, J. Biol. Chem., 279, 7264 (2004). (Original; Intermedin)
4) Y. Fujisawa, Y. Nagai, A. Miyatake, Y. Takei, K. Miura, T. Shoukouji, A. Nishiyama, S. Kim ura, and Y. Abe, Eur. J.
Pharmacol., 497, 75 (2004). (Pharmacol.)5) M.M. Taylor, S.L. Bagley, and W.K. Samson, Am. J. Physiol. Regul. Integr. Comp. Physiol., 288, R919 (2005).
(Pharmacol.)6) K. Takahashi, K. Kikuchi, Y. Maruyama, T. Urabe, K. Nakajima, H. Sasano, Y. Imai, O. Murakami, and K. Totsune,
Peptides, 27, 1383 (2006). (Histochem.)
7) D. Bell and B.J. McDermott, Br. J. Pharmacol., 153, S247 (2008). (Review)–4 –Adrenomedullin and Related Peptides (continued)
4291-v

PAMP (Human)
Proadrenomedullin N-terminal 20 Peptide (Human)
Ala-Arg-Leu-Asp-Val-Ala-Ser-Glu-Phe-ArgLys-Lys-Trp-Asn-Lys-Trp-Ala-Leu-Ser-Arg-NH2-20

(M.W. 2460.8)

Price:Yen

C112H178N36O27

Vial

0.5 mg21,000and Proteins

Compound[150238-87-2]

Hypotensive Peptide
1) K. Kitamura, J. Sakata, K. Kangawa, M. Kojima, H. Matsuo, and T. Eto, Biochem. Biophys. Res. Commun.,
194, 720 (1993). (Original; cDNA)2) H. Washimine, K. Kitamura, Y. Ichiki, Y. Yamamoto, K. Kangawa, H. Matsuo, and T. Eto, Biochem. Biophys. Res.
Commun., 202, 1081 (1994). (Distribution in Human Tissue)3) K. Kitamura, K. Kangawa, Y. Ishiyama, H. Washimine, Y. Ichiki, M. Kawamoto, N. Minamino, H. Matsuo, and T. Eto,
FEBS Lett., 351, 35 (1994). (Pharmacol.)4) F. Katoh, K. Kitamura, H. Niina, R. Yamamoto, H. Washimine, K. Kangawa, Y. Yamamoto, H. Kobayashi, T. Eto, andA. Wada, J. Neurochem., 64, 459 (1995). (Pharmacol.)• This product is distributed under the license of Shionogi & Co., Ltd. Its use for any purpose other than research isstrictly prohibited.

4292-v-20

PAMP (Rat)
Proadrenomedullin N-terminal 20 Peptide (Rat)
Ala-Arg-Leu-Asp-Thr-Ser-Ser-Gln-Phe-ArgLys-Lys-Trp-Asn-Lys-Trp-Ala-Leu-Ser-Arg-NH2(M.W. 2477.8)

Vial

0.5 mg21,000C111H177N37O28

Hypotensive Peptide
1) J. Sakata, T. Shimokubo, K. Kitamura, S. Nakamura, K. Kangawa, H. Matsuo, and T. Eto, Biochem. Biophys. Res.
Commun., 195, 921 (1993). (Original; cDNA)

4339-v-20

PAMP-12 (Human)
Proadrenomedullin N-terminal 20 Peptide (Human, 9-20)
Phe-Arg-Lys-Lys-Trp-Asn-Lys-Trp-Ala-LeuSer-Arg-NH2(M.W. 1618.9)

Vial

0.5 mg

8,000

C77H119N25O14

Hypotensive Peptide / Major Endogenous Form of PAMP
1) K. Kuwasato, K. Kitamura, Y. Ishiyama, H. Washimine, J. Kato, K. Kangawa, and T. Eto, FEBS Lett., 414, 105 (1997).
(Original)

List of Adrenomedullin and Related Peptides
Code

Adrenomedullin4278-s4302-v
4325-v
4281-s4421-s4422-sPAMP4291-v
4292-v
4339-v
CGRP
4160-s
4160-v
4232-v
4163-s4163-v
Amylin4219-v
4220-vCompoundQuantity

Price: Yen

Page

Adrenomedullin (Human)
Adrenomedullin (Human, 22-52)★1
Adrenomedullin (Human, 1-25)★2
Adrenomedullin (Rat)
Adrenomedullin 2 / Intermedin (Human)
Adrenomedullin 2 / Intermedin (Rat)

0.1 mg vial
0.5 mg vial
0.5 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial

28,00025,00025,00028,00024,00024,000

3
3
3
3
4
4

PAMP (Human)
PAMP (Rat)
PAMP-12 (Human)

0.5 mg vial
0.5 mg vial
0.5 mg vial

21,00021,000
8,000

above
above
above

CGRP (Human)
CGRP (Human)
CGRP (Human, 8-37)★1
CGRP (Rat)
CGRP (Rat)

0.1 mg vial
0.5 mg vial
0.5 mg vial
0.1 mg vial
0.5 mg vial

11,50035,00022,00011,50035,000

34
34
34
35
35

Amylin (Human)
Amylin (Rat)

0.5 mg vial
0.5 mg vial

41,00038,00010
10★1: Antagonist, ★2: Vasopressor Fragment–5 –Biologically Active Peptides

CodeAdropin
Code

Compound4456-sAdropin (Human, 34-76)(Rat, Mouse)
Cys-His-Ser-Arg-Ser-Ala-Asp-Val-Asp-SerLeu-Ser-Glu-Ser-Ser-Pro-Asn-Ser-Ser-ProGly-Pro-Cys-Pro-Glu-Lys-Ala-Pro-Pro-ProGln-Lys-Pro-Ser-His-Glu-Gly-Ser-Tyr-LeuLeu-Gln-Pro

New

-20

Price:Yen
Vial

0.1 mg25,000(Disulfide bond between Cys34-Cys56)(M.W. 4499.8)

C190H293N55O68S2

Regulatory Factor in Energy Homeostasis
Peptides secreted from peripheral organs regulate lipid metabolism in key insulin-target tissues and areimportant for energy homeostasis and maintaining insulin sensitivity. Much attention has been given to
adipokines secreted by adipocytes. While receiving less attention, liver-secreted factors are also critical forenergy homeostasis.
Adropin, initially identified during microarray analysis of liver gene expression in mouse models of obesity,
is a 76-residue peptide encoded by the energy homeostasis associated gene Enho1). Bioinformatics analysis
suggested adropin (34-76) being a secreted form of adropin with high probability. Thus disulfide-linked
adropin (34-76) was chemically synthesized for biological tests; glucose homeostasis and hepatic lipid
metabolism were improved in mouse with 90 or 900 nmol/kg/day through intraperitoneal administration.
These effects were independent of adiposity or food intake. Considering the alteration of adropin mRNA levelassociated with obesity, adropin (34-76) may be a powerful peptide in the study of obesity-associatedhepatosteatosis and hyperinsulinemia.
1) K.G. Kumar, J.L. Trevaskis, D.D. Lam, G.M. Sutton, R.A. Koza, V.N. Chouljenko, K.G. Kousoulas, P.M. Rogers,
R.A. Kesterson, M. Thearle, A.W. Ferrante, Jr., R.L. Mynatt, T.P. Burris, J.Z. Dong, H.A. Halem, M.D. Culler,
L.K. Heisler, J.M. Stephens, and A.A. Butler, Cell Metab., 8, 468 (2008). (Original: Primary Structure / Pharmacol.)ω-Agatoxins
1) B.M. Olivera, G.P. Miljanich, J. Ramachandran, and M.E. Adams, Annu. Rev. Biochem., 63, 823 (1994). (Review)2) O.D. Uchitel, Toxicon, 35, 1161 (1997). (Review)

4256-s-20ω-Agatoxin IVA
ω-Aga-IVA(Funnel Web Spider, Agelenopsis aperta)
Lys-Lys-Lys-Cys-Ile-Ala-Lys-Asp-Tyr-GlyArg-Cys-Lys-Trp-Gly-Gly-Thr-Pro-Cys-CysArg-Gly-Arg-Gly-Cys-Ile-Cys-Ser-Ile-MetGly-Thr-Asn-Cys-Glu-Cys-Lys-Pro-Arg-LeuIle-Met-Glu-Gly-Leu-Gly-Leu-Ala

Vial

0.1 mg30,000(Disulfide bonds between Cys4-Cys20, Cys12-Cys25, Cys19-Cys36, and Cys27-Cys34)(M.W. 5202.2)

P-type Ca

2+

C217H360N68O60S10Channel Selective Blocker

1) I.M. Mintz, V.J. Venema, K.M. Swiderek, T.D. Lee, B.P. Bean, and M.E. Adams, Nature, 355, 827 (1992). (Original)
2) T.J. Turner, M.E. Adams, and K. Dunlap, Science, 258, 310 (1992). (Pharmacol.)3) H. Nishio, K.Y. Kumagaye, S. Kubo, Y.-N. Chen, A. Momiyama, T. Takahashi, T. Kimura, and S. Sakakibara,
Biochem. Biophys. Res. Commun., 196, 1447 (1993). (Chem. Synthesis & Biological Activity)• This compound is distributed through Peptide Institute, Inc. The customers in the U.S.A. may order this compound
through Peptides International, Inc. under their license agreement with the University of Utah.

–6 –ω-Agatoxins (continued)
4294-sω-Agatoxin TK
ω-Aga-TK
ω-Aga-IVB(Funnel Web Spider, Agelenopsis aperta)
Glu-Asp-Asn-Cys-Ile-Ala-Glu-Asp-Tyr-GlyLys-Cys-Thr-Trp-Gly-Gly-Thr-Lys-Cys-CysArg-Gly-Arg-Pro-Cys-Arg-Cys-Ser-Met-IleGly-Thr-Asn-Cys-Glu-Cys-Thr-Pro-Arg-LeuIle-Met-Glu-Gly-Leu-D-Ser-Phe-Ala-20

Price:Yen
Vial

0.1 mg30,000(Reported disulfide bonds between Cys4-Cys20, Cys12-Cys25, Cys19-Cys36, and Cys27-Cys34)(M.W. 5273.0)

C215H337N65O70S10 [145017-83-0]
Purity Information : QE See page IV (XVI)

P-type Ca2+ Channel Blocker
1) M. Kuwada, T. Teramoto, K.Y. Kumagaye, K. Nakajima, T. Watanabe, T. Kawai, Y. Kawakami, T. Niidome,
K. Sawada, Y. Nishizawa, and K. Katayama, Mol. Pharmacol., 46, 587 (1994). (Original; ω-Aga-TK)
2) Y. Shikata, T. Watanabe, T. Teramoto, A. Inoue, Y. Kawakami, Y. Nishizawa, K. Katayama, and M. Kuwada,
J. Biol. Chem., 270, 16719 (1995). (L-Ser to D-Ser Isomerase)3) M.E. Adams, I.M. Mintz, M.D. Reily, V. Thanabal, and B.P. Bean, Mol. Pharmacol., 38, 681 (1990).
(Original; ω-Aga-IVB)
4) S.D. Heck, P.R. Kelbaugh, M.E. Kelly, P.F. Thadeio, N.A. Saccomano, J.G Stroh. and R.A. Volkmann,
J. Am. Chem. Soc., 116, 10426 (1994). (S-S Bond; ω-Aga-IVB)
5) T. Teramoto, T. Niidome, M. Kimura, M. Ohgoh, Y. Nishizawa, K. Katayama, T. Mayumi, and K. Sawada, Brain Res.,
756, 225 (1997). (Pharmacol.)6) S.P. Lieske and J.-M. Ramirez, J. Neurophysiol., 95, 1323 (2006). (Pharmacol.)• This product is distributed under the license of Eisai Co., Ltd. Its use for any purpose other than research is strictly
prohibited.

3402-sNew

Biotinyl-ω-Agatoxin IVA
Biotinyl-ω-Aga-IVA-20

(Trifluoroacetate Form)

Vial

0.1 mg35,000

Biotinyl-Lys-Lys-Lys-Cys-Ile-Ala-Lys-Asp-Tyr-GlyArg-Cys-Lys-Trp-Gly-Gly-Thr-Pro-Cys-CysArg-Gly-Arg-Gly-Cys-Ile-Cys-Ser-Ile-MetGly-Thr-Asn-Cys-Glu-Cys-Lys-Pro-Arg-LeuIle-Met-Glu-Gly-Leu-Gly-Leu-Ala(Disulfide bonds between Cys4-Cys20, Cys12-Cys25, Cys19-Cys36 and Cys27-Cys34)(M.W. 5428.5)

C227H374N70O62S11

Reagent for Localization Study of ω -Agatoxin IVA Binding Site
1) H. Nishio, K. Y. Kumagaye, S. Kubo, Y.-N. Chen, A. Momiyama, T. Takahashi, T. Kimura, and S. Sakakibara,
Biochem. Biophys. Res. Commun., 196, 1447 (1993). (Chem. Synthesis & Biological Activity)
2) S. Nakanishi, A. Fujii, T. Kimura, S. Sakakibara, and K. Mikoshiba, J. Neurosci. Res., 41, 532 (1995).
(Biochem.: Distribution of Binding Sites)–7 –and Proteins

CompoundBiologically Active Peptides

CodeAgelenin
Code

Compound4247-sAgelenin(Spider, Agelena opulenta)
Gly-Gly-Cys-Leu-Pro-His-Asn-Arg-Phe-CysAsn-Ala-Leu-Ser-Gly-Pro-Arg-Cys-Cys-SerGly-Leu-Lys-Cys-Lys-Glu-Leu-Ser-Ile-TrpAsp-Ser-Arg-Cys-Leu-NH2-20

Price:Yen
Vial

0.1 mg30,000(Disulfide bonds between Cys3-Cys19, Cys10-Cys24, and Cys18-Cys34)(M.W. 3818.4)

C160H254N52O45S6

Presynaptic Ca2+ Channel Antagonist
1) K. Hagiwara, T. Sakai, A. Miwa, N. Kawai, and T. Nakajima, Biomed. Res., 11, 181 (1990). (Original)
2) T. Inui, K. Hagiwara, K. Nakajima, T. Kimura, T. Nakajima, and S. Sakakibara, Pept. Res., 5, 140 (1992).
(Chem. Synthesis, S-S Bond & Amide)3) N. Yamaji, K. Sugase, T. Nakajima, T. Miki, M. Wakamori, Y. Mori, and T. Iwashita, FEBS Lett., 581, 3789 (2007).
(Solution Structure)

Agouti-Related Protein
4366-s-20

Agouti-Related Protein (Human, 86-132)
AGRP (Human, 86-132)
Arg-Cys-Val-Arg-Leu-His-Glu-Ser-Cys-LeuGly-Gln-Gln-Val-Pro-Cys-Cys-Asp-Pro-CysAla-Thr-Cys-Tyr-Cys-Arg-Phe-Phe-Asn-AlaPhe-Cys-Tyr-Cys-Arg-Lys-Leu-Gly-Thr-AlaMet-Asn-Pro-Cys-Ser-Arg-Thr

Vial

0.1 mg30,000(Reported disulfide bonds between Cys87-Cys102, Cys94-Cys108, Cys101-Cys119, Cys105-Cys129, and Cys110-Cys117)(M.W. 5347.2)

C223H339N69O63S11

Melanocortin Receptor-3 / 4 Antagonist, Appetite Boosting Peptide
A gene encoding agouti-related protein (AGRP) was isolated in 1997 during a search of the proteins related
to agouti protein which was known to affect pigmentation through the melanocortin receptor 1 (MC-1). AGRP
shows some sequence similarity to agouti protein, including the distribution of the 10 cysteine residues in the
C-terminal domain. However, AGRP and agouti protein bind to distinct types of melanocortin receptors. The
receptors for AGRP are reported to be MC-3 and MC-4, which are known to participate in the regulation of
feeding, whereby the binding of an antagonist like AGRP stimulates food intake. Some groups have attempted to
identify the active domain of a 132 amino acid precursor protein, one of which is AGRP(86-132)1). IC50 valuesof this peptide in the competitive binding assay for MC-3 and MC-4, expressed in human embryonic kidneycells, were 2 nM and 19 nM, respectively. Competitive inhibition of α-MSH-stimulated cAMP production was
also detected for MC-3 and MC-4, but not for MC-1 and MC-5, indicating the selective nature of the action ofAGRP(86-132) with respect to melanocortin receptors.
1) R.D. Rosenfeld, L. Zeni, A.A. Welcher, L.O. Narhi, C. Hale, J. Marasco, J. Delaney, T. Gleason, J.S. Philo, V. Katta,
J. Hui, J. Baumgartner, M. Graham, K.L. Stark, and W. Karbon, Biochemistry, 37, 16041 (1998). (Original)
2) E.J. Bures, J.O. Hui, Y. Young, D.T. Chow, V. Katta, M.F. Rohde, L. Zeni, R.D. Rosenfeld, K.L. Stark, and M. Haniu,
Biochemistry, 37, 12172 (1998). (Structure; S-S Bond)
3) J.R. Shutter, M. Graham, A.C. Kinsey, S. Scully, R. Lu
thy, and K.L. Stark, Genes Dev., 11, 593 (1997).
(Agouti-Related Transcript Sequence)4) D.M. Dinulescu and R.D. Cone, J. Biol. Chem., 275, 6695 (2000). (Review)5) A.M. Wilczynski, C.G. Joseph, and C. Haskell-Luevano, Med. Res. Rev., 25, 545 (2005). (Review)6) O. Ilnytska and G. Argyropoulos, Cell. Mol. Life Sci., 65, 2721 (2008). (Review)

Ala-Arg-Gly-Ile-Lys-Gly-Ile-Arg-Gly-Phe-Ser-Gly [Lysine Hydroxylase Substrate L-1] See Code 4166 on page 208–8 –Alarin4449-sAlarin (Human)
Ala-Pro-Ala-His-Arg-Ser-Ser-Thr-Phe-ProLys-Trp-Val-Thr-Lys-Thr-Glu-Arg-Gly-ArgGln-Pro-Leu-Arg-Ser-20

(M.W. 2894.3)

Price:Yen

C127H205N43O35

Vial

0.1 mg10,000[909409-86-5]

Splice Variant of Galanin-Like Peptide
Human galanin [Code 4245-v] and galanin-like peptide (GALP) [Code 4391-s], are members of the galanin
peptide family. Galanin (1-13) is identical to (9-21) of GALP, so it is not surprising that both peptides interact
with galanin receptors 1-3 with some subtype specificity1).

GWTLNSAGYLLGPHAVGNHRSFSDKNGLTS
Galanin:
APAHRGRGGWTLNSAGYLLGPVLHLPQMGDQDGKRETALEILDLWKAIDGLPYSHPPQPSGALP:APAHRSSTFPKWVTKTERGRQPLRSAlarin:GALP is a 60 amino acid residue peptide, which is encoded by its gene comprised of 6 exons. In 2007, a
splicing variant of GALP was identified in human neuroblastic tumors2) and later in mouse. The identified
peptide, termed "alarin", is based on the amino-terminal Ala and the carboxyl-terminal Ser residues in the
primary structure, which comprises 25 amino acid residues3). Primary structure of alarin (1-5) is the same asthat of GALP (1-5) (encoded by exon 2), which follows the 20 amino acid residue peptide from exon 4, thus,
exon 3 is excluded from the alarin transcript.
Alarin immunoreactivity is detected in pericytes and venules in human dermis, but not in endothelial cells ofblood vessels. Alarin is reported to inhibit inflammatory edema induced by substance P and CGRP at doses in
the picomolar range in mouse, which is a characteristic feature also observed in galanin and GALP. The
mechanism of alarin-eliciting inhibitory activity is considered to be decreased in cutaneous blood flow because
alarin did not affect microvascular permeability or vasoconstricting activity of endothelin-1. Alarin fails tointeract with galanin receptors, as expected, since the alarin transcript lacks the GALP (9-21)-encoding exon 3,
suggesting that a specific receptor for alarin may exist in the body.
In conjunction with galanin and GALP, alarin might be an essential tool for vascular systems research.
* Note: In the literature3), the carboxyl-terminal structure of alarin is not definitely described, therefore, we
synthesize the 25 amino acid residue peptide with the free- carboxyl-terminus based on the reported
sequence in the GenBank database (DQ155644) and distribute it as alarin.
1) R. Lang, A.L. Gundlach, and B. Kofler, Pharmacol. Ther., 115, 177 (2007). (Review)2) R. Santic, K. Fenninger, K. Graf, R. Schneider, C. Hauser-Kronberger, F.H. Schilling, P. Kogner, M. Ratschek,
N. Jones, W. Sperl, and B. Kofler, J. Mol. Neurosci., 29, 145 (2006). (Original)
3) R. Santic, S.M. Schmidhuber, R. Lang, I. Rauch, E. Voglas, N. Eberhard, J.W. Bauer, S.D. Brain, and B. Kofler,
Proc. Natl. Acad. Sci. U.S.A., 104, 10217 (2007). (Original.)–9 –and Proteins

CompoundBiologically Active Peptides

CodeAmylins
1) G.J.S. Cooper, Endocrinol. Rev., 15, 163 (1994). (Review)2) J.W.M. Hoppener, B. Ahrén, and C.J.M. Lips, N. Engl. J. Med., 343, 411 (2000). (Review)3) S.A. Jayasinghe and R. Langen, Biochim. Biophys. Acta, 1768, 2002 (2007). (Review)4) L. Haataja, T. Gurlo, C.J. Huang, and P.C. Butler, Endocr. Rev., 29, 303 (2008). (Review)

Code

Compound4219-v

Amylin (Human)
IAPP (Islet Amyloid Polypeptide)
DAP (Diabetes-Associated Peptide)-20

Price:Yen
Vial

0.5 mg41,000(Trifluoroacetate Form)

Lys-Cys-Asn-Thr-Ala-Thr-Cys-Ala-Thr-GlnArg-Leu-Ala-Asn-Phe-Leu-Val-His-Ser-SerAsn-Asn-Phe-Gly-Ala-Ile-Leu-Ser-Ser-ThrAsn-Val-Gly-Ser-Asn-Thr-Tyr-NH2(Disulfide bond between Cys2-Cys7)(M.W. 3903.3)

C165H261N51O55S2[122384-88-7]

Purity Information : Qx See page IV (XVI)
1) P. Westermark, C. Wernstedt, E. Wilander, D.W. Hayden, T.D. O'Brien, and K.H. Johnson, Proc. Natl. Acad. Sci.
U.S.A., 84, 3881 (1987). (Original; 36th A.A. Unknown)
2) G.J.S. Cooper, A.C. Willis, A. Clark, R.C. Turner, R.B. Sim, and K.B.M. Reid, Proc. Natl. Acad. Sci. U.S.A.,84, 8628 (1987). (Original; Complete Sequence)3) A. Clark, G.J.S. Cooper, C.E. Lewis, J.F. Morris, A.C. Willis, K.B.M. Reid, and R.C. Turner, Lancet, 2, 231 (1987).
(Pharmacol; May be Pathogenic)

4220-v-20

Amylin (Rat)
IAPP (Islet Amyloid Polypeptide)
DAP (Diabetes-Associated Peptide)
Lys-Cys-Asn-Thr-Ala-Thr-Cys-Ala-Thr-GlnArg-Leu-Ala-Asn-Phe-Leu-Val-Arg-Ser-SerAsn-Asn-Leu-Gly-Pro-Val-Leu-Pro-Pro-ThrAsn-Val-Gly-Ser-Asn-Thr-Tyr-NH2

Vial

0.5 mg38,000(Disulfide bond between Cys2-Cys7)(M.W. 3920.4)

C167H272N52O53S2[124447-81-0]

1) J.D. Leffert, C.B. Newgard, H. Okamoto, J.L. Milburn, and K.L. Luskey, Proc. Natl. Acad. Sci. U.S.A., 86, 3127
(1989). (Original; cDNA)
2) J. Asai, M. Nakazato, K. Kangawa, S. Matsukura, and H. Matsuo, Biochem. Biophys. Res. Commun., 164, 400 (1989).
(Original; Isolation & Structure)– 10 –

Amyloid β-Protein and Related Peptides
CompoundQuantity

Price: Yen

Page

4307-v
4379-v
4349-v
4370-v
4359-v
4309-v
4367-v
4358-v

0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
5 mg vial

18,00020,00030,00035,00010,0004,000
30,00016,000

12
12
13
13
13
13
14
14

0.1 mg vial
0.1 mg vial

9,000
18,000

14
14

Lys-Thr-Glu-Glu-Ile-Ser-Glu-Val-Asn-Sta-Val-Ala-Glu-Phe

1 mg vial

20,000196

MOCAc-Ser-Glu-Val-Asn-Leu-Asp-Ala-Glu-Phe-ArgLys(Dnp)-Arg-Arg-NH2

1 mg vial

15,000221

1 mg vial
5 mg vial

30,00010,000194
187

1 mg vial

15,000222

50 µl vial
50 µl vial
50 µl vial
50 µl vial
50 µl vial

25,00025,00025,00025,00025,000

262
262
262
263
263

Amyloid β-Protein (Human, 1-40)
Amyloid β-Protein (Human, 1-40) [HCl Form]
Amyloid β-Protein (Human, 1-42)
Amyloid β-Protein (Human, 1-43)
Amyloid β-Protein (Human, 1-16)
Amyloid β-Protein (Human, 25-35)[Pyr3]-Amyloid β-Protein (Human, 3-42)β-Sheet Breaker Peptide iAβ5Amyloid β-Protein Control Peptides
4413-s
4420-sAmyloid β-Protein (40-1)
Amyloid β-Protein (42-1)

β-Secretase Inhibitor
4378-vβ-Secretase Substrate
3212-vγ-Secretase Inhibitors
4394-v
L-685,458(3,5-Difluorophenylacetyl)-Ala-Phg-OBut (DAPT)
3219-vγ-Secretase Substrate
3217-v
Nma-Gly-Gly-Val-Val-Ile-Ala-Thr-Val-Lys(Dnp)D-Arg- D-Arg- D-Arg-NH2
Antisera
14359-v
14307-v
14356-v
14357-v
14414-v

Amyloid β-Protein (Human, 1-16) Antiserum
Amyloid β-Protein (Human, 1-40) Antiserum
Amyloid β-Protein (Human, 34-40) Antiserum
Amyloid β-Protein (Human, 37-42) Antiserum
Amyloid β-Protein (Human, 37-43) Antiserum– 11 –and Proteins

Code

Amyloid β-Protein Fragments

Biologically Active Peptides

List of Products for Alzheimer's Disease Research

Amyloid β-Protein and Related Peptides (continued)
1) A. Rauk, Chem. Soc. Rev., 38, 2698 (2009). (Review)

Code

CompoundPrice:Yen

4307-v

Amyloid β-Protein (Human, 1-40)-20

(Trifluoroacetate Form)

Vial

0.5 mg18,000

Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-TyrGlu-Val-His-His-Gln-Lys-Leu-Val-Phe-PheAla-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-AlaIle-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val(M.W. 4329.8) C194H295N53O58S [131438-79-4]
Purity Information: Q Z See page IV (XVI)

Peptide Deposited in the Brain of Alzheimer's Disease Patient
1) B.A. Yankner, L.K. Duffy, and D.A. Kirschner, Science, 250, 279 (1990). (Original)

4379-v

Amyloid β-Protein (Human, 1-40) [HCI Form]-20

Lyophilized from Dilute HCl Solution

Vial

0.5 mg20,000

Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-TyrGlu-Val-His-His-Gln-Lys-Leu-Val-Phe-PheAla-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-AlaIle-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val(M.W. 4329.8) C194H295N53O58S [131438-79-4]
Purity Information: Q Z See page IV (XVI)Specific Form Easily Convertible to β -Structure1) I. Kaneko, N. Yamada, Y. Sakuraba, M. Kamenosono, and S. Tutumi, J. Neurochem., 65, 2585 (1995). (Original)
2) I. Kaneko and S. Tutumi, J. Neurochem., 68, 438 (1997). (Facile β -Structure Formation)

Bulk material of our "Amyloid β-Protein (Human, 1-40)" is synthesized in trifluoroacetate form. Vials of this
peptide (Code 4307-v and Code 4379-v), described as "Trifluoroacetate Form" and "HCI Form" are thenprepared by lyophilization from DMSO and dilute HCI solution, respectively. Characteristic features of these
peptides, which are analyzed by CD in aqueous buffer at pH 7.4 and 37 (peptide concentration = 10 µM), areshown below in italics:
     






    

  

!#&$%

!"#$%




              

        
   

– 12 –

Amyloid β-Protein and Related Peptides (continued)
Price:Yen

4349-v

Amyloid β-Protein (Human, 1-42)-20

(Trifluoroacetate Form)

Vial

0.5 mg30,000

Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-TyrGlu-Val-His-His-Gln-Lys-Leu-Val-Phe-PheAla-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-AlaIle-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-ValIle-Ala(M.W. 4514.0) C203H311N55O60S [107761-42-2]
Purity Information: Q Z See page IV (XVI)

Major Plaque Component in Alzheimer's Disease
1) D. Goldgaber, M.I. Lerman, O.W. McBride, U. Saffiotti, and D.C. Gajdusek, Science, 235, 877 (1987).
(Original; cDNA)
2) A.E. Roher, J.D. Lowenson, S. Clarke, A.S. Woods, R.J. Cotter, E. Gowing, and M.J. Ball, Proc. Natl. Acad. Sci. U.S.A.,
90, 10836 (1993). (Pathophysiology)3) N. Suzuki, T.T. Cheung, X.-D. Cai, A. Okada, L. Otvos, Jr., C. Eckman, T.E. Golde, and S.G. Younkin,
Science, 264, 1336 (1994). (Pathophysiology)4) M. Citron, T.S. Diehl, G. Gordon, A.L. Biere, P. Seubert, and D.J. Selkoe, Proc. Natl. Acad. Sci. U.S.A.,
93, 13170 (1996). (Biosynthesis)

4370-v

Amyloid β-Protein (Human, 1-43)-20

(Trifluoroacetate Form)

Vial

0.5 mg35,000

Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-TyrGlu-Val-His-His-Gln-Lys-Leu-Val-Phe-PheAla-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-AlaIle-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-ValIle-Ala-Thr(M.W. 4615.1)

C207H318N56O62S[134500-80-4]

Purity Information: Q Z See page IV (XVI)
1) A. Tamaoka, T. Kondo, A. Odaka, N. Sahara, N. Sawamura, K. Ozawa, N. Suzuki, S. Shoji, and H. Mori,
Biochem. Biophys. Res. Commun., 205, 834 (1994). (Pharmacol.)2) K. Hsiao, P. Chapman, S. Nilsen, C. Eckman, Y. Harigaya, S. Younkin, F. Yang, and G. Cole, Science, 274, 99 (1996).
(Pharmacol.)3) K. Duff, C. Eckman, C. Zehr, X. Yu, C.-M. Prada, J. Perez-tur, M. Hutton, L. Buee, Y. Harigaya, D. Yager, D. Morgan,
M.N. Gordon, L. Holcomb, L. Refolo, B. Zenk, J. Hardy, and S. Younkin, Nature, 383, 710 (1996). (Pharmacol.)4) T. Kawarabayashi, Y. Igeta, M. Sato, A. Sasaki, E. Matsubara, M. Kanai, Y. Tomidokoro, K. Ishiguro, K. Okamoto,
S. Hirai, and M. Shoji, Brain Res., 765, 343 (1997). (Pharmacol.)4359-v-20

Amyloid β-Protein (Human, 1-16)
Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-TyrGlu-Val-His-His-Gln-Lys(M.W. 1955.0)

C84H119N27O28

Vial

0.5 mg10,000[131580-10-4]

Blocker for Plaque-Induced Microgliosis / Reducer for Brain Inflammation
1) D. Giulian, L.J. Haverkamp, J. Yu, W. Karshin, D. Tom, J. Li, A. Kazanskaia, J. Kirkpatrick, and A.E. Roher,
J. Biol. Chem., 273, 29719 (1998). (Original; Pharmacol.)2) M. Nakamura, N. Shishido, A. Nunomura, M.A. Smith, G. Perry, Y. Hayashi, K. Nakayama, and T. Hayashi,
Biochemistry, 46, 12737 (2007). (Pharmacol.)4309-v

Amyloid β-Protein (Human, 25-35)-20

(Trifluoroacetate Form)

Vial

0.5 mg4,000

Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-LeuMet(M.W. 1060.3)

C45H81N13O14S[131602-53-4]

Neurotrophic / Neurodegenerative Peptide
1) B.A. Yankner, L.K. Duffy, and D.A. Kirschner, Science, 250, 279 (1990). (Original)
2) L. Meda, M.A. Cassatella, G.I. Szendrei, L. Otvos, Jr., P. Baron, M. Villalba, D. Ferrari, and F. Rossi, Nature,374, 647 (1995). (Pharmacol.)3) L. Millucci, L. Ghezzi, G. Bernardini, and A. Santucci, Curr. Protein Pept. Sci., 11, 54 (2010). (Review)– 13 –and Proteins

CompoundBiologically Active Peptides

CodeAmyloid β-Protein and Related Peptides (continued)
Code

CompoundPrice:Yen

4367-v[Pyr3]-Amyloid β-Protein (Human, 3-42)-20

(Trifluoroacetate Form)

Vial

0.5 mg30,000

Pyr-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-ValHis-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-GluAsp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-IleGly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala(M.W. 4309.9)

C196H299N53O55S [183449-57-2]
Purity Information: QZ See page IV (XVI)

Major Neuritic Plaque Component in Alzheimer's Disease
1) T.C. Saido, T. Iwatsubo, D.M.A. Mann, H. Shimada, Y. Ihara, and S. Kawashima, Neuron, 14, 457 (1995).
(Pharmacol.; Dominant Deposition in Senile Plaques)
2) T. Iwatsubo, T.C. Saido, D.M.A. Mann, V.M.-Y. Lee, and J.Q. Trojanowski, Am. J. Pathol., 149, 1823 (1996).
(Histochem.; Distribution in Brains of Patients)
3) Y.-M. Kuo, M.R. Emmerling, A.S. Woods, R.J. Cotter, and A.E. Roher, Biochem. Biophys. Res. Commun.,
237, 188 (1997). (Pharmacol.; Form in Neuritic Plaques and Vascular Amyloid Deposits)

4413-s-20

Amyloid β-Protein (40-1)Vial
0.1 mgPeptide with Reversed Sequence of Amyloid β-Protein (Human, 1-40)

9,000(Trifluoroacetate Form)

Val-Val-Gly-Gly-Val-Met-Leu-Gly-Ile-IleAla-Gly-Lys-Asn-Ser-Gly-Val-Asp-Glu-AlaPhe-Phe-Val-Leu-Lys-Gln-His-His-Val-GluTyr-Gly-Ser-Asp-His-Arg-Phe-Glu-Ala-Asp(M.W. 4329.8)

C194H295N53O58S [144409-99-4]
Purity Information : QZ See page IV (XVI)

Control Peptide for Amyloid β -Protein (Human, 1-40)
4420-s-20

Amyloid β-Protein (42-1)Vial
0.1 mgPeptide with Reversed Sequence of Amyloid β-Protein (Human, 1-42)

18,000(Trifluoroacetate Form)

Ala-Ile-Val-Val-Gly-Gly-Val-Met-Leu-GlyIle-Ile-Ala-Gly-Lys-Asn-Ser-Gly-Val-AspGlu-Ala-Phe-Phe-Val-Leu-Lys-Gln-His-HisVal-Glu-Tyr-Gly-Ser-Asp-His-Arg-Phe-GluAla-Asp(M.W. 4514.0)

C203H311N55O60S [317366-82-8]
Purity Information : QZ See page IV (XVI)

Control Peptide for Amyloid β -Protein (Human, 1-42)
4358-v-20

β-Sheet Breaker Peptide iAβ5
Leu-Pro-Phe-Phe-Asp(M.W. 637.72)

C33H43N5O8

Vial

5 mg

16,000[182912-74-9]

Inhibitor of Amyloid Deposition
1) C. Soto, E.M. Sigurdsson, L. Morelli, R.A. Kumar, E.M. Castano, and B. Frangione, Nat. Med., 4, 822 (1998).
(Original; Pharmacol.)– 14 –

Angiotensin and Related Peptides
Berlin, 1974. (Review)

List of Angiotensin and Related Peptides
Code

CompoundQuantity

Price: Yen

Page

4007-v
4069-v
4001-v
4034-v
4036-v
4028-v
4296-v
4439-v

Angiotensin I (Human)★
[Val5]-Angiotensin I (Bovine)★
Angiotensin II (Human)★
[Val5]-Angiotensin II★
[Asn1,Val5]-Angiotensin II★
Angiotensin III (Human)★
CGP 42112
Proangiotensin-12 (Rat)

0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial

2,900
3,200
2,700
2,800
2,800
2,700
5,000
4,000

below
16
below
17
16
below
18
18

4035-v
4016-v
4102-v
4071-v
4037-v[Sar1,Ala8]-Angiotensin II★
[Sar1,Ile8]-Angiotensin II★
[Sar1,Thr8]-Angiotensin II★
[Sar1,Val5,Ala8]-Angiotensin II★
Des-Asp1-[Ile8]-Angiotensin II★

0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial

2,800
2,700
2,900
2,900
2,700

17
17
17
17
18

4331-v
4332-v

Angiotensin IV (Human)★
Angiotensin (Human, 1-7)★

0.5 mg vial
0.5 mg vial

2,700
2,700

16
16

AgonistAntagonist

Ligand★

Other bulk packaging is available.

Code

Compound4007-v

Angiotensin I (Human)*(Porcine, Canine, Rat, Mouse, Rabbit, Guinea pig)
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu

-20

Vial

0.5 mg2,900

Angiotensin I (Human)*(Porcine, Canine, Rat, Mouse, Rabbit, Guinea pig)
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu • 2AcOH • 4H2O

Bulk

25 mg
100 mg39,000104,000(M.W. 1296.5 • 120.10 • 72.06)[70937-97-2](M.W. 1296.5)

4007
-20

Price:Yen

C62H89N17O14[484-42-4]

C62H89N17O14 • 2CH3COOH • 4H2O

1) K. Arakawa, M. Nakatani, A. Minohara, and M. Nakamura, Biochem. J., 104, 900 (1967). (Original; Human)
2) T. Nakayama, T. Nakajima, and H. Sokabe, Chem. Pharm. Bull., 20, 1579 (1972). (Original; Rat)
3) H. Akagi, T. Hayashi, T. Nakayama, T. Nakajima, T.X. Watanabe, and H. Sokabe, Chem. Pharm. Bull., 30, 2498
(1982). (Original; Porcine etc.)
4) W.M. Clouston, B.A. Evans, J. Haralambidis, and R.I. Richards, Genomics, 2, 240 (1988). (Original; Mouse-cDNA)

4001-v-20

Angiotensin II (Human)*
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe(M.W. 1046.2)

4001
-20

C50H71N13O12

Vial

0.5 mg

2,700

Bulk

25 mg
100 mg38,000100,000[4474-91-3]

Angiotensin II (Human)*
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe • AcOH • 4H2O
(M.W. 1046.2 • 60.05 • 72.06)

C50H71N13O12 • CH3COOH • 4H2O
1) K. Arakawa, M. Nakatani, A. Minohara, and M. Nakamura, Biochem. J., 104, 900 (1967). (Original)

4028-v-20

Angiotensin III (Human)*
Arg-Val-Tyr-Ile-His-Pro-Phe(M.W. 931.09)

4028
-20

C46H66N12O9

Vial

0.5 mg

2,700

Bulk

25 mg
100 mg30,00080,000[13602-53-4]

Angiotensin III (Human)*
Arg-Val-Tyr-Ile-His-Pro-Phe • 2AcOH • 4H2O
(M.W. 931.09 • 120.10 • 72.06)

C46H66N12O9 • 2CH3COOH • 4H2O [100900-06-9]1) W.B. Campbell, S.N. Brooks, and W.A. Pettinger, Science, 184, 994 (1974). (Original)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 15 –and Proteins2) M.J. Peach, Physiol. Rev., 57, 313 (1977). (Review)

Biologically Active Peptides1) I.H. Page and F.M. Bumpus (eds.), Angiotensin, Handbook of Experimental Pharmacology, Vol. 37, Springer-Verlag,

Angiotensin and Related Peptides (continued)
Code

Compound4331-v

Angiotensin IV (Human)*
Angiotensin (Human, 3-8)
Val-Tyr-Ile-His-Pro-Phe-20

(M.W. 774.91)

4331
-20

Price:Yen

C40H54N8O8

Vial

0.5 mg

2,700

Bulk

25 mg

30,000[23025-68-5]

Angiotensin IV (Human)*
Angiotensin (Human, 3-8)
Val-Tyr-Ile-His-Pro-Phe • 1/ 2 AcOH • 3H2O
(M.W. 774.91 • 30.03 • 54.05)

C40H54N8O8 • 1/2 CH3COOH • 3H2O

1) R.L. Haberl, P.J. Decker, and K.M. Einhaupl, Circ. Res., 68, 1621 (1991). (Biological Activity)
2) J.W. Harding, V.I. Cook, A.V. Miller-Wing, J.M. Hanesworth, M.F. Sardinia, K.L. Hall, J.W. Stobb, G.N. Swanson,
J.K.M. Coleman, J.W. Wright, and E.C. Harding, Brain Res., 583, 340 (1992). (Specific Binding Site in Brain)
3) J.M. Hanesworth, M.F. Sardinia, L.T. Krebs, K.L. Hall, and J.W. Harding, J. Pharmacol. Exp. Ther., 266, 1036 (1993).
(Specific Binding Site in Heart)4) M. de Gasparo, A. Husain, W. Alexander, K.J. Catt, A.T. Chiu, M. Drew, T. Goodfriend, J.W. Harding, T. Inagami,
and P.B.M.W.M. Timmermans, Hypertension, 25, 924 (1995). (AT4 Receptor; Non AT1/2 Recognition,
Nomenclature)4069-v-20

[Val5]-Angiotensin I (Bovine)*
Asp-Arg-Val-Tyr-Val-His-Pro-Phe-His-Leu(M.W. 1282.4)

4069
-20

C61H87N17O14

0.5 mg

3,200

Bulk

25 mg

50,000[484-43-5][Val5]-Angiotensin I (Bovine)*
Asp-Arg-Val-Tyr-Val-His-Pro-Phe-His-Leu • AcOH • 5H2O
(M.W. 1282.4 • 60.05 • 90.08)

Vial

C61H87N17O14 • CH3COOH • 5H2O

1) D.F. Elliott and W.S. Peart, Biochem. J., 65, 246 (1957). (Original; Heterogenous Renin)
2) H. Akagi, T. Hayashi, T. Nakayama, T. Nakajima, T.X. Watanabe, and H. Sokabe, Chem. Pharm. Bull.,30, 2498 (1982). (Original; Homologous Renin)
3) M. Takai, Y. Kurano, T. Kimura, and S. Sakakibara, Peptide Chemistry 1979, 187 (1980). (Chem. Synthesis)4036-v-20

[Asn1,Val5]-Angiotensin II*
Asn-Arg-Val-Tyr-Val-His-Pro-Phe(M.W. 1031.2)

4036
-20

C49H70N14O11

4332-v
-20

4332
-20

C41H62N12O11

Bulk

25 mg

41,000Vial

0.5 mg

2,700

Bulk

25 mg

30,000[51833-78-4]

Angiotensin (Human, 1-7)*(Canine, Rat)
Asp-Arg-Val-Tyr-Ile-His-Pro • AcOH • 4H2O
(M.W. 899.00 • 60.05 • 72.06)

2,800

C49H70N14O11 • CH3COOH • 4H2O

Angiotensin (Human, 1-7)*(Canine, Rat)
Asp-Arg-Val-Tyr-Ile-His-Pro(M.W. 899.00)

0.5 mg[53-73-6][Asn1,Val5]-Angiotensin II*
Asn-Arg-Val-Tyr-Val-His-Pro-Phe • AcOH • 4H2O
(M.W. 1031.2 • 60.05 • 72.06)

Vial

C41H62N12O11 • CH3COOH • 4H2O

1) M.T. Schiavone, R.A.S. Santos, K.B. Brosnihan, M.C. Khosla, and C.M. Ferrario, Proc. Natl. Acad. Sci. U.S.A.,
85, 4095 (1988). (Original)
2) C.M. Ferrario, K.B. Brosnihan, D.I. Diz, N. Jaiswal, M.C. Khosla, A. Milsted, and E.A. Tallant, Hypertension,
18 (Suppl. III), III-126 (1991). (Review)3) R.A.S. Santos, K.B. Brosnihan, D.W. Jacobsen, P.E. DiCorleto, and C.M. Ferrario, Hypertension,
19 (Suppl. II), II-56 (1992). (Metabolic Pathway)
4) A. DelliPizzi, S.D. Hilchey, and C.P. Bell-Quilley, Br. J. Pharmacol., 111, 1 (1994). (Pharmacol.)*The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 16 –

Angiotensin and Related Peptides (continued)
4035-v[Sar1,Ala8]-Angiotensin II
Sar-Arg-Val-Tyr-Ile-His-Pro-Ala-20

(M.W. 926.07)

4035
-20

Price:Yen

C43H67N13O10

0.5 mg

2,800

Bulk

25 mg
100 mg34,00096,000[38027-95-1][Sar1,Ala8]-Angiotensin II
Sar-Arg-Val-Tyr-Ile-His-Pro-Ala • AcOH • 4H2O
(M.W. 926.07 • 60.05 • 72.06)

Vial

C43H67N13O10 • CH3COOH • 4H2O

Angiotensin II Selective Antagonist
1) D.T. Pals, F.D. Masucci, G.S. Denning, Jr., F. Sipos, and D.C. Fessler, Circ. Res., 29, 673 (1971). (Original)
2) F.M. Bumpus, S. Sen, R.R. Smeby, C. Sweet, C.M. Ferrario, and M.C. Khosla, Circ. Res., 32 and 33 (Suppl.I), I-150(1973). (Pharmacol.)4016-v-20

[Sar1,Ile8]-Angiotensin II
Sar-Arg-Val-Tyr-Ile-His-Pro-Ile(M.W. 968.15)

4016
-20

C46H73N13O10

0.5 mg

2,700

Bulk

25 mg
100 mg34,00096,000[37827-06-8][Sar1,Ile8]-Angiotensin II
Sar-Arg-Val-Tyr-Ile-His-Pro-Ile • AcOH • 4H2O
(M.W. 968.15 • 60.05 • 72.06)

Vial

C46H73N13O10 • CH3COOH • 4H2O

Angiotensin II Selective Antagonist
1) R.K. Tu
rker, M.M. Hall, M. Yamamoto, C.S. Sweet,and F.M. Bumpus, Science, 177, 1203 (1972). (Original)
2) F.M. Bumpus, S. Sen, R.R. Smeby, C. Sweet, C.M. Ferrario, and M.C. Khosla, Circ. Res., 32 and 33 (Suppl.I), I-150(1973). (Pharmacol.)4102-v-20

[Sar1,Thr8]-Angiotensin II
Sar-Arg-Val-Tyr-Ile-His-Pro-Thr(M.W. 956.10)

4102
-20

C44H69N13O11

0.5 mg

2,900

Bulk

25 mg

41,000[53632-49-8][Sar1,Thr8]-Angiotensin II
Sar-Arg-Val-Tyr-Ile-His-Pro-Thr • 2AcOH • 4H2O
(M.W. 956.10 • 120.10 • 72.06)

Vial

C44H69N13O11 • 2CH3COOH • 4H2O

Angiotensin II Selective Antagonist
1) M.C. Khosla, M.M. Hall, R.B. Smeby, and F.M. Bumpus, J. Med. Chem., 17, 1156 (1974).
(Original)

4071-v-20

[Sar1,Val5,Ala8]-Angiotensin II*
Sar-Arg-Val-Tyr-Val-His-Pro-Ala(M.W. 912.05)

4071
-20

C42H65N13O10

0.5 mg

2,900

Bulk

25 mg

41,000[34273-10-4][Sar1,Val5,Ala8]-Angiotensin II*
Sar-Arg-Val-Tyr-Val-His-Pro-Ala • AcOH • 4H2O
(M.W. 912.05 • 60.05 • 72.06)

Vial

C42H65N13O10 • CH3COOH • 4H2O

Angiotensin II Selective Antagonist
1) D.T. Pals, F.D. Masucci, G.S. Denning, Jr., F. Sipos, and D.C. Fessler, Circ. Res., 29, 673 (1971). (Original)

4034-v-20

[Val5]-Angiotensin II*
Asp-Arg-Val-Tyr-Val-His-Pro-Phe(M.W. 1032.2)

4034
-20

C49H69N13O12

Vial

0.5 mg

2,800

Bulk

25 mg
100 mg34,00096,000[58-49-1][Val5]-Angiotensin II*
Asp-Arg-Val-Tyr-Val-His-Pro-Phe • AcOH • 4H2O
(M.W. 1032.2 • 60.05 • 72.06)
C49H69N13O12 • CH3COOH • 4H2O

[5649-07-0]

1) D.F. Elliott and W.S. Peart, Nature, 177, 527 (1956). (Original; Heterogenous Renin)
2) H. Akagi, T. Hayashi, T. Nakayama, T. Nakajima, T.X. Watanabe, and H. Sokabe, Chem. Pharm. Bull.,30, 2498 (1982). (Original; Homologous Renin)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 17 –and Proteins

CompoundBiologically Active Peptides

CodeAngiotensin and Related Peptides (continued)
Code

Compound4037-v

Des-Asp1-[Ile8]-Angiotensin II
Arg-Val-Tyr-Ile-His-Pro-Ile-20

(M.W. 897.08)

4037
-20

Price:Yen

C43H68N12O9

Vial

0.5 mg

2,700

Bulk

25 mg
100 mg33,00088,000[52498-25-6]

Des-Asp1-[Ile8]-Angiotensin II
Arg-Val-Tyr-Ile-His-Pro-Ile • 2AcOH • 4H2O
(M.W. 897.08 • 120.10 • 72.06)
C43H68N12O9 • 2CH3COOH • 4H2O

[102029-49-2]

Angiotensin III Selective Antagonist
1) T. Kono, F. Ikeda, F. Oseko, H. Imura, and J. Endo, J. Clin. Endocrinol. Metab., 52, 354 (1981). (Pharmacol.)4296-v-20

Vial

CGP 42112
Nic-Tyr-Lys(Z-Arg)-His-Pro-Ile

0.5 mg5,000(Nic-: Nicotinoyl, Z-: Benzyloxycarbonyl)(M.W. 1052.2)

C52H69N13O11[127060-75-7]

Angiotensin AT2 Receptor Agonist
1) S.E. Whitebread, V. Taylor, S.P. Bottari, B. Kamber, and M. de Gasparo, Biochem. Biophys. Res. Commun.,
181, 1365 (1991). (Original)
2) B. Buisson, S.P. Bottari, M. de Gasparo, N. Gallo-Payet, and M.D. Payet, FEBS Lett., 309, 161 (1992). (Pharmacol.)3) G. Koike, M. Horiuchi, T. Yamada, C. Szpirer, H.J. Jacob, and V.J. Dzau, Biochem. Biophys. Res. Commun.,
203, 1842 (1994). (Pharmacol.)4439-v-20

Proangiotensin-12 (Rat)
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-LeuLeu-Tyr(M.W. 1572.8)

C77H109N19O17

Vial

0.5 mg

4,000[914910-73-9]

New Member of Angiotensin Family
It is well-established that the renin-angiotensin system plays an essential role in the maintenance of bloodpressure and body fluid homeostasis [M.J. Peach, Physiol. Rev., 57, 313 (1977). (Review), D.J. Campbell,
J. Clin. Invest., 79, 1 (1987). (Review)]. In the cardiovascular system, the expressed angiotensinogen is cleaved
by renin, which generates a 10 amino acid residue peptide, angiotensin I (Ang I). This Ang I is attacked byangiotensin I converting enzyme (ACE), and the carboxyl-terminal 2 amino acid truncated Ang II is produced.
Further trimmed peptides of Ang II at either the amino- or carboxyl-terminus, that is, Ang III, Ang IV, and Ang(1-7), were also identified in mammals. As far as we know, the primary structure of Ang I is conserved in many
animals (human, rat, porcine, canine, rabbit, and guinea pig), although bovine Ang I is Val5 instead of Ile5.

Code

CompoundPrimary structure

4007-v
4001-v
4028-v
4331-v
4332-v
4439-v

Angiotensin I (Human)
Angiotensin II (Human)
Angiotensin III (Human)
Angiotensin IV (Human)
Angiotensin (Human, 1-7)
Proangiotensin-12 (Rat)

DRVYIHPFHLDRVYIHPF
RVYIHPFVYIHPFDRVYIHPDRVYIHPFHLLY– 18 –

Angiotensin and Related Peptides (continued)

ANP and Related Peptides
1) P. Needleman, E.H. Blaine, J.E. Greenwald, M.L. Michener, C.B. Saper, P.T. Stockmann, and H.E. Tolunay,
Annu. Rev. Pharmacol. Toxicol., 29, 23 (1989). (Review)2) A. Rosenzweig and C.E. Seidman, Annu. Rev. Biochem., 60, 229 (1991). (Review)

List of ANP and Related Peptides
Species
Human

Code

CompoundQuantity

Price: Yen

Page4135-s4135-v
4145-v
4138-v
4137-v
4139-v
4168-sANP (Human, 1-28)
ANP (Human, 1-28)[Met(O)12]-ANP (Human, 1-28)
ANP (Human, 5-27)
ANP (Human, 5-28)
ANP (Human, 7-28)
β-ANP (Human), Antiparallel Dimer

0.1 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.1 mg vial

11,00034,00037,00029,00029,00029,00030,000

20
20
20
20
20
21
21

4151-s
4151-v
4159-v

ANP (Rat, 1-28)
ANP (Rat, 1-28)
ANP (Rat, 3-28)

0.1 mg vial
0.5 mg vial
0.5 mg vial

11,00034,00029,000

21
21
21

Rat

– 19 –and Proteins

1) S. Nagata, J. Kato, K. Sasaki, N. Minamino, T. Eto, and K. Kitamura, Biochem. Biophys. Res. Commun., 350, 1026
(2006). (Original; Primary Structure & Pharmacol.)• This compound is distributed through Peptide Institute, Inc. under the license of University of Miyazaki.

Biologically Active Peptides

In the survey of Ang-related peptide in the various tissues, a novel form of the peptide was isolated as a major
component in the small intestine of rats1). The isolated peptide, named proangiotensin-12, elutes later than Ang
II and Ang I on reversed-phase (RP)-HPLC, and its primary structure, analyzed by tandem mass spectrometricmethod, revealed that proangiotensin-12 is composed of 12 amino acid residues corresponding to theamino-terminus of angiotensinogen. Thus, proangiotensin-12 is the carboxyl-terminally 2 amino acidextended form of Ang I. Immunological proangiotensin-12 is detected in a variety of tissues as a major
component except for lungs, adrenal glands, pancreas, and aorta. In contrast, the plasma concentration ofproangiotensin-12 is lower than those of Ang I and Ang II. Biological activity measurements indicate that i)proangiotensin-12 constricts rat aortic ring preparation in a dose-dependent manner (3-100 nM), ii) the
constricting activity is blocked completely by either ACE inhibitor or Ang II type 1 blocker, and iii)
proangiotensin-12 elicits the blood pressure rise in rats (3-100 pmol/kg). These results suggest that the observed
functions of proangiotensin-12 may be afforded by converting the parental proangiotensin-12 to Ang II throughAng I.
Proangiotensin-12 is now available as a new member of the endogenous angiotensin peptide family. This
alternatively processed peptide of angiotensinogen may shed some light on evaluating the functions elicited by
the angiotensin family peptides, which may be sustained by the lack of the endogenous peptide ofproangiotensin-12. The enzyme(s) involved and the mechanism by which proangiotensin-12 is produced
remains to be clarified.

ANP and Related Peptides (continued)
Code

Compound4135-sANP (Human, 1-28)*
A-type (Atrial) Natriuretic Peptide (Human,1-28)(Porcine, Bovine, Canine)
Ser-Leu-Arg-Arg-Ser-Ser-Cys-Phe-Gly-GlyArg-Met-Asp-Arg-Ile-Gly-Ala-Gln-Ser-GlyLeu-Gly-Cys-Asn-Ser-Phe-Arg-Tyr-20

Price:Yen
Vial

0.1 mg11,000Vial

0.5 mg34,000(Disulfide bond between Cys7-Cys23)(M.W. 3080.4)

4135-v-20

C127H203N45O39S3[91917-63-4]

ANP (Human, 1-28)*
A-type (Atrial) Natriuretic Peptide (Human,1-28)(Porcine, Bovine, Canine)

1) K. Kangawa and H. Matsuo, Biochem. Biophys. Res. Commun., 118, 131 (1984). (Original)
2) T.X. Watanabe, Y. Noda, N. Chino, Y. Nishiuchi, T. Kimura, S. Sakakibara, and M. Imai, Eur. J. Pharmacol.,147, 49 (1988). (Pharmacol.)4145-v-20

[Met(O)12]-ANP (Human, 1-28)*
Vial[Met(O)12]-A-type (Atrial) Natriuretic Peptide (Human, 1-28)
Ser-Leu-Arg-Arg-Ser-Ser-Cys-Phe-Gly-GlyArg-Met(O)-Asp-Arg-Ile-Gly-Ala-Gln-Ser-GlyLeu-Gly-Cys-Asn-Ser-Phe-Arg-Tyr

0.5 mg37,000(Disulfide bond between Cys7-Cys23)(M.W. 3096.4)

C127H203N45O40S3

1) T.X. Watanabe, Y. Noda, N. Chino, Y. Nishiuchi, T. Kimura, S. Sakakibara, and M. Imai, Eur. J. Pharmacol.,147, 49 (1988). (Pharmacol.)4138-v-20

ANP (Human, 5-27)*
A-type (Atrial) Natriuretic Peptide (Human, 5-27)
Ser-Ser-Cys-Phe-Gly-Gly-Arg-Met-Asp-ArgIle-Gly-Ala-Gln-Ser-Gly-Leu-Gly-Cys-AsnSer-Phe-Arg

Vial

0.5 mg29,000(Disulfide bond between Cys7-Cys23)(M.W. 2404.7)

C97H154N34O32S3

1) T.X. Watanabe, Y. Noda, N. Chino, Y. Nishiuchi, T. Kimura, S. Sakakibara, and M. Imai, Eur. J. Pharmacol.,147, 49 (1988). (Pharmacol.)4137-v-20

ANP (Human, 5-28)*
A-type (Atrial) Natriuretic Peptide (Human, 5-28)
Ser-Ser-Cys-Phe-Gly-Gly-Arg-Met-Asp-ArgIle-Gly-Ala-Gln-Ser-Gly-Leu-Gly-Cys-AsnSer-Phe-Arg-Tyr

Vial

0.5 mg29,000(Disulfide bond between Cys7-Cys23)(M.W. 2567.8)

C106H163N35O34S31) S. Ueda, T. Sudoh, K. Fukuda, K. Kangawa, N. Minamino, and H. Matsuo, Biochem. Biophys. Res. Commun.,
149, 1055 (1987). (Original)
2) T.X. Watanabe, Y. Noda, N. Chino, Y. Nishiuchi, T. Kimura, S. Sakakibara, and M. Imai, Eur. J. Pharmacol.,147, 49 (1988). (Pharmacol.)*The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 20 –

ANP and Related Peptides (continued)
4139-v

ANP (Human, 7-28)*
A-type (Atrial) Natriuretic Peptide (Human, 7-28)
Cys-Phe-Gly-Gly-Arg-Met-Asp-Arg-Ile-GlyAla-Gln-Ser-Gly-Leu-Gly-Cys-Asn-Ser-PheArg-Tyr-20

Price:Yen
Vial

0.5 mg29,000(Disulfide bond between Cys7-Cys23)(M.W. 2393.7)

C100H153N33O30S3

1) T.X. Watanabe, Y. Noda, N. Chino, Y. Nishiuchi, T. Kimura, S. Sakakibara, and M. Imai, Eur. J. Pharmacol.,147, 49 (1988). (Pharmacol.)4168-s-20

β-ANP (Human)*
β-A-type (Atrial) Natriuretic Peptide
Antiparallel Dimer of ANP (Human, 1-28)

Vial

0.1 mg30,000――――――――――――――→
Ser-Leu-Arg-Arg-Ser-Ser-Cys7-Phe-Gly-Gly-Arg-Met-Asp-Arg-Ile-Gly-Ala-Gln-Ser-Gly-Leu-Gly-Cys23-Asn-Ser-Phe-Arg-Tyr
Tyr-Arg-Phe-Ser-Asn-Cys23'-Gly-Leu-Gly-Ser-Gln-Ala-Gly-Ile-Arg-Asp-Met-Arg-Gly-Gly-Phe-Cys7'-Ser-Ser-Arg-Arg-Leu-Ser―←―――――――――――――

7(Disulfide bonds between Cys -Cys
(M.W. 6160.9)

23'

and Cys7'-Cys23)

C254H406N90O78S61) K. Kangawa, A. Fukuda, and H. Matsuo, Nature, 313, 397 (1985). (Original)
2) N. Chino, K. Yoshizawa-Kumagaye, Y. Noda, T.X. Watanabe, T. Kimura, and S. Sakakibara, Biochem. Biophys.
Res. Commun., 141, 665 (1986). (Chem. Synthesis & Pharmacol.)4151-s-20

ANP (Rat, 1-28)
A-type (Atrial) Natriuretic Peptide (Rat, 1-28)(Rabbit, Mouse)
Ser-Leu-Arg-Arg-Ser-Ser-Cys-Phe-Gly-GlyArg-Ile-Asp-Arg-Ile-Gly-Ala-Gln-Ser-GlyLeu-Gly-Cys-Asn-Ser-Phe-Arg-Tyr

Vial

0.1 mg11,000Vial

0.5 mg34,000(Disulfide bond between Cys7-Cys23)(M.W. 3062.4)

4151-v-20

C128H205N45O39S2[88898-17-3]

ANP (Rat, 1-28)*
A-type (Atrial) Natriuretic Peptide (Rat, 1-28)(Rabbit, Mouse)

1) T.G. Flynn, M.L. DeBold, and A.J. DeBold, Biochem. Biophys. Res. Commun., 117, 859 (1983). (Original)
2) T.X. Watanabe, Y. Noda, N. Chino, Y. Nishiuchi, T. Kimura, S. Sakakibara, and M. Imai, Eur. J. Pharmacol.,147, 49 (1988). (Pharmacol.)4159-v-20

ANP (Rat, 3-28)
A-type (Atrial) Natriuretic Peptide (Rat, 3-28)
Arg-Arg-Ser-Ser-Cys-Phe-Gly-Gly-Arg-IleAsp-Arg-Ile-Gly-Ala-Gln-Ser-Gly-Leu-GlyCys-Asn-Ser-Phe-Arg-Tyr

Vial

0.5 mg29,000(Disulfide bond between Cys7-Cys23)(M.W. 2862.2)

C119H189N43O36S2[90984-99-9]

1) N.G. Seidah, C. Lazure, M. Chre｀tien, G. Thibault, R. Garcia, M. Cantin, J. Genest, R.F. Nutt, S.F. Brady, T.A. Lyle,
W.J. Paleveda, C.D. Colton, T.M. Ciccarone, and D.F. Veber, Proc. Natl. Acad. Sci. U.S.A., 81, 2640 (1984).
(Original)

Arg-Arg-Leu-Ile-Glu-Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Gly [RR-SRC] See Code 4184 on page 208*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 21 –and Proteins

CompoundBiologically Active Peptides

CodeApamin
Code

Compound4257-v

Apamin(Honeybee, Apis mellifera)
Cys-Asn-Cys-Lys-Ala-Pro-Glu-Thr-Ala-LeuCys-Ala-Arg-Arg-Cys-Gln-Gln-His-NH2-20

Price:Yen
Vial

0.5 mg18,000(Disulfide bonds between Cys1-Cys11 and Cys3-Cys15)(M.W. 2027.3)

C79H131N31O24S4[24345-16-2]

2+

Small Conductance Ca -Activated K+ Channel Blocker
1) E. Haberman, Pharmacol. Ther., 25, 255 (1984). (Review)2) A.L. Blatz and K.L. Magleby, Nature, 323, 718 (1986). (Pharmacol.)3) M.L. Garcia, A. Galvez, M. Garcia-Calvo, V.F. King, J. Vazquez, and G.J. Kaczorowski, J. Bioenerg. Biomembr.,23, 615 (1991). (Review)

Apelins
1) S.C. Sorli, L. van den Berghe, B. Masri, B. Knibiehler, and Y. Audigier, Drug Discov. Today, 11, 1100 (2006).
(Review)
2) C. Carpene, C. Dray, C. Attane, P. Valet, M.P. Portillo, I. Churruca, F.I. Milagro, and I. Castan-Laure, J. Physiol.
Biochem., 63, 359 (2007). (Review)3) I. Falcao-Pires, R. Ladeiras-Lopes, and A.F. Leite-Moreira, Expert Opin. Ther. Targets, 14, 633 (2010). (Review)

4362-s-20

Apelin-36 (Human)
Leu-Val-Gln-Pro-Arg-Gly-Ser-Arg-Asn-GlyPro-Gly-Pro-Trp-Gln-Gly-Gly-Arg-Arg-LysPhe-Arg-Arg-Gln-Arg-Pro-Arg-Leu-Ser-HisLys-Gly-Pro-Met-Pro-Phe(M.W. 4195.8)

C184H297N69O43S

Vial

0.1 mg15,000[252642-12-9]

Ligand for APJ Receptor
1) K. Tatemoto, M. Hosoya, Y. Habata, R. Fujii, T. Kakegawa, M.-X. Zou, Y. Kawamata, S. Fukusumi, S. Hinuma,
C. Kitada, T. Kurokawa, H. Onda, and M. Fujino, Biochem. Biophys. Res. Commun., 251, 471 (1998).
(Original; Human and Bovine)2) M.-X. Zou, H.-Y. Liu, Y. Haraguchi, Y. Soda, K. Tatemoto, and H. Hoshino, FEBS Lett., 473, 15 (2000). (Pharmacol.)3) M. Hosoya, Y. Kawamata, S. Fukusumi, R. Fujii, Y. Habata, S. Hinuma, C. Kitada, S. Honda, T. Kurokawa, H. Onda,
O. Nishimura, and M. Fujino, J. Biol. Chem., 275, 21061 (2000). (Pharmacol.)• This compound is distributed through Peptide Institute, Inc. under the license of Takeda Pharmaceutical Company
Limited.

4361-v-20

[Pyr1]-Apelin-13 (Human)(Bovine, Rat)
Pyr-Arg-Pro-Arg-Leu-Ser-His-Lys-Gly-ProMet-Pro-Phe(M.W. 1533.8)

C69H108N22O16S

Vial

0.5 mg

7,000[217082-60-5]

Ligand for APJ Receptor
1) K. Tatemoto, M. Hosoya, Y. Habata, R. Fujii, T. Kakegawa, M.-X. Zou, Y. Kawamata, S. Fukusumi, S. Hinuma,
C. Kitada, T. Kurokawa, H. Onda, and M. Fujino, Biochem. Biophys. Res. Commun., 251, 471 (1998).
(Original; Human and Bovine)2) M.-X. Zou, H.-Y. Liu, Y. Haraguchi, Y. Soda, K. Tatemoto, and H. Hoshino, FEBS Lett., 473, 15 (2000). (Pharmacol.)3) M. Hosoya, Y. Kawamata, S. Fukusumi, R. Fujii, Y. Habata, S. Hinuma, C. Kitada, S. Honda, T. Kurokawa, H. Onda,
O. Nishimura, and M. Fujino, J. Biol. Chem., 275, 21061 (2000). (Pharmacol.)4) D.K. Lee, R. Cheng, T. Nguyen, T. Fan, A.P. Kariyawasam, Y. Liu, D.H. Osmond, S.R. George, and B.F.O'Dowd,
J. Neurochem., 74, 34 (2000). (cDNA Seq.; Rat)
5) N. De Mota, A.R.-L. Goazigo, S.E. Messari, N. Chartrel, D. Roesch, C. Dujardin, C. Kordon, H. Vaudry, F. Moos, andC. Llorens-Cortes, Proc. Natl. Acad. Sci. U.S.A., 101, 10464 (2004). (Endogenous Apelin 13 in Rat)
• This compound is distributed through Peptide Institute, Inc. under the license of Takeda Pharmaceutical Company
Limited.

– 22 –

Arg-Gly-Asp-Peptides
Price:Yen

4304-v

cyclo (Arg-Gly-Asp-D-Phe-Val)-20

(M.W. 574.63)

4304

cyclo (Arg-Gly-Asp-D-Phe-Val) • AcOH • 2H2O

-20

(M.W. 574.63 • 60.05 • 36.03)

C26H38N8O7

Vial

0.5 mg

6,000

Bulk

25 mg

56,000[137813-35-5]

C26H38N8O7 • CH3COOH • 2H2O

Angiogenesis Inhibitor
1) P.C. Brooks, A.M.P. Montgomery, M. Rosenfeld, R.A. Reisfeld, T. Hu, G. Klier, and D.A. Cheresh, Cell,79, 1157 (1994). (Original)
2) M. Friedlander, C.L. Theesfeld, M. Sugita, M. Fruttiger, M.A. Thomas, S. Chang, and D.A. Cheresh,
Proc. Natl. Acad. Sci. U.S.A., 93, 9764 (1996). (Pharmacol.)4269-s-20

Decorsin(Leech, Macrobdella decora)
Ala-Pro-Arg-Leu-Pro-Gln-Cys-Gln-Gly-AspAsp-Gln-Glu-Lys-Cys-Leu-Cys-Asn-Lys-AspGlu-Cys-Pro-Pro-Gly-Gln-Cys-Arg-Phe-ProArg-Gly-Asp-Ala-Asp-Pro-Tyr-Cys-Glu

Vial

0.1 mg25,000(Disulfide bonds between Cys7-Cys15, Cys17-Cys27, and Cys22-Cys38)(M.W. 4377.8)

C179H271N55O62S6

Glycoprotein IIb / IIIa Antagonist, Platelet Aggregation Inhibitor
1) J.L. Seymour, W.J. Henzel, B. Nevins, J.T. Stults, and R.A. Lazarus, J. Biol. Chem., 265, 10143 (1990). (Original)
2) A.M. Krezel, G. Wagner, J. Seymour-Ulmer, and R.A. Lazarus, Science, 264, 1944 (1994). (S-S Bond)

4171-v-20

Fibronectin Active Fragment (RGDS)
Arg-Gly-Asp-Ser(M.W. 433.42)

4171
-20

C15H27N7O8

Vial

0.5 mg

2,900

Bulk

25 mg
100 mg24,00075,000[91037-65-9]

Fibronectin Active Fragment (RGDS)
Arg-Gly-Asp-Ser • 1/ 2 AcOH • 2H2O
C15H27N7O8 • 1/2 CH3COOH • 2H2O
Purity Information: Qp See page IV (XVI)(M.W. 433.42 • 30.03 • 36.03)

1) M.D. Piershbacher and E. Ruoslahti, Nature, 309, 30 (1984). (Original)
2) D.M. Haverstick, J.F. Cowan, K.M. Yamada, and S.A. Santoro, Blood, 66, 946 (1985). (Pharmacol.)4189-v-20

Fibronectin Active Fragment (GRGDS)
Gly-Arg-Gly-Asp-Ser(M.W. 490.47)

4189
-20

C17H30N8O9

Vial

0.5 mg

3,000

Bulk

25 mg
100 mg28,00075,000[96426-21-0]

Fibronectin Active Fragment (GRGDS)
Gly-Arg-Gly-Asp-Ser • 1/ 2 AcOH • 2H2O

C17H30N8O9 • 1/2 CH3COOH • 2H2O
1) S.K. Akiyama and K.M. Yamada, J. Biol. Chem., 260, 10402 (1985). (Original)
2) K. Olden, S. Mohla, S.A. Newton, S.L. White, and M.J. Humphries, Ann. N. Y. Acad. Sci., 551, 421 (1988). (Review)(M.W. 490.47 • 30.03 • 36.03)

Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His See Code 4133 on page 209– 23 –and Proteins

CompoundBiologically Active Peptides

CodeBovine Adrenal Medulla Dodecapeptide (BAM-12P)
CodeCompound4119-v

BAM-12P
Bovine Adrenal Medulla Dodecapeptide
Tyr-Gly-Gly-Phe-Met-Arg-Arg-Val-Gly-ArgPro-Glu-20

(M.W. 1424.6)

Price:Yen

C62H97N21O16S

Vial

0.5 mg6,600[75513-71-2]

1) K. Mizuno, N. Minamino, K. Kangawa, and H. Matsuo, Biochem. Biophys. Res. Commun., 95, 1482 (1980).
(Original)

Big Endothelin-1 (Human, 1-38) See Code 4208 on page 61
Big Endothelin-1 (Porcine, 1-39) See Code 4207 on page 61
Big Endothelin-1 (Rat, 1-39) See Code 4266 on page 61
Big Endothelin-2 (Human, 1-37) See Code 4222 on page 61
Big Endothelin-2 (Human, 1-38) See Code 4253 on page 62
Big Endothelin-3 (Human, 1-41 Amide) See Code 4223 on page 62
Big Endothelin-3 (Rat, 1-41 Amide) See Code 4267 on page 62
Big Gastrin (Human) See Code 4183 on page 68
BNP See page 30 and 31

Bombesin
4086-v-20

Bombesin*(Frog, Bombina bombina)
Pyr-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-ValGly-His-Leu-Met-NH2(M.W. 1619.8)

4086
-20

C71H110N24O18S

0.5 mg

5,200

Bulk

25 mg

100,000[31362-50-2]

Bombesin*(Frog, Bombina bombina)
Pyr-Gln-Arg-Leu-Gly-Asn-Gln-Trp-Ala-ValGly-His-Leu-Met-NH2 • AcOH • 7H2O
(M.W. 1619.8 • 60.05 • 126.11)

Vial

C71H110N24O18S • CH3COOH • 7H2O

1) A. Anastasi, V. Erspamer, and M. Bucci, Experientia, 27, 166 (1971). (Original)
2) V. Erspamer and P. Melchiorri, Trends Pharmacol. Sci., 1, 391 (1980). (Review)3) J.G. McCoy and D.D. Avery, Peptides, 11, 595 (1990). (Review)4) L.K. Malendowicz, Horm. Metab. Res., 30, 374 (1998). (Review)

Bovine Adrenal Medulla Dodecapeptide See Code 4119 BAM-12P above*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 24 –

Bradykinin and Related Peptides
Berlin, 1970. (Review)
Verlag, Berlin, 1979. (Review)

List of Bradykinin and Related Peptides
Code

CompoundQuantity

Price: Yen

Page

0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial

2,600
3,100
3,300
3,300
3,200
3,400

below
28
29
28
28
29

0.5 mg vial
0.5 mg vial

2,700
2,700

27
27

0.5 mg vial

2,700

27

0.5 mg vial
0.5 mg vial
0.5 mg vial

4,100
4,800
12,00029
26
26

0.5 mg vial
0.5 mg vial

3,500
3,200

29 & 241
29 & 241

Agonist4002-v
Bradykinin★
4008-v
Lysyl-Bradykinin (Kallidin)★
Methionyl-Lysyl-Bradykinin★
4012-v
4130-vIsoleucyl-Seryl-Bradykinin★
4193-v[Hyp3]-Bradykinin
Lysyl-[Hyp3]-Bradykinin
4191-v
B1-Selective Agonist
4303-v
Des-Arg10-Kallidin★
4067-v
Des-Arg9-Bradykinin★
B1-Selective Antagonist
4065-v
Des-Arg9-[Leu8]-Bradykinin★
B2-Selective Antagonist
4175-v[Thi5,8,D-Phe7]-Bradykinin
D-Arginyl-[Hyp3,Thi5,8, D-Phe7]-Bradykinin★
4202-v
D-Arginyl-[Hyp3,Thi5, D-Tic7,Oic8]-Bradykinin★
4293-v
Radioimmunoassay
4075-v[Tyr8]-Bradykinin
4056-vTyrosyl-Bradykinin★

Other bulk packaging is available.

Code

Compound4002-v

Bradykinin*(Human, Bovine, Rat, Mouse)
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-20

(M.W. 1060.2)

4002
-20

Price:Yen

C50H73N15O11

Vial

0.5 mg

2,600

Bulk

25 mg
100 mg24,00064,000[58-82-2]

Bradykinin*(Human, Bovine, Rat, Mouse)
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg •2AcOH • 3H2O
(M.W. 1060.2 • 120.10 • 54.05)

C50H73N15O11 • 2CH3COOH • 3H2O
1) D.F. Elliott, G.P. Lewis, and E.W. Horton, Biochem. Biophys. Res. Commun., 3, 87 (1960). (Original; Bovine)
2) E.D. Nicolaides and H.A. DeWald, J. Org. Chem., 26, 3872 (1961). (Chem. Synthesis)
3) J.V. Pierce and M.E. Webster, Biochem. Biophys. Res. Commun., 5, 353 (1961). (Original; Human)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 25 –and Proteins

2) E.G. Erdos (ed.), Bradykinin, Kallidin and Kallikrein, Handbook of Experimental Pharmacology, Vol. 25, Suppl. Springer-

Biologically Active Peptides

1) E.G. Erdos (ed.), Bradykinin, Kallidin and Kallikrein, Handbook of Experimental Pharmacology, Vol. 25, Springer-Verlag,

Bradykinin and Related Peptides (continued)
Code

Compound4293-v

D-Arginyl-[Hyp3,Thi5, D-Tic7,Oic8]-Bradykinin
Hoe 140, Icatibant
D-Arg-Arg-Pro-Hyp-Gly-Thi-Ser- D-Tic-Oic-Arg-20

Price:Yen
Vial

0.5 mg12,00025 mg

152,500(Thi: L-Thienylalanine, Tic: 1,2,3,4-Tetrahydroisoquinoline-3-carboxylic acid,
Oic: (3aS,7aS)-Octahydroindolyl-2-carboxylic acid)(M.W. 1304.5)

C59H89N19O13S[130308-48-4]

4293

D-Arginyl-[Hyp3,Thi5, D-Tic7,Oic8]-Bradykinin-20

Hoe 140, Icatibant
D-Arg-Arg-Pro-Hyp-Gly-Thi-Ser- D-Tic-Oic-Arg •2AcOH • 4H2O

Bulk

(Thi: L-Thienylalanine, Tic: 1,2,3,4-Tetrahydroisoquinoline-3-carboxylic acid,
Oic: (3aS,7aS)-Octahydroindolyl-2-carboxylic acid)(M.W. 1304.5 • 120.10 • 72.06)

C59H89N19O13S • 2CH3COOH • 4H2O

[138614-30-9]

Bradykinin B2-Receptor Antagonist
1) F.J. Hock, K. Wirth, U. Albus, W. Linz, H.J. Gerhards, G. Wiemer, St. Henke, G. Breipohl, W. Konig, J. Knolle, andB.A. Scholkens, Br. J. Pharmacol., 102, 769 (1991). (Original & Pharmacol.; in vitro)
2) K. Wirth, F.J. Hock, U. Albus, W. Linz, H.G. Alpermann, H. Anagnostopoulos, S. Henke, G. Breipohl, W. Ko
nig,
J. Knolle, and B.A. Scholkens, Br. J. Pharmacol., 102, 774 (1991). (Original & Pharmacol.; in vivo)
3) A.R. Baydon and B. Woodward, Br. J. Pharmacol., 103, 1829 (1991). (Pharmacol.)4) G. Wiemer, R. Popp, B.A. Scholkens, and H. Go
gelein, Brain Res., 638, 261 (1994). (Pharmacol.; Icatibant)4202-v

D-Arginyl-[Hyp3,Thi5,8,D-Phe7]-Bradykinin-20

D-Arg-Arg-Pro-Hyp-Gly-Thi-Ser- D-Phe-Thi-Arg

Vial

0.5 mg

4,800

Bulk

25 mg

61,000(Thi: L-Thienylalanine)(M.W. 1294.5)

C56H83N19O13S2[103412-42-6]

4202

D-Arginyl-[Hyp3,Thi5,8,D-Phe7]-Bradykinin-20

D-Arg-Arg-Pro-Hyp-Gly-Thi-Ser- D-Phe-Thi-Arg •2AcOH • 4H2O
(Thi: L-Thienylalanine)(M.W. 1294.5 • 120.10 • 72.06)

C56H83N19O13S2 • 2CH3COOH • 4H2O

Bradykinin B2-Receptor Antagonist
1) M. Schachter, Y. Uchida, D.J. Longridge, T. Labedz, E.T. Whalley, R.J. Vavrek, and J.M. Stewart, Br. J. Pharmacol.,92, 851 (1987). (Original)
2) J.M. Stewart and R.J. Vavrek, Adv. Biosci., 65, 73 (1987). (Pharmacol.; pA2)
3) D.C. Perry, Pharmacol. Biochem. Behav., 28, 15 (1987). (Pharmacol.; CNS)

4009-v-20

Bradykinin-Potentiator B(Mamushi, Agkistrodon halys blomhoffii)
Pyr-Gly-Leu-Pro-Pro-Arg-Pro-Lys-Ile-ProPro(M.W. 1182.4)

C56H91N15O13

Vial

0.5 mg2,800[30892-86-5]

Inhibitor for Peptidyl-Dipeptidase A, Kininase II, and Angiotensin Converting Enzyme (ACE)1) H. Kato and T. Suzuki, Biochemistry, 10, 972 (1971). (Original)– 26 –

Bradykinin and Related Peptides (continued)
4010-v

Bradykinin-Potentiator C(Mamushi, Agkistrodon halys blomhoffii)
Pyr-Gly-Leu-Pro-Pro-Gly-Pro-Pro-Ile-ProPro-20

(M.W. 1052.2)

Price:Yen

C51H77N11O13

Vial

0.5 mg2,300[30953-20-9]

Inhibitor for Peptidyl-Dipeptidase A, Kininase II, and Angiotensin Converting Enzyme (ACE)1) H. Kato and T. Suzuki, Biochemistry, 10, 972 (1971). (Original)

4067-v-20

Des-Arg9-Bradykinin
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe(M.W. 904.02)

4067
-20

C44H61N11O10

0.5 mg

2,700

Bulk

25 mg

43,000[15958-92-6]

Des-Arg9-Bradykinin
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe • AcOH • 3H2O
(M.W. 904.02 • 60.05 • 54.05)

Vial

C44H61N11O10 • CH3COOH • 3H2O

Bradykinin B1-Receptor Agonist
1) D. Regoli, J. Barabe, and W.K. Park, Can. J. Physiol. Pharmacol., 55, 855 (1977). (Original)

4303-v-20

Des-Arg10-Kallidin
Lysyl-Des-Arg9-Bradykinin
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe(M.W. 1032.2)

4303
-20

C50H73N13O11

0.5 mg

2,700

Bulk

25 mg

43,000[71800-36-7]

Des-Arg10-Kallidin
Lysyl-Des-Arg9-Bradykinin
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe • 2AcOH • 4H2O
(M.W. 1032.2 • 120.10 • 72.06)

Vial

C50H73N13O11 • 2CH3COOH • 4H2O

Bradykinin B1-Receptor Agonist
1) J.P. Galizzi, M.C. Bodinier, B. Chapelain, S.M. Ly, L. Coussy, S. Giraud, G. Neliat, and T. Jean, Br. J. Pharmacol.,113, 389 (1994). (Original)
2) J.G. Menke, J.A. Borkowski, K.K. Bierilo, T. MacNeil, A.W. Derrick, K.A. Schneck, R.W. Ransom, C.D. Strader,
D.L. Linemeyer, and J.F. Hess, J. Biol. Chem., 269, 21583 (1994). (Pharmacol.)3) J.S. Zuzack, M.R. Burkard, D.K. Curdrado, R.A. Greer, W.M. Selig, and E.T. Whalley, J. Pharmacol. Exp. Ther.,
277, 1337 (1996). (Pharmacol.)4065-v-20

Des-Arg9-[Leu8]-Bradykinin
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Leu(M.W. 870.01)

4065
-20

C41H63N11O10

Vial

0.5 mg

2,700

Bulk

25 mg

39,000[64695-06-3]

Des-Arg9-[Leu8]-Bradykinin
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Leu • AcOH • 3H2O
(M.W. 870.01 • 60.05 • 54.05)
C41H63N11O10 • CH3COOH • 3H2O

[115035-45-5]

Bradykinin B1-Receptor Antagonist
1) D. Regoli, J. Barabe, and W.K. Park, Can. J. Physiol. Pharmacol., 55, 855 (1977). (Original ; pA2)

– 27 –and Proteins

CompoundBiologically Active Peptides

CodeBradykinin and Related Peptides (continued)
Code

Compound4097-v

Des-Pro2-Bradykinin
Arg-Pro-Gly-Phe-Ser-Pro-Phe-Arg-20

(M.W. 963.09)

4097
-20

Price:Yen

C45H66N14O10

Vial

0.5 mg

2,800

Bulk

25 mg

43,000[80943-05-1]

Des-Pro2-Bradykinin
Arg-Pro-Gly-Phe-Ser-Pro-Phe-Arg • 2AcOH • 3H2O
(M.W. 963.09 • 120.10 • 54.05) C45H66N14O10 • 2CH3COOH • 3H2O
Purity Information : Qp See page IV (XVI)

Inhibitor for Peptidyl-Dipeptidase A, Kininase II, and Angiotensin Converting Enzyme (ACE)1) M. Naruse, S. Tamanami, K. Shuto, S. Sakakibara, and T. Kimura, Chem. Pharm. Bull., 29, 3369 (1981). (Original)

4193-v-20

[Hyp3]-Bradykinin*(Human)Arg-Pro-Hyp-Gly-Phe-Ser-Pro-Phe-Arg(M.W. 1076.2)

C50H73N15O12Vial

0.5 mg

3,200

Vial

0.5 mg

3,300

Bulk

25 mg

47,000[37642-65-2]

1) H. Kato, Y. Matsumura, and H. Maeda, FEBS Lett., 232, 252 (1988). (Original)

4130-v-20

Isoleucyl-Seryl-Bradykinin*
T-Kinin(Rat)
Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-PheArg(M.W. 1260.4)

4130
-20

C59H89N17O14[86030-63-9]

Isoleucyl-Seryl-Bradykinin*
T-Kinin(Rat)
Ile-Ser-Arg-Pro-Pro-Gly-Phe-Ser-Pro-PheArg • 2AcOH • 5H2O
(M.W. 1260.4 • 120.10 • 90.08)

C59H89N17O14 • 2CH3COOH • 5H2O

1) H. Okamoto and L.M. Greenbaum, Biochem. Biophys. Res. Commun., 112, 701 (1983). (Original)

4008-v-20

Vial

0.5 mg3,100

Lysyl-Bradykinin*
Kallidin(Human, Bovine)
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg •3AcOH • 4H2O

Bulk

25 mg

36,000(M.W. 1188.4 • 180.16 • 72.06)[100900-38-7]

Lysyl-Bradykinin*
Kallidin(Human, Bovine)
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg(M.W. 1188.4)

4008
-20

C56H85N17O12[342-10-9]

C56H85N17O12 • 3CH3COOH • 4H2O

1) J.V. Pierce and M.E. Webster, Biochem. Biophys. Res. Commun., 5, 353 (1961). (Original; Human)
2) D.F. Elliott and G.P. Lewis, Biochem. J., 95, 437 (1965). (Seq.; Bovine)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 28 –

Bradykinin and Related Peptides (continued)
4191-v

Lysyl-[Hyp3]-Bradykinin*(Human)Lys-Arg-Pro-Hyp-Gly-Phe-Ser-Pro-Phe-Arg-20

(M.W. 1204.4)

Price:Yen
Vial

0.5 mg3,400

C56H85N17O131) M. Sasaguri, M. Ikeda, M. Ideishi, and K. Arakawa, Biochem. Biophys. Res. Commun., 150, 511 (1988). (Original)

4012-v-20

Methionyl-Lysyl-Bradykinin*(Human, Bovine)
Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-PheArg(M.W. 1319.6)

4012
-20

C61H94N18O13S

0.5 mg

3,300

Bulk

25 mg

43,000[550-19-6]

Methionyl-Lysyl-Bradykinin*(Human, Bovine)
Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-PheArg • 3AcOH • 2H2O
(M.W. 1319.6 • 180.16 • 36.03)

Vial

C61H94N18O13S • 3CH3COOH • 2H2O

1) D.F. Elliott and G.P. Lewis, Biochem. J., 95, 437 (1965). (Original; Bovine)2) I. Ohkubo, K. Kurachi, T. Takasawa, H. Shiokawa, and M. Sasaki, Biochemistry, 23, 5691 (1984).
(cDNA Seq.; Human)4175-v-20

[Thi5,8,D-Phe7]-Bradykinin
Arg-Pro-Pro-Gly-Thi-Ser-D-Phe-Thi-Arg

Vial

0.5 mg

4,100

Vial

0.5 mg3,500(Thi: L-Thienylalanine)(M.W. 1122.3)

C50H71N15O11S2[97825-07-5]

Bradykinin B2-Receptor Antagonist
1) R.J. Vavrek and J.M. Stewart, Peptides, 6, 161 (1985). (Original)

4075-v-20

[Tyr8]-Bradykinin
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Tyr-Arg(M.W. 1076.2)

C50H73N15O12[32222-00-7]

For Radioimmunoassay
1) M.D. Nielsen, F. Nielsen, A.M. Kappelgaard, and J. Giese, Clinica Chimica Acta, 125, 145 (1982).
(Radioimmunoassay)
2) M.J. Fredrick, F.C. Abel, W.A. Rightsel, E.E. Muirhead, and C.E. Odya, Life Sci., 37, 331 (1985).
(Radioimmunoassay)

4056-v-20

Tyrosyl-Bradykinin
Tyr-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg(M.W. 1223.4)

C59H82N16O13

Vial

0.5 mg[33289-76-8]

For Radioimmunoassay
1) R.E. Lewis, S.R. Childers, and M.I. Phillips, Brain Res., 346, 263 (1985). (Radioimmunoassay)
2) M.J. Fredrick, F.C. Abel, W.A. Rightsel, E.E. Muirhead, and C.E. Odya, Life Sci., 37, 331 (1985).
(Radioimmunoassay)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 29 –

3,200

and Proteins

CompoundBiologically Active Peptides

CodeB-type (Brain) Natriuretic Peptides (BNP)
1) A. Rosenzweig and C.E. Seidman, Annu. Rev. Biochem., 60, 229 (1991). (Review)

Code

Compound4212-v

BNP-32 (Human)*B-type (Brain) Natriuretic Peptide-32 (Human)
Ser-Pro-Lys-Met-Val-Gln-Gly-Ser-Gly-CysPhe-Gly-Arg-Lys-Met-Asp-Arg-Ile-Ser-SerSer-Ser-Gly-Leu-Gly-Cys-Lys-Val-Leu-ArgArg-His-20

Price:Yen
Vial

0.5 mg41,000(Disulfide bond between Cys10-Cys26)(M.W. 3464.0)

C143H244N50O42S4[124584-08-3]

1) T. Sudoh, K. Maekawa, M. Kojima, N. Minamino, K. Kangawa, and H. Matsuo, Biochem. Biophys. Res. Commun.,
159, 1427 (1989). (Original; cDNA)
2) Y. Kambayashi, K. Nakao, M. Mukoyama, Y. Saito, Y. Ogawa, S. Shiono, K. Inouye, N. Yoshida, and H. Imura,
FEBS Lett., 259, 341 (1990). (Original; Isolation & Structure)

4230-v-20

Tyrosyl-BNP-32 (Human)*Tyrosyl-B-type (Brain) Natriuretic Peptide-32 (Human)
Tyr-Ser-Pro-Lys-Met-Val-Gln-Gly-Ser-GlyCys-Phe-Gly-Arg-Lys-Met-Asp-Arg-Ile-SerSer-Ser-Ser-Gly-Leu-Gly-Cys-Lys-Val-LeuArg-Arg-His

Vial

0.5 mg48,000Vial

0.5 mg41,000(Disulfide bond between Cys10-Cys26)(M.W. 3627.2)

C152H253N51O44S4
Purity Information : QX See page IV (XVI)For Radioimmunoassay
4200-v-20

BNP-26 (Porcine)*
B-type (Brain) Natriuretic Peptide-26 (Porcine)
Asp-Ser-Gly-Cys-Phe-Gly-Arg-Arg-Leu-AspArg-Ile-Gly-Ser-Leu-Ser-Gly-Leu-Gly-CysAsn-Val-Leu-Arg-Arg-Tyr(Disulfide bond between Cys4-Cys20)(M.W. 2869.2)

C120H198N42O36S2[114547-28-3]

1) T. Sudoh, K. Kangawa, N. Minamino, and H. Matsuo, Nature, 332, 78 (1988). (Original)

4213-v-20

BNP-32 (Rat)*
B-type (Brain) Natriuretic Peptide-32 (Rat)
Asn-Ser-Lys-Met-Ala-His-Ser-Ser-Ser-CysPhe-Gly-Gln-Lys-Ile-Asp-Arg-Ile-Gly-AlaVal-Ser-Arg-Leu-Gly-Cys-Asp-Gly-Leu-ArgLeu-Phe

Vial

0.5 mg41,000(Disulfide bond between Cys10-Cys26)(M.W. 3452.9)

C146H239N47O44S3[133448-20-1]

1) M. Kojima, N. Minamino, K. Kangawa, and H. Matsuo, Biochem. Biophys. Res. Commun., 159, 1420 (1989).
(Original; cDNA)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 30 –

B-type (Brain) Natriuretic Peptides (BNP) (continued)
4218-s

BNP-45 (Rat)*
B-type (Brain) Natriuretic Peptide-45 (Rat)
Ser-Gln-Asp-Ser-Ala-Phe-Arg-Ile-Gln-GluArg-Leu-Arg-Asn-Ser-Lys-Met-Ala-His-SerSer-Ser-Cys-Phe-Gly-Gln-Lys-Ile-Asp-ArgIle-Gly-Ala-Val-Ser-Arg-Leu-Gly-Cys-AspGly-Leu-Arg-Leu-Phe-20

Price:Yen
Vial

0.1 mg14,000(Disulfide bond between Cys23-Cys39)(M.W. 5040.7)

C213H349N71O65S3[123337-89-3]

1) M. Aburaya, J. Hino, N. Minamino, K. Kangawa, and H. Matsuo, Biochem. Biophys. Res. Commun.,
163, 226 (1989). (Original)
2) Y. Kambayashi, K. Nakao, H. Itoh, K. Hosoda, Y. Saito, T. Yamada, M. Mukoyama, H. Arai, G. Shirakami, S. Suga,
Y. Ogawa, M. Jougasaki, N. Minamino, K. Kangawa, H. Matsuo, K. Inouye, and H. Imura, Biochem. Biophys. Res.
Commun., 163, 233 (1989). (Original)Calcicludine
4310-s-20

Calcicludine*
CaC(Green Mamba, Dendroaspis angusticeps)
Trp-Gln-Pro-Pro-Trp-Tyr-Cys-Lys-Glu-ProVal-Arg-Ile-Gly-Ser-Cys-Lys-Lys-Gln-PheSer-Ser-Phe-Tyr-Phe-Lys-Trp-Thr-Ala-LysLys-Cys-Leu-Pro-Phe-Leu-Phe-Ser-Gly-CysGly-Gly-Asn-Ala-Asn-Arg-Phe-Gln-Thr-IleGly-Glu-Cys-Arg-Lys-Lys-Cys-Leu-Gly-Lys

Vial

0.1 mg30,000(Disulfide bonds between Cys7-Cys57, Cys16-Cys40, and Cys32-Cys53)(M.W. 6980.1)

C321H476N86O78S6

Neuronal L-type Ca2+ Channel Blocker
1) H. Schweitz, C. Heurteaux, P. Bois, D. Moinier, G. Romey, and M. Lazdunski, Proc. Natl. Acad. Sci. U.S.A.,91, 878 (1994). (Original)
2) H. Nishio, Y. Nishiuchi, T. Inui, M. Nakao, T.X. Watanabe, T. Kimura, and S. Sakakibara, Peptide Chemistry
1995, 113 (1996). (Chem. Synthesis & Pharmacol.)3) O.D. Uchitel, Toxicon, 35, 1161 (1997). (Review)4) J. Santos-Torres, A. Fuente, J.M. Criado, A.S. Riolobos, M. Heredia, and J. Yajeya, J. Neurosci. Res., 85, 634 (2007).
(Pharmacol.)*The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 31 –and Proteins

CompoundBiologically Active Peptides

CodeCalciseptine
CodeCompound4255-sCalciseptine*(Black Mamba, Dendroaspis polylepis polylepis)
Arg-Ile-Cys-Tyr-Ile-His-Lys-Ala-Ser-LeuPro-Arg-Ala-Thr-Lys-Thr-Cys-Val-Glu-AsnThr-Cys-Tyr-Lys-Met-Phe-Ile-Arg-Thr-GlnArg-Glu-Tyr-Ile-Ser-Glu-Arg-Gly-Cys-GlyCys-Pro-Thr-Ala-Met-Trp-Pro-Tyr-Gln-ThrGlu-Cys-Cys-Lys-Gly-Asp-Arg-Cys-Asn-Lys-20

Price:Yen
Vial

0.1 mg30,000(Disulfide bonds between Cys3-Cys22, Cys17-Cys39, Cys41-Cys52, and Cys53-Cys58)(M.W. 7036.1)

L-type Ca2+

C299H468N90O87S10[134710-25-1]

Channel Blocker

1) J.R. De Weille, H. Schweitz, P. Maes, A. Tartar, and M. Lazdunski, Proc. Natl. Acad. Sci. U.S.A., 88, 2437 (1991).
(Original)
2) H. Kuroda, Y.-N. Chen, T.X. Watanabe, T. Kimura, and S. Sakakibara, Pept. Res., 5, 265 (1992). (Chem. Synthesis)
3) T.X. Watanabe, Y. Itahara, H. Kuroda, Y.-N. Chen, T. Kimura, and S. Sakakibara, Jpn. J. Pharmacol., 68, 305, (1995).
(Pharmacol.)4) N. Teramoto, R. Ogata, K. Okabe, A. Kameyama, M. Kameyama, T.X. Watanabe, H. Kuriyama, and K. Kitamura,Pflugers Arch., 432, 462 (1996). (Pharmacol.)Calcitonin
4051-s-20

Calcitonin (Human)
Cys-Gly-Asn-Leu-Ser-Thr-Cys-Met-Leu-GlyThr-Tyr-Thr-Gln-Asp-Phe-Asn-Lys-Phe-HisThr-Phe-Pro-Gln-Thr-Ala-Ile-Gly-Val-GlyAla-Pro-NH2

Vial

0.1 mg

9,000

Vial

0.5 mg27,000(Disulfide bond between Cys1-Cys7)(M.W. 3417.8)

4051-v

C151H226N40O45S3[21215-62-3]

Calcitonin (Human)-201) R. Neher, B. Riniker, W. Rittel, and H. Zuber, Helv. Chim. Acta, 51, 1900 (1968). (Original)
2) Y. Nakagawa, T. Morikawa, and S. Sakakibara, Peptide Chemistry 1977, 189 (1978). (Chem. Synthesis)

Calcitonin Gene Related Peptides See page 34 and 35*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 32 –

CART

Compound4350-sCART (Human, 55-102)
Vial
Cocaine- and Amphetamine-Regulated Transcript (Human, 55-102)
Val-Pro-Ile-Tyr-Glu-Lys-Lys-Tyr-Gly-GlnVal-Pro-Met-Cys-Asp-Ala-Gly-Glu-Gln-CysAla-Val-Arg-Lys-Gly-Ala-Arg-Ile-Gly-LysLeu-Cys-Asp-Cys-Pro-Arg-Gly-Thr-Ser-CysAsn-Ser-Phe-Leu-Leu-Lys-Cys-Leu-20

Price:Yen
0.1 mg30,000(Disulfide bonds between Cys68-Cys86, Cys74-Cys94, and Cys88-Cys101)(M.W. 5245.2)

C225H365N65O65S7[214050-22-3]

Food-Intake Inhibitor
1) P. Kristensen, M.E. Judge, L. Thim, U. Ribel, K.N. Christjansen, B.S. Wulff, J.T. Clausen, P.B. Jensen, O.D. Madsen,
N. Vrang, P.J. Larsen, and S. Hastrup, Nature, 393, 72 (1998). (Pharmacol.; Anorectic Peptide)2) J. Douglass and S. Daoud, Gene, 169, 241 (1996). (Original; cDNA)
3) A.J. Kastin and V. Akerstrom, Am. J. Physiol., 277, E901 (1999). (Pharmacol.; across BBB)
4) M.J. Kuhar, L.D. Adams, R.G. Hunter, S. Dall Vechia, and Y. Smith, Regul. Pept., 89, 1 (2000). (Review)

4351-s-20

CART (Rat, 55-102)
Vial
Cocaine- and Amphetamine-Regulated Transcript (Rat, 55-102)
Ile-Pro-Ile-Tyr-Glu-Lys-Lys-Tyr-Gly-GlnVal-Pro-Met-Cys-Asp-Ala-Gly-Glu-Gln-CysAla-Val-Arg-Lys-Gly-Ala-Arg-Ile-Gly-LysLeu-Cys-Asp-Cys-Pro-Arg-Gly-Thr-Ser-CysAsn-Ser-Phe-Leu-Leu-Lys-Cys-Leu

0.1 mg30,000(Disulfide bonds between Cys68-Cys86, Cys74-Cys94, and Cys88-Cys101)(M.W. 5259.2)

C226H367N65O65S7[209615-79-2]

Food-Intake Inhibitor
1) P. Kristensen, M.E. Judge, L. Thim, U. Ribel, K.N. Christjansen, B.S. Wulff, J.T. Clausen, P.B. Jensen, O.D. Madsen,
N. Vrang, P.J. Larsen, and S. Hastrup, Nature, 393, 72 (1998). (Pharmacol.; Anorectic Peptide)2) J. Douglass, A.A. McKinzie, and P. Couceyro, J. Neurosci., 15, 2471 (1995). (Original; cDNA)
3) L. Thim, P.F. Nielsen, M.E. Judge, A.S. Andersen, I. Diers, M. Egel-Mitani, and S. Hastrup, FEBS Lett.,
428, 263 (1998). (Biochem. & Pharmacol.)4) M.J. Kuhar, L.D. Adams, R.G. Hunter, S. Dall Vechia, and Y. Smith, Regul. Pept., 89, 1 (2000). (Review)

β-Casomorphins4079-v-20

β-Casomorphin-5 (Bovine)
Tyr-Pro-Phe-Pro-Gly(M.W. 579.64)

4079
-20

C30H37N5O7

0.5 mg

2,100

Bulk

25 mg
100 mg16,00047,000[72122-63-5]β-Casomorphin-5 (Bovine)
Tyr-Pro-Phe-Pro-Gly • 2H2O
(M.W. 579.64 • 36.03)

Vial

C30H37N5O7 • 2H2O

[72122-63-5]

1) V. Brantl, H. Teschemacher, A. Henschen, and F. Lottspeich, Hoppe-Seyler's Z. Physiol. Chem., 360, 1211 (1979).
(Original; Isolation)
2) A. Henschen, F. Lottspeich, V. Brantl, and H. Teschemacher, Hoppe-Seyler's Z. Physiol. Chem., 360, 1217 (1979).
(Original; Structure)– 33 –and Proteins

Code

Biologically Active Peptides

1) P.J. Larsen and R.G. Hunter, Peptides, 27, 1981 (2006). (Review)2) A. Vicentic and D.C. Jones, J. Pharmacol. Exp. Ther., 320, 499 (2007). (Review)

β-Casomorphins (continued)
Code

Compound4078-vβ-Casomorphin-7 (Bovine)
Tyr-Pro-Phe-Pro-Gly-Pro-Ile-20

(M.W. 789.92)

Price:Yen

C41H55N7O9

Vial

0.5 mg2,700[72122-62-4]

1) V. Brantl, H. Teschemacher, A. Henschen, and F. Lottspeich, Hoppe-Seyler's Z. Physiol. Chem., 360, 1211 (1979).
(Original; Isolation)
2) A. Henschen, F. Lottspeich, V. Brantl, and H. Teschemacher, Hoppe-Seyler's Z. Physiol. Chem., 360, 1217 (1979).
(Original; Structure)

CCK See page 36 and 37
CGP 42112 See Code 4296 on page 18

CGRP
4160-s-20

CGRP (Human)*Calcitonin Gene Related Peptide (Human)
α-CGRP (Human)
Ala-Cys-Asp-Thr-Ala-Thr-Cys-Val-Thr-HisArg-Leu-Ala-Gly-Leu-Leu-Ser-Arg-Ser-GlyGly-Val-Val-Lys-Asn-Asn-Phe-Val-Pro-ThrAsn-Val-Gly-Ser-Lys-Ala-Phe-NH2

Vial

0.1 mg11,500Vial

0.5 mg35,000(Disulfide bond between Cys2-Cys7)(M.W. 3789.3)

4160-v-20

C163H267N51O49S2[90954-53-3]

CGRP (Human)*Calcitonin Gene Related Peptide (Human)
α-CGRP (Human)

1) H.R. Morris, M. Panico, T. Etienne, J. Tippins, S.I. Girgis, and I. MacIntyre, Nature, 308, 746 (1984). (Original)• This compound is distributed through Peptide Institute, Inc. under the license of The Salk Institute. However, it is nolonger available in the United Kingdom due to the patent rights held by Celltech Ltd.

4232-v-20

CGRP (Human, 8-37)*
Calcitonin Gene Related Peptide (Human, 8-37)
α-CGRP (Human, 8-37)
Val-Thr-His-Arg-Leu-Ala-Gly-Leu-Leu-SerArg-Ser-Gly-Gly-Val-Val-Lys-Asn-Asn-PheVal-Pro-Thr-Asn-Val-Gly-Ser-Lys-Ala-Phe-NH2(M.W. 3125.6)

C139H230N44O38

Vial

0.5 mg22,000[119911-68-1]

CGRP Antagonist
1) T. Chiba, A. Yamaguchi, T. Yamatani, A. Nakamura, T. Morishita, T. Inui, M. Fukase, T. Noda, and T. Fujita,
Am. J. Physiol., 256, E331 (1989). (Original)
2) S.-P. Han, L. Naes, and T.C. Westfall, Biochem. Biophys. Res. Commun., 168, 786 (1990). (Pharmacol.)3) T. Dennis, A. Fournier, A. Cadieux, F. Pomerleau, F.B. Jolicoeur, S.St. Pierre, and R. Quirion,
J. Pharmacol. Exp. Ther., 254, 123 (1990). (Pharmacol.)4) S.M. Gardiner, A.M. Compton, P.A. Kemp, T. Bennett, C. Bose, R. Foulkes, and B. Hughes, Biochem. Biophys. Res.
Commun., 171, 938 (1990). (Pharmacol.)*The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 34 –CGRP (continued)
4163-sCGRP (Rat)*
Calcitonin Gene Related Peptide (Rat)α-CGRP (Rat)
Ser-Cys-Asn-Thr-Ala-Thr-Cys-Val-Thr-HisArg-Leu-Ala-Gly-Leu-Leu-Ser-Arg-Ser-GlyGly-Val-Val-Lys-Asp-Asn-Phe-Val-Pro-ThrAsn-Val-Gly-Ser-Glu-Ala-Phe-NH2-20

Price:Yen
Vial

0.1 mg11,500Vial

0.5 mg35,000(Disulfide bond between Cys2-Cys7)(M.W. 3806.2)

4163-v-20

C162H262N50O52S2[83651-90-5]

CGRP (Rat)*
Calcitonin Gene Related Peptide (Rat)α-CGRP (Rat)1) S.G. Amara, V. Jonas, M.G. Ronsenfeld, E.S. Ong, and R.M. Evans, Nature, 298, 240 (1982). (Original)
2) M.G. Rosenfeld, J.-J. Mermod, S,G. Amara, L.W. Swanson, P.E. Sawchenko, J. Rivier, W.W. Vale, and R.M. Evans,Nature, 304, 129 (1983). (Processing & Distribution in Neural Tissue)• This compound is distributed through Peptide Institute, Inc. under the license of The Salk Institute.

Charybdotoxin
1) M.L. Garcia, H.-G. Knaus, P. Munujos, R.S. Slaughter, and G.J. Kaczorowski, Am. J. Physiol., 269, C1 (1995). (Review)

4227-s-20

Charybdotoxin*
ChTX(Scorpion, Leiurus quinquestriatus hebraeus)
Pyr-Phe-Thr-Asn-Val-Ser-Cys-Thr-Thr-SerLys-Glu-Cys-Trp-Ser-Val-Cys-Gln-Arg-LeuHis-Asn-Thr-Ser-Arg-Gly-Lys-Cys-Met-AsnLys-Lys-Cys-Arg-Cys-Tyr-Ser

Vial

0.1 mg22,000(Disulfide bonds between Cys7-Cys28, Cys13-Cys33, and Cys17-Cys35)(M.W. 4295.9)
2+

C176H277N57O55S7[95751-30-7]+

Ca -Activated K Channel Blocker
1) G. Gimenez-Gallego, M.A. Navia, J.P. Reuben, G.M. Katz, G.J. Kaczorowski, and M.L. Garcia, Proc. Natl. Acad. Sci.
U.S.A., 85, 3329 (1988). (Original)
2) P. Lambert, H. Kuroda, N. Chino, T.X. Watanabe, T. Kimura, and S. Sakakibara, Biochem. Biophys. Res. Commun.,
170, 684 (1990). (Chem. Synthesis & Pharmacol.)Chemotactic Peptide
4066-v-20

Chemotactic Peptide
For-Met-Leu-Phe
FMLP(M.W. 437.55)

4066
-20

C21H31N3O5S

Vial

0.5 mg

2,400

Bulk

25 mg
100 mg

8,000
24,000[59880-97-6]

Chemotactic Peptide
For-Met-Leu-Phe
FMLP(M.W. 437.55)

C21H31N3O5S [59880-97-6]
1) L.T. Williams, R. Snyderman, M.C. Pike, and R.J. Lefkowitz, Proc. Natl. Acad. Sci. U.S.A., 74, 1204 (1977).
(Receptor Site on Human Leukocyte)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 35 –and Proteins

CompoundBiologically Active Peptides

CodeChlorotoxin
Code

Compound4282-v

Chlorotoxin(Scorpion, Leiurus quinquestriatus)
Met-Cys-Met-Pro-Cys-Phe-Thr-Thr-Asp-HisGln-Met-Ala-Arg-Lys-Cys-Asp-Asp-Cys-CysGly-Gly-Lys-Gly-Arg-Gly-Lys-Cys-Tyr-GlyPro-Gln-Cys-Leu-Cys-Arg-NH2-20

Price:Yen
Vial

0.5 mg45,000(Reported disulfide bonds between Cys2-Cys19, Cys5-Cys28, Cys16-Cys33, and Cys20-Cys35)(M.W. 3995.7)

C158H249N53O47S11[163515-35-3]

Small-Conductance Cl – Channel Blocker
1) J.A. DeBin, J.E. Maggio, and G.R. Strichartz, Am. J. Physiol., 264, C361 (1993). (Original)
2) J. Najib, P. Sautie｀re, J.C. Gesquie｀re, and A. Tartar, In, Inovation and Perspective in Solid Phase Synthesis,(R. Epton, ed.), Mayflower Worldwide, Birmingham, 1994, pp. 615-618. (Original; Amide)3) G. Lippens, J. Najib, S.J. Wodak, and A. Tartar, Biochemistry, 34, 13 (1995). (NMR Structure)4) L. Soroceanu, Y. Gillespie, M.B. Khazaeli, and H. Sontheimer, Cancer Res., 58, 4871 (1998). (Pharmacol.)5) D.B. Jacoby, E. Dyskin, M. Yalcin, K. Kesavan, W. Dahlberg, J. Ratliff, E.W. Johnson, and S.A. Mousa,
Anticancer Res., 30, 39 (2010). (Review)6) K. Kesavan, J. Ratliff, E.W. Johnson, W. Dahlberg, J.M. Asara, P. Misra, J.V. Frangioni, and D.B. Jacoby,
J. Biol. Chem., 285, 4366 (2010). (Review)

Cholecystokinin (CCK) and Related Peptides
1) J.E. Jorpes and V. Mutt (eds.), Secretin, Cholecystokinin, Pancreozymin and Gastrin, Handbook of Experimental
Pharmacology, Vol. 34, Springer-Verlag, Berlin, 1973. (Review)

4083-v-20

CCK-Tetrapeptide (30-33)*
CCK-4

Vial

0.5 mg

2,100

Bulk

25 mg
100 mg

9,000
27,000(Hydrochloride Form)

Trp-Met-Asp-Phe-NH2(M.W. 596.70)

4083
-20

C29H36N6O6S

CCK-Tetrapeptide (30-33)*
CCK-4
Trp-Met-Asp-Phe-NH2 • HCl • H2O(M.W. 596.70• 36.46 • 18.02)

C29H36N6O6S • HCl • H2O [5609-49-4]
1) J.F. Rehfeld, L.I. Larsson, N.R. Goltermann, T.W. Schwarz, J.J. Holst, S.L. Jensen, and J.S. Morley, Nature,
284, 33 (1980). (Neural Pharmacol.)4087-v-20

CCK-Octapeptide (26-33) (Non-Sulfated Form)*
CCK-8 (Non-Sulfated Form)

Vial

0.5 mg5,000(Ammonium Form)

Asp-Tyr-Met-Gly-Trp-Met-Asp-Phe-NH2(M.W. 1063.2)

C49H62N10O13S2[25679-24-7]

1) M.A. Ondetti, J. Pluscec, E.F. Sabo, J.T. Sheehan, and N. Williams, J. Am. Chem. Soc., 92, 195 (1970).
(Chem. Synthesis)

4100-v-20

CCK-Octapeptide (26-33) (Sulfated Form)*
CCK-8 (Sulfated Form)

Vial

0.5 mg12,000(Ammonium Form)

Asp-Tyr(SO3H)-Met-Gly-Trp-Met-Asp-Phe-NH2(M.W. 1143.3)

C49H62N10O16S3[25126-32-3]

1) M.A. Ondetti, J. Pluscec, E.F. Sabo, J.T. Sheehen, and N. Williams, J. Am. Chem. Soc., 92, 195 (1970).
(Chem. Synthesis)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 36 –

Cholecystokinin (CCK) and Related Peptides (continued)
4201-sCCK-33 (Human)*
Lys-Ala-Pro-Ser-Gly-Arg-Met-Ser-Ile-ValLys-Asn-Leu-Gln-Asn-Leu-Asp-Pro-Ser-HisArg-Ile-Ser-Asp-Arg-Asp-Tyr(SO3H)-Met-Gly-TrpMet-Asp-Phe-NH2-20

(M.W. 3945.4)

Price:Yen

C167H263N51O52S4

Vial

0.1 mg43,000[96827-04-2]

1) Y. Takahashi, K. Kato, Y. Hayashizaki, and K. Matsubara, Proc. Natl. Acad. Sci. U.S.A., 82, 1931 (1987).
(Original; Nucleotide Seq.)
2) Y. Kurano, T. Kimura, and S. Sakakibara, In, Peptides, Proceedings of the 10th American Peptide Symposium,(G.R. Marshall, ed.), ESCOM Science Publishers B.V. 1988, pp.162-165. (Chem. Synthesis)4176-s-20

CCK-33 (Porcine)*
Lys-Ala-Pro-Ser-Gly-Arg-Val-Ser-Met-IleLys-Asn-Leu-Gln-Ser-Leu-Asp-Pro-Ser-HisArg-Ile-Ser-Asp-Arg-Asp-Tyr(SO3H)-Met-Gly-TrpMet-Asp-Phe-NH2(M.W. 3918.4)

C166H262N50O52S4

Vial

0.1 mg43,000[67256-27-3]

1) V. Mutt and J.E. Jorpes, Eur. J. Biochem., 6, 156 (1968). (Original; Partial Structure)2) V. Mutt and J.E. Jorpes, Biochem. J., 125, 57P (1971). (Original)
3) Y. Kurano, T. Kimura, and S. Sakakibara, J. Chem. Soc. Chem. Commun., 5, 323 (1987). (Chem. Synthesis)

Chromogranin A (Human, 286-301 Amide) See Code 4214 on page 117

CINC-1/gro
4233-v-20

CINC-1/gro (Rat)
Cytokine-Induced Neutrophil Chemoattractant-1/
growth-related oncogene (Rat)
Ala-Pro-Val-Ala-Asn-Glu-Leu-Arg-Cys-GlnCys-Leu-Gln-Thr-Val-Ala-Gly-Ile-His-PheLys-Asn-Ile-Gln-Ser-Leu-Lys-Val-Met-ProPro-Gly-Pro-His-Cys-Thr-Gln-Thr-Glu-ValIle-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Glu-AlaCys-Leu-Asp-Pro-Glu-Ala-Pro-Met-Val-GlnLys-Ile-Val-Gln-Lys-Met-Leu-Lys-Gly-ValPro-Lys

Vial

20 µg

30,000(Disulfide bonds between Cys9-Cys35 and Cys11-Cys51)(M.W. 7845.3)

C343H572N98O97S71) K. Watanabe, K. Konishi, M. Fujioka, S. Kinoshita, and H. Nakagawa, J. Biol. Chem., 264, 19559 (1989). (Original)
2) Y. Nishiuchi, M. Tsunemi, S. Kumagaye, S. Kubo, H. Nishio, K. Watanabe, T. Kinoshita, and S. Sakakibara,In, Peptides: Chemistry and Biology (Proceedings of the 12th American Peptide Symposium)(J.A. Smith and J.E. Rivier, eds.), ESCOM, Leiden, 1992, pp.911-913. (Chem. Synthesis)
3) H. Nakagawa, N. Komorita, F. Shibata, A. Ikesue, K. Konishi, M. Fujioka, and H. Kato, Biochem. J., 301, 545 (1994).
(CINC Family)

CNP See page 44 and 45
Cocaine- and Amphetamine-Regulated Transcript (Human, 55-102)
See Code 4350 CART (Human, 55-102) on page 33
Cocaine- and Amphetamine-Regulated Transcript (Rat, 55-102)
See Code 4351 CART (Rat, 55-102) on page 33*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 37 –and Proteins

CompoundBiologically Active Peptides

CodeConantokins
1) W.R. Gray, B.M. Olivera, and L.J. Cruz, Annu. Rev. Biochem., 57, 665 (1988). (Review)2) R.T. Layer, J.D. Wagstaff, and H.S. White, Curr. Med. Chem., 11, 3073 (2004). (Review)

Code

Compound4265-vConantokin G(Marine Snail, Conus geographus)
Gly-Glu-Gla-Gla-Leu-Gln-Gla-Asn-Gln-GlaLeu-Ile-Arg-Gla-Lys-Ser-Asn-NH2-20

Price:Yen
Vial

0.5 mg18,000(Gla: L-γ-Carboxyglutamic acid)(M.W. 2264.2) C88H138N26O44 [93438-65-4]
Purity Information : QZ See page IV (XVI)

Sleeper Peptide / N-methyl-D-Aspartate (NMDA) Receptor Antagonist
1) J.M. McIntosh, B.M. Olivera, L.J. Cruz, and W.R. Gray, J. Biol. Chem., 259, 14343 (1984). (Original)
2) L.G. Hammerland, B.M. Olivera, and D. Yoshikami, Eur. J. Pharmacol., 226, 239 (1992). (Pharmacol.)3) Y. Nishiuchi, M. Nakao, M. Nakata, T. Kimura, and S. Sakakibara, Int. J. Pept. Protein Res., 42, 533 (1993).
(Chem. Synthesis)4264-v-20

Conantokin T(Marine Snail, Conus tulipa)
Gly-Glu-Gla-Gla-Tyr-Gln-Lys-Met-Leu-GlaAsn-Leu-Arg-Gla-Ala-Glu-Val-Lys-Lys-AsnAla-NH2

Vial

0.5 mg21,000(Gla: L-γ-Carboxyglutamic acid)(M.W. 2683.8) C110H175N31O45S
Purity Information : Qx See page IV (XVI)

Sleeper Peptide / N-methyl-D-Aspartate (NMDA) Receptor Antagonist
1) J.A. Haack, J. Rivier, T.N. Parks, E.E. Mena, L.J. Cruz, and B.M. Olivera, J. Biol. Chem., 265, 6025 (1990). (Original)
2) Y. Nishiuchi, M. Nakao, M. Nakata, T. Kimura, and S. Sakakibara, Int. J. Pept. Protein Res., 42, 533 (1993).
(Chem. Synthesis)

Conotoxins
1) B.M. Olivera, W.R. Gray, R. Zeikus, J.M. McIntosh, J. Varga, J. Rivier, V. De Santos, and L.J. Cruz, Science, 230, 1338 (1985).
(Review)
2) W.R. Gray, B.M. Olivera, and L.J. Cruz, Annu. Rev. Biochem., 57, 665 (1988). (Review)3) R.A. Myers, L.J. Cruz, J.E. Rivier, and B.M. Olivera, Chem. Rev., 93, 1923 (1993). (Review)4) B.M. Olivera, G.P. Miljanich, J. Ramachandran, and M.E. Adams, Annu. Rev. Biochem., 63, 823 (1994). (Review)

List of Conotoxins
CodeCompoundα-Conotoxins (ACh-R Blocker)
4126-vα-Conotoxin GI
α-Conotoxin ImI
4311-vα-Conotoxin MI
4140-vα-Conotoxin SI
4228-vµ-Conotoxins (Na+ Channel Blocker)
4217-vµ-Conotoxin GIIIBµ-Conotoxin GS
4263-vµ-Conotoxin SIIIA
4440-vNew
ω-Conotoxins (Ca2+ Channel Blocker)
4161-v
ω-Conotoxin GVIA
ω-Conotoxin MVIIA
4289-v
ω-Conotoxin MVIIC
4283-sω-Conotoxin MVIIC
4283-v
ω-Conotoxin SVIB
4284-v– 38 –

Quantity

Price: Yen

Page

0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial

20,00025,00020,00020,000

39
39
39
39

0.5 mg vial
0.5 mg vial
0.5 mg vial

38,00040,00030,00040
40
40

0.5 mg vial
0.5 mg vial
0.1 mg vial
0.5 mg vial
0.5 mg vial

38,00030,00015,00030,00030,000

41
41
41
41
41

Conotoxins (continued)
4126-vα-Conotoxin GI*(Marine Snail, Conus geographus)-20

Price:Yen
Vial

0.5 mg20,000(Hydrochloride Form)

Glu-Cys-Cys-Asn-Pro-Ala-Cys-Gly-Arg-HisTyr-Ser-Cys-NH2(Disulfide bonds between Cys2-Cys7 and Cys3-Cys13)(M.W. 1437.6) C55H80N20O18S4 [76862-65-2]
Purity Information : QE See page IV (XVI)Blocker for Nicotinic Acetylcholine Receptor
1) W.R. Gray, A. Luque, B.M. Olivera, J. Barrett, and L.J. Cruz, J. Biol. Chem., 256, 4734 (1981). (Original)
2) Y. Nishiuchi and S. Sakakibara, FEBS Lett., 148, 260 (1982). (Chem. Synthesis)4311-v-20

α-Conotoxin ImI(Marine Snail, Conus imperialis)
Gly-Cys-Cys-Ser-Asp-Pro-Arg-Cys-Ala-TrpArg-Cys-NH2

Vial

0.5 mg25,000(Disulfide bonds between Cys2-Cys8 and Cys3-Cys12)(M.W. 1351.6)

C52H78N20O15S4[156467-85-5]

Blocker for Nicotinic Acetylcholine Receptor in Central Nervous System
1) J.M. McIntosh, D. Yoshikami, E. Mahe, D.B. Nielsen, J.E. Rivier, W.R. Gray, and B.M. Olivera, J. Biol. Chem.,
269, 16733 (1994). (Original)
2) D.S. Johnson, J. Martinez, A.B. Elgoyhen, S.F. Heinemann, and J.M. McIntosh, Mol. Pharmacol., 48,194 (1995).
(Pharmacol.)3) E.F.R. Pereira, M. Alkondon, J.M. McIntosh, and E.X. Albuquerque, J. Pharmacol. Exp. Ther., 278, 1472 (1996).
(Pharmacol.; Competitive Antagonist)

4140-v-20

α-Conotoxin MI*(Marine Snail, Conus magus)
Gly-Arg-Cys-Cys-His-Pro-Ala-Cys-Gly-LysAsn-Tyr-Ser-Cys-NH2

Vial

0.5 mg20,000(Disulfide bonds between Cys3-Cys8 and Cys4-Cys14)(M.W. 1493.7)

C58H88N22O17S4Blocker for Nicotinic Acetylcholine Receptor
1) M. McIntosh, L.J. Cruz, M.W. Hunkapiller, W.R. Gray, and B.M. Olivera, Arch. Biochem. Biophys., 218, 329 (1982).
(Original)
2) Y. Nishiuchi and S. Sakakibara, Peptide Chemistry 1983, 191 (1984). (Chem. Synthesis)4228-v-20

α-Conotoxin SI*(Marine Snail, Conus striatus)
Ile-Cys-Cys-Asn-Pro-Ala-Cys-Gly-Pro-LysTyr-Ser-Cys-NH2

Vial

0.5 mg20,000(Disulfide bonds between Cys2-Cys7 and Cys3-Cys13)(M.W. 1353.6)

C55H84N16O16S4Blocker for Nicotinic Acetylcholine Receptor
1) G.C. Zafaralla, C. Ramilo, W.R. Gray, R. Karlstrom, B.M. Olivera, and L.J. Cruz, Biochemistry, 27, 7102 (1988).
(Original)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 39 –and Proteins

CompoundBiologically Active Peptides

CodeConotoxins (continued)
Code

Compound4217-vµ-Conotoxin GIIIB*(Marine Snail, Conus geographus)
Arg-Asp-Cys-Cys-Thr-Hyp-Hyp-Arg-Lys-CysLys-Asp-Arg-Arg-Cys-Lys-Hyp-Met-Lys-CysCys-Ala-NH2-20

Price:Yen
Vial

0.5 mg38,000(Disulfide bonds between Cys3-Cys15, Cys4-Cys20, and Cys10-Cys21)(M.W. 2640.2)

C101H175N39O30S7[140678-12-2]+

Na Channel Blocker : Specific for Skeletal Muscle
1) S. Sato, H. Nakamura, Y. Ohizumi, J. Kobayashi, and Y. Hirata, FEBS Lett., 155, 277 (1983). (Original)
2) L.J. Cruz, W.R. Gray, B.M. Olivera, R.D. Zeikus, L. Kerr, D. Yoshikami, and E. Mocyzydlowski, J. Biol. Chem.,
260, 9280 (1985). (Naming)3) Y. Ohizumi, H. Nakamura, J. Kobayashi, and W.A. Catterall, J. Biol. Chem., 261, 6149 (1986). (Pharmacol.)4) S. Kubo, N. Chino, T.X. Watanabe, T. Kimura, and S. Sakakibara, Pept. Res., 6, 66 (1993).
(Chem. Synthesis & Pharmacol.)4263-v-20

µ-Conotoxin GS(Marine Snail, Conus geographus)
Ala-Cys-Ser-Gly-Arg-Gly-Ser-Arg-Cys-HypHyp-Gln-Cys-Cys-Met-Gly-Leu-Arg-Cys-GlyArg-Gly-Asn-Pro-Gln-Lys-Cys-Ile-Gly-AlaHis-Gla-Asp-Val

Vial

0.5 mg40,000(Gla:L-γ-Carboxyglutamic acid)(Disulfide bonds between Cys2-Cys14, Cys9-Cys19, and Cys13-Cys27)(M.W. 3618.1)

C139H226N52O48S7

Purity Information : QZ See page IV (XVI)

Na+ Channel Blocker
1) Y. Yanagawa, T. Abe, M. Satake, S. Odani, J. Suzuki, and K. Ishikawa, Biochemistry, 27, 6256 (1988). (Original)
2) M. Nakao, Y. Nishiuchi, M. Nakata, T. Kimura, and S. Sakakibara, Lett. Pept. Sci., 2, 17 (1995).
(Chem. Synthesis & S-S Bond)

4440-vNew-20

µ-Conotoxin SIIIA(Marine Snail, Conus striatus)
Pyr-Asn-Cys-Cys-Asn-Gly-Gly-Cys-Ser-SerLys-Trp-Cys-Arg-Asp-His-Ala-Arg-Cys-Cys-NH2

Vial

0.5 mg30,000(Reported disulfide bonds between Cys3-Cys13, Cys4-Cys19, and Cys8-Cys20)(M.W. 2207.5)

C83H123N33O27S6

Tetrodotoxin-Resistant Na+ Channel Blocker with Analgesic Activityµ-Conotoxin SIIIA, isolated from Conus striatus, is a 20 amino acid residue peptide with three intrachain
disulfide bonds1), the solution structure of which was recently determined by NMR2). In contrast to µ-conotoxin
GIIIB (Code 4217-v), this peptide is featured to inhibit tetrodotoxin-resistant Na+ channels in frog sympathetic
and dorsal root ganglia, and rat small-diameter dorsal root ganglia neurons at 0.1-10 µM doses1,3). Later, in
relation to Na+ channel blocking activity, µ-conotoxin SIIIA was found to exhibit analgesic activity in mousewhen injected intraperitoneally (10 nmol per mouse)4).
µ-Conotoxin SIIIA might be a potential research tool for efficient pain modulation.
1) G. Bulaj, P.J. West, J.E. Garrett, M. Marsh, M.-M. Zhang, R.S. Norton, B.J. Smith, D. Yoshikami, and B.M. Olivera,
Biochemistry, 44, 7259 (2005). (Original; Primary Structure & Pharmacol.)2) S. Yao, M.-M. Zhang, D. Yoshikami, L. Azam, B.M. Olivera, G. Bulaj, and R.S. Norton, Biochemistry, 47,
10940 (2008). (Solution Structure, S-S Bond, & Pharmacol.)3) C.-Z. Wang, H. Zhang, H. Jiang, W. Lu, Z.-Q. Zhao, and C.-W. Chi, Toxicon, 47, 122 (2006). (Pharmacol.)4) B.R. Green, P. Catlin, M.-M. Zhang, B. Fiedler, W. Bayudan, A. Morrison, R.S. Norton, B.J. Smith, D. Yoshikami,
B.M. Olivera, and G. Bulaj, Chem. Biol., 14, 399 (2007). (Pharmacol.)*The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 40 –

Conotoxins (continued)
4161-v

ω-Conotoxin GVIA*(Marine Snail, Conus geographus)
Cys-Lys-Ser-Hyp-Gly-Ser-Ser-Cys-Ser-HypThr-Ser-Tyr-Asn-Cys-Cys-Arg-Ser-Cys-AsnHyp-Tyr-Thr-Lys-Arg-Cys-Tyr-NH2-20

Price:Yen
Vial

0.5 mg38,000(Disulfide bonds between Cys1-Cys16, Cys8-Cys19, and Cys15-Cys26)(M.W. 3037.3)

C120H182N38O43S6

2+Channel Blocker

N-type Ca[106375-28-4]

1) B.M. Olivera, J.M. McIntosh, L.J. Cruz, F.A. Luque, and W.R. Gray, Biochemistry, 23, 5087 (1984). (Original)
2) Y. Nishiuchi, K.Y. Kumagaye, Y. Noda, T.X. Watanabe, and S. Sakakibara, Biopolymers, 25, S61 (1986).
(Chem. Synthesis & S-S Bond)4289-v-20

ω-Conotoxin MVIIA*(Marine Snail, Conus magus)
Cys-Lys-Gly-Lys-Gly-Ala-Lys-Cys-Ser-ArgLeu-Met-Tyr-Asp-Cys-Cys-Thr-Gly-Ser-CysArg-Ser-Gly-Lys-Cys-NH2

Vial

0.5 mg30,000(Reported disulfide bonds between Cys1-Cys16, Cys8-Cys20, and Cys15-Cys25)(M.W. 2639.1)

C102H172N36O32S7
2+

Reversible N-type Ca[107452-89-1]

Channel Blocker

1) B.M. Olivera, L.J. Cruz, V. de Santos, G.W. Le Cheminant, D. Griffin, R. Zeikus, J.M. McIntosh, R. Galyean, J. Varga,
W.R. Gray, and J. Rivier, Biochemistry, 26, 2086 (1987). (Original)
2) K. Valentino, R. Newcomb, T. Gadbois, T. Singh, S. Bowersox, S. Binter, A. Justice, D. Yamashiro, B.B. Hoffman,
R. Ciaranello, G. Miljanich, and J. Ramachandran, Proc. Natl. Acad. Sci. U.S.A., 90, 7894 (1993). (Pharmacol.)3) J.A. Fox, Pflu gers Arch., 429, 873 (1995). (Pharmacol.)4283-s-20

ω-Conotoxin MVIIC(Marine Snail, Conus magus)
Cys-Lys-Gly-Lys-Gly-Ala-Pro-Cys-Arg-LysThr-Met-Tyr-Asp-Cys-Cys-Ser-Gly-Ser-CysGly-Arg-Arg-Gly-Lys-Cys-NH2

Vial

0.1 mg15,000Vial

0.5 mg30,000(Disulfide bonds between Cys1-Cys16, Cys8-Cys20, and Cys15-Cys26)(M.W. 2749.3)

4283-v-20

C106H178N40O32S7[147794-23-8]

ω-Conotoxin MVIIC(Marine Snail, Conus magus)
P / Q-type Ca2+ Channel Blocker

1) D.R. Hillyard, V.D. Monje, I.M. Mintz, B.P. Bean, L. Nadasdi, J. Ramachandran, G. Miljanich, A. Azimi-Zoonooz,
J.M. McIntosh, L.J. Crutz, J.S. Imperial, and B.M. Olivera, Neuron, 9, 69 (1992). (Original; cDNA and Pharmacol.)2) M.E. Adams, R.A. Myers, J.S. Imperial, and B.M. Olivera, Biochemistry, 32, 12566 (1993). (Pharmacol.)3) W.A. Sather, T. Tanabe, J.-F. Zhang, Y. Mori, M.E. Adams, and R.W. Tsien, Neuron, 11, 291 (1993). (Pharmacol.)4) D.B. Wheeler, A. Randall, and R.W. Tsien, Science, 264, 107 (1994). (Pharmacol.)4284-v-20

ω-Conotoxin SVIB*(Marine Snail, Conus striatus)
Cys-Lys-Leu-Lys-Gly-Gln-Ser-Cys-Arg-LysThr-Ser-Tyr-Asp-Cys-Cys-Ser-Gly-Ser-CysGly-Arg-Ser-Gly-Lys-Cys-NH2

Vial

0.5 mg30,000(Reported disulfide bonds between Cys1-Cys16, Cys8-Cys20, and Cys15-Cys26)(M.W. 2739.1)

C105H176N38O36S6

2+Channel Blocker

N-type Ca[150433-82-2]

1) C.A. Ramilo, G.C. Zafaralla, L. Nadasdi, L.G. Hammerland, D. Yoshikami, W.R. Gray, R. Kristipati,
J. Ramachandran, G. Miljanich, B.M. Olivera, and L.J. Cruz, Biochemistry, 31, 9919 (1992). (Original)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 41 –and Proteins

CompoundBiologically Active Peptides

CodeList of lon Channel Blockers
Code
2+

Ca

CompoundQuantity

Price: Yen

Channel Blockers

L-type4255-s4310-sCalciseptine
Calcicludine

0.1 mg vial
0.1 mg vial

30,00030,0004161-v
4289-v
4284-v

ω-Conotoxin GVIA
ω-Conotoxin MVIIA
ω-Conotoxin SVIB

0.5 mg vial
0.5 mg vial
0.5 mg vial

38,00030,00030,0004256-s4294-sω-Agatoxin IVA
ω-Agatoxin TK (ω-Agatoxin IVB)

0.1 mg vial
0.1 mg vial

30,00030,0004283-s4283-v

ω-Conotoxin MVIIC
ω-Conotoxin MVIIC

0.1 mg vial
0.5 mg vial

15,00030,0004363-s

SNX-482

0.1 mg vial

30,0004375-s

Kurtoxin(also has Na+ channel blocking activity)

0.1 mg vial

30,0004300-s4247-s

PLTX-II
Agelenin

0.1 mg vial
0.1 mg vial

30,00030,0000.1 mg vial
0.1 mg vial

23,00022,0000.1 mg vial

22,0000.5 mg vial
0.1 mg vial

18,00020,0000.5 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial

25,00022,00022,00030,00030,00022,0000.1 mg vial

15,0000.5 mg vial
0.5 mg vial
0.5 mg vial
0.1 mg vial
0.1 mg vial

38,00040,00030,00022,00020,000Chlorotoxin

0.5 mg vial

45,000GsMTx-4
ProTx-I
Psalmotoxin 1
Purotoxin-1

0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial

22,00022,00023,00022,000N-typeP-typeP/Q-type

R-typeT-typeOthersK+ Channel Blockers
Ca2+-Activated K+ Channel Blockers
BK-type (High conductance)
4235-sIberiotoxin
4259-sKaliotoxin (1-37)
IK-type (Intermediate conductance)
Charybdotoxin
4227-s(also has BK-type blocking activity)
SK-type (Small conductance)
Apamin4257-v
4260-sScyllatoxin (Leiurotoxin I)

Voltage-Dependent K+ Channel Blockers
4258-v
4287-s
4290-s
4313-s4330-s4433-sMCD-Peptide
Stichodactyla Toxin
Margatoxin
Tityustoxin Kα
Dendrotoxin I
Guangxitoxin-1E

Inward-Rectifier K+ Channel Blocker
4364-sTertiapin

Na+ Channel Blockers
New
New
New

4217-v
4263-v
4440-v
4455-s4450-sµ-Conotoxin GIIIBµ-Conotoxin GSµ-Conotoxin SIIIA
Huwentoxin-IV
ProTx-II

Cl- Channel Blocker
4282-v

Other Blockers

New

4393-s4409-s4435-s4457-s– 42 –

Corticotropin Releasing Factor/Hormones (CRF/CRH)

4) M. Schaefer, S.A. Mousa, and C. Stein, Eur. J. Pharmacol., 323, 1 (1997). (Review)

Code

Compound4136-sCRF (Human, Rat)
Corticotropin Releasing Factor (Human, Rat)
CRH / Corticotropin Releasing Hormone (Human, Rat)
Ser-Glu-Glu-Pro-Pro-Ile-Ser-Leu-Asp-LeuThr-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-GluMet-Ala-Arg-Ala-Glu-Gln-Leu-Ala-Gln-GlnAla-His-Ser-Asn-Arg-Lys-Leu-Met-Glu-IleIle-NH2-20

(M.W. 4757.5)

4136-v-20

Price:Yen

C208H344N60O63S2

Vial

0.1 mg12,000Vial

0.5 mg41,000[86784-80-7]

CRF (Human, Rat)
Corticotropin Releasing Factor (Human, Rat)
CRH / Corticotropin Releasing Hormone (Human, Rat)

1) J. Spiess, J. Rivier, and W. Vale, Biochemistry, 22, 4341 (1983). (Original; Rat)
2) S. Shibahara, Y. Morimoto, Y. Furutani, M. Notake, H. Takahashi, S. Shimizu, S. Horikawa, and S. Numa,
EMBO J., 2, 775 (1983). (Original; Human)• This compound is distributed through Peptide Institute, Inc. under the license of The Salk Institute.

4111-s-20

CRF (Ovine)
Corticotropin Releasing Factor (Ovine)
CRH / Corticotropin Releasing Hormone (Ovine)
Ser-Gln-Glu-Pro-Pro-Ile-Ser-Leu-Asp-LeuThr-Phe-His-Leu-Leu-Arg-Glu-Val-Leu-GluMet-Thr-Lys-Ala-Asp-Gln-Leu-Ala-Gln-GlnAla-His-Ser-Asn-Arg-Lys-Leu-Leu-Asp-IleAla-NH2(M.W. 4670.3)

4111-v-20

C205H339N59O63S

Vial

0.1 mg12,000Vial

0.5 mg41,000[79804-71-0]

CRF (Ovine)
Corticotropin Releasing Factor (Ovine)
CRH / Corticotropin Releasing Hormone (Ovine)

1) W. Vale, J. Spiess, C. Rivier, and J. Rivier, Science, 213, 1394 (1981). (Original)• This compound is distributed through Peptide Institute, Inc. under the license of The Salk Institute.

4141-s-20

Tyrosyl-CRF (Human, Rat)
Vial
0.1 mgTyrosyl-Corticotropin Releasing Factor (Human, Rat)
Tyrosyl-CRH / Tyrosyl-Corticotropin Releasing Hormone (Human, Rat)
Tyr-Ser-Glu-Glu-Pro-Pro-Ile-Ser-Leu-AspLeu-Thr-Phe-His-Leu-Leu-Arg-Glu-Val-LeuGlu-Met-Ala-Arg-Ala-Glu-Gln-Leu-Ala-GlnGln-Ala-His-Ser-Asn-Arg-Lys-Leu-Met-GluIle-Ile-NH2

14,000(M.W. 4920.6) C217H353N61O65S2 [100513-58-4]
Purity Information : QX See page IV (XVI)For Radioimmunoassay
1) P.C. Wynn, G. Aguilera, J. Morell, and K.J. Catt, Biochem. Biophys. Res. Commun., 110, 602 (1983). (Biochem.)• This compound is distributed through Peptide Institute, Inc. under the license of The Salk Institute.

– 43 –and Proteins3) M.J. Owens and C.B. Nemeroff, Pharmacol. Rev., 43, 425 (1991). (Review)

Biologically Active Peptides

1) C.L. Rivier and P.M. Plotsky, Annu. Rev. Physiol., 48, 475 (1986). (Review)2) F.A. Antoni, Endocrinol. Rev., 7, 351 (1986). (Review)

Cortistatin
Code

Compound4329-v

Cortistatin (Rat)
CST-14 (Rat)
Pro-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-PheSer-Ser-Cys-Lys-20

Price:Yen
Vial

0.5 mg15,000(Disulfide bond between Cys2-Cys13)(M.W. 1721.0)

C81H113N19O19S2

Neuronal Depressant and Sleep-Modulating Peptide
1) L. de Lecea, J.R. Criado, O. Prospero-Garcia, K.M. Gautvik, P. Schweitzer, P.E. Danielson, C.L.M. Dunlop,
G.R. Siggins, S.J. Henriksen, and J.G. Sutcliffe, Nature, 381, 242 (1996). (Original)
2) L. de Lecea, J.A. del Rio, J.R. Criado, S. Alcantara, M. Morales, P.E. Danielson, S.J. Henriksen, E. Soriano, andJ.G. Sutcliffe, J. Neurosci., 17, 5868 (1997). (Biochem.)
3) M. Connor, S.L. Ingram, and M.J. Christie, Br. J. Pharmacol., 122, 1567 (1997). (Pharmacol.)4) A.D. Spier and L. de Lecea, Brain Res. Rev., 33, 228 (2000). (Review)

C-type Natriuretic Peptides (CNP)
1) A. Rosenzweig and C.E. Seidman, Annu. Rev. Biochem., 60, 229 (1991). (Review)4229-v-20

CNP-22 (Human)*C-type Natriuretic Peptide-22 (Human)(Porcine, Rat, Mouse)
Gly-Leu-Ser-Lys-Gly-Cys-Phe-Gly-Leu-LysLeu-Asp-Arg-Ile-Gly-Ser-Met-Ser-Gly-LeuGly-Cys

Vial

0.5 mg36,000(Disulfide bond between Cys6-Cys22)(M.W. 2197.6)

C93H157N27O28S3[127869-51-6]

1) T. Sudoh, N. Minamino, K. Kangawa, and H. Matsuo, Biochem. Biophys. Res. Commun., 168, 863 (1990).
(Original; Porcine)2) Y. Tawaragi, K. Fuchimura, S. Tanaka, N. Minamino, K. Kangawa, H. Matsuo, Biochem. Biophys. Res. Commun.,
175, 645 (1991). (cDNA Seq.; Human)3) M. Kojima, N. Minamino, K. Kangawa, and H. Matsuo, FEBS Lett., 276, 209 (1990). (cDNA Seq.; Rat)
4) Y. Ogawa, H. Itoh, Y. Yoshitake, M. Inoue, T. Yoshimasa, T. Serikawa, K. Nakao, Genomics, 24, 383 (1994).
(Nucleotide Seq.; Mouse)

4241-s-20

CNP-53 (Human)*C-type Natriuretic Peptide-53 (Human)
Asp-Leu-Arg-Val-Asp-Thr-Lys-Ser-Arg-AlaAla-Trp-Ala-Arg-Leu-Leu-Gln-Glu-His-ProAsn-Ala-Arg-Lys-Tyr-Lys-Gly-Ala-Asn-LysLys-Gly-Leu-Ser-Lys-Gly-Cys-Phe-Gly-LeuLys-Leu-Asp-Arg-Ile-Gly-Ser-Met-Ser-GlyLeu-Gly-Cys

Vial

0.1 mg28,000(Disulfide bond between Cys37-Cys53)(M.W. 5801.7)

C251H417N81O71S3[141294-77-1]

1) Y. Tawaragi, K. Fuchimura, S. Tanaka, N. Minamino, K. Kangawa, and H. Matsuo, Biochem. Biophys. Res.
Commun., 175, 645 (1991). (Original)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 44 –

C-type Natriuretic Peptides (CNP) (continued)
4240-s

CNP-53 (Porcine, Rat)*
C-type Natriuretic Peptide-53 (Porcine, Rat)
Asp-Leu-Arg-Val-Asp-Thr-Lys-Ser-Arg-AlaAla-Trp-Ala-Arg-Leu-Leu-His-Glu-His-ProAsn-Ala-Arg-Lys-Tyr-Lys-Gly-Gly-Asn-LysLys-Gly-Leu-Ser-Lys-Gly-Cys-Phe-Gly-LeuLys-Leu-Asp-Arg-Ile-Gly-Ser-Met-Ser-GlyLeu-Gly-Cys-20

Price:Yen
Vial

0.1 mg28,000and Proteins

Compound(Disulfide bond between Cys37-Cys53)(M.W. 5796.7)

C251H414N82O70S3

1) N. Minamino, K. Kangawa, and H. Matsuo, Biochem. Biophys. Res. Commun., 170, 973 (1990). (Original; Porcine)2) Y. Tawaragi, K. Fuchimura, H. Nakazato, S. Tanaka, N. Minamino, K. Kangawa, and H. Matsuo, Biochem. Biophys.
Res. Commun., 172, 627 (1990). (Original; Porcine Nucleotide Seq.)
3) M. Kojima, N. Minamino, K. Kangawa, and H. Matsuo, FEBS Lett., 276, 209 (1990). (Original; Rat cDNA)

4251-v-20

Tyrosyl-CNP-22 (Human)*Tyrosyl-C-type Natriuretic Peptide-22 (Human)
Tyr-Gly-Leu-Ser-Lys-Gly-Cys-Phe-Gly-LeuLys-Leu-Asp-Arg-Ile-Gly-Ser-Met-Ser-GlyLeu-Gly-Cys

Vial

0.5 mg43,000(Disulfide bond between Cys6-Cys22)(M.W. 2360.8)

C102H166N28O30S3[142878-79-3]

For Radioimmunoassay
1) J. Brown and Z. Zuo, Am. J. Physiol., 266, R1383 (1994). (Pharmacol.)2) J. Zhao, N. Ardaillou, C.-Y. Lu, S. Placier, P. Pham, L. Badre, J. Cambar, and R. Ardaillou, Kidney Int., 46, 717 (1994).
(Pharmacol.)cyclo (Arg-Gly-Asp-D-Phe-Val) See Code 4304 on page 23
Decorsin See Code 4269 on page 23*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

Defensins
1) R.I. Lehrer and T. Ganz, Ann. N. Y. Acad. Sci., 797, 228 (1996). (Review)2) M. Zasloff, Nature, 415, 389 (2002). (Review)
3) T. Hirsch, F. Jacobsen, H.-U. Steinau, and L. Steinstraesser, Protein Pept. Lett., 15, 238 (2008). (Review)4) M. Pazgier, X. Li, W. Lu, and J. Lubkowski, Curr. Pharm. Des., 13, 3096 (2007). (Review)5) Y.P. Lai and R.L. Gallo, Trends Immunol., 30,131 (2009). (Review)

List of Defensins

New
New

Code

CompoundQuantity

Price: Yen

Page4271-s4428-s4416-s4431-s4415-s4458-s4337-s4338-s4382-s
4406-sα-Defensin-1 (Human) HNP–1
α-Defensin-2 (Human) HNP–2
α-Defensin-3 (Human) HNP–3
α-Defensin-4 (Human) HNP-4
α-Defensin-5 (Human) HD–5
α-Defensin-6 (Human) HD-6β-Defensin-1 (Human) hBD–1
β-Defensin-2 (Human) hBD–2
β-Defensin-3 (Human) hBD–3
β-Defensin-4 (Human) hBD–4

0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial

20,00020,00020,00022,00022,00022,00022,00023,00024,00022,000

46
46
47
48
49
50
51
51
52
53

– 45 –

Biologically Active Peptides

CodeDefensins (continued)
Code

Compound4271-sα-Defensin-1 (Human)
HNP-1 (Human Neutrophil Peptide-1)
Ala-Cys-Tyr-Cys-Arg-Ile-Pro-Ala-Cys-IleAla-Gly-Glu-Arg-Arg-Tyr-Gly-Thr-Cys-IleTyr-Gln-Gly-Arg-Leu-Trp-Ala-Phe-Cys-Cys-20

Price:Yen
Vial

0.1 mg20,000(Disulfide bonds between Cys2-Cys30, Cys4-Cys19, and Cys9-Cys29)(M.W. 3442.0)

C150H222N44O38S6

Antimicrobial Peptide / Chemoattractant for Monocytes
1) T. Ganz, M.E. Selsted, D. Szklarek, S.S.L. Harwig, K. Daher, D.F. Bainton, and R.I. Lehrer, J. Clin. Invest.,
76, 1427 (1985). (Original; Isolation)2) M.E. Selsted, S.S.L. Harwig, T. Ganz, J.W. Schilling, and R.I. Lehrer, J. Clin. Invest., 76, 1436 (1985).
(Original; Structure)3) S. Kubo, K. Tanimura, H. Nishio, N. Chino, T. Teshima, T. Kimura, and Y. Nishiuchi, Int. J. Pept. Res. Ther.,14, 341 (2008). (Chem. Synthesis & Pharmacol.)4428-s-20

α-Defensin-2 (Human)
HNP-2 (Human Neutrophil Peptide-2)
Cys-Tyr-Cys-Arg-Ile-Pro-Ala-Cys-Ile-AlaGly-Glu-Arg-Arg-Tyr-Gly-Thr-Cys-Ile-TyrGln-Gly-Arg-Leu-Trp-Ala-Phe-Cys-Cys

Vial

0.1 mg20,000(Disulfide bonds between Cys1-Cys29, Cys3-Cys18, and Cys8-Cys28)(M.W. 3371.0)

C147H217N43O37S6

Antimicrobial Peptide
Human α-defensins are composed of 6 peptides: 4 human neutrophil peptides [HNP-1 (Code 4271-s),
HNP-2, HNP-3 (Code 4416-s), and HNP-4 (Code 4431-s)] and 2 human defensins [HD-5 (Code 4415-s) andHD-6 (Code 4458-s)]. Among them, the primary structures of HNP-1, HNP-2 and HNP-3 differ only at theamino-terminal residue, in which the first residue is Ala for HNP-1 and Asp for HNP-3, whereas HNP-2 lacks
this position, resulting in the 29-residue peptide1,2). Recent studies by mass spectroscopic analysis clarified that
HNP-2 is the second major component in squamous cell carcinoma of human tongue3) and gingival crevicular
fluid from periodontitis patients and healthy controls4), where HNP-1 is the most abundant and HNP-3 is theleast. Taking this fact into account, it is speculated that HNP-2 is produced post-translationally from HNP-3.
Concerning the activity, HNP-2 is revealed to be as active as HNP-1 in neutralizing anthrax lethal toxin5) andblocking papillomavirus infection6), although some differences were pointed out in the candidacidal activity
among HNPs7).
1) T. Ganz, M.E. Selsted, D. Szklarek, S.S.L. Harwig, K. Daher, D.F. Bainton, and R.I. Lehrer, J. Clin. Invest., 76, 1427
(1985). (Original; Isolation)2) M.E. Selsted, S.S.L. Harwig, T. Ganz, J.W. Schilling, and R.I. Lehrer, J. Clin. Invest., 76, 1436 (1985).
(Original; Structure)3) F.T. Lundy, D.F. Orr, J.R. Gallagher, P. Maxwell, C. Shaw, S.S. Napier, C.G. Cowan, P.-J. Lamey, and J.J. Marley, Oral
Oncol., 40, 139 (2004). (Pharmacol.; HNP in Squamous Cell Carcinoma)
4) F.T. Lundy, D.F. Orr, C. Shaw, P.-J. Lamey, and G.J. Linden, Mol. Immunol., 42, 575 (2005). (Pharmacol.; HNP in
Gingival Crevicular Fluid)5) C. Kim, N. Gajendran, H.-W. Mittru
ker, M. Weiwad, Y-H. Song, R. Hurwitz, M. Wilmanns, G. Fischer, and S.H.E.
Kaufmann, Proc. Natl. Acad. Sci., U.S.A., 102, 4830 (2005). (Pharmacol.; Neutralization of Anthrax Lethal Toxin)6) C.B. Buck, P.M. Day, C.D. Thompson, J. Lubkowski, W. Lu, D.R. Lowy, and J.T. Schiller, Proc. Natl. Acad. Sci.,
U.S.A., 103, 1516 (2006). (Pharmacol.; Inhibition of Papillomavirus Infection)7) R.I. Lehrer, T. Ganz, D. Szklarek, and M.E. Selsted, J. Clin. Invest., 81, 1829 (1988). (Pharmacol.; Activity differencein HNP)
8) S. Kubo, K. Tanimura, H. Nishio, N. Chino, T. Teshima, T. Kimura, and Y. Nishiuchi, Int. J. Pept. Res. Ther., 14, 341(2008). (Chem. Synthesis & Pharmacol.)– 46 –

Defensins (continued)
4416-sα-Defensin-3 (Human)
HNP-3 (Human Neutrophil Peptide-3)
Asp-Cys-Tyr-Cys-Arg-Ile-Pro-Ala-Cys-IleAla-Gly-Glu-Arg-Arg-Tyr-Gly-Thr-Cys-IleTyr-Gln-Gly-Arg-Leu-Trp-Ala-Phe-Cys-Cys-20

Price:Yen
Vial

0.1 mg20,000(Disulfide bonds between Cys2-Cys30, Cys4-Cys19, and Cys9-Cys29)(M.W. 3486.0)

C151H222N44O40S6

Antimicrobial Peptide
HNP-1 to HNP-3 are the major components in azophilic granules of human neutrophils1, 2). The primarystructures of HNP-1 to HNP-3 differ by only one amino acid residue at position 1; HNP-2 corresponds topositions 2 through 30 of HNP-1 (des-Ala1-HNP-1) while HNP-3 is Asp1-HNP-1. Interesting publications using
HNP include: i) HNP-1 to HNP-3 may show anti-HIV-1 activity3), and ii) HNP-1 to HNP-3 are overexpressed insquamous cell carcinomas of the human tongue, representing a possible role in innate host defense against
tumor invasion 4) . It has been reported that expression of HNP-1 to HNP-3 is not upregulated bylipopolysaccharide5), while they locate in intestinal epithelial cells in cases of inflammatory bowel disease6).
1) T. Ganz, M.E. Selsted, D. Szklarek, S.S.L. Harwig, K. Daher, D.F. Bainton, and R.I. Lehrer, J. Clin. Invest.,
76, 1427 (1985). (Original; Isolation of HNP 1-3)
2) M.E. Selsted, S.S.L. Harwig, T. Ganz, J.W. Schilling, and R.I. Lehrer, J. Clin. Invest., 76, 1436 (1985).
(Original; Structure of HNP 1-3)
3) C.E. Mackewicz, J. Yuan, P. Tran, L. Diaz, E. Mack, M.E. Selsted, and J.A. Levy, AIDS, 17, F23 (2003). (Pharmacol.;Anti–HIV–1 Activity)
4) F.T. Lundy, D.F. Orr, J.R. Gallagher, P. Maxwell, C. Shaw, S.S. Napier, C.G. Cowan, P.-J. Lamey, and J.J. Marley,
Oral Oncol., 40, 139 (2004). (Pharmacol.; Role in Tumor Invasion)5) X.-M. Fang, Q. Shu, Q.-X. Chen, M. Book, H.-G. Sahl, A. Hoeft, and F. Stuber, Eur. J. Clin. Invest., 33, 82 (2003).
(Histochem.; Regulation of Expression)6) R.N. Cunliffe, Mol. Immunol., 40, 463 (2003). (Histochem.; α -Defensin in Gastrointestinal Tract)7) S. Kubo, K. Tanimura, H. Nishio, N. Chino, T. Teshima, T. Kimura, and Y. Nishiuchi, Int. J. Pept. Res. Ther., 14, 341(2008). (Chem. Synthesis & Pharmacol.)– 47 –and Proteins

CompoundBiologically Active Peptides

CodeDefensins (continued)
Code

Compound4431-sα-Defensin-4 (Human)
HNP-4 (Human Neutrophil Peptide-4)
Val-Cys-Ser-Cys-Arg-Leu-Val-Phe-Cys-ArgArg-Thr-Glu-Leu-Arg-Val-Gly-Asn-Cys-LeuIle-Gly-Gly-Val-Ser-Phe-Thr-Tyr-Cys-CysThr-Arg-Val

New

-20

Price:Yen
Vial

0.1 mg22,000(Disulfide bonds between Cys2-Cys30, Cys4-Cys19, and Cys9-Cys29)(M.W. 3709.4)

C157H255N49O43S6

Antimicrobial Peptide
Four α-defensins in neutrophils are called human neutrophil peptide-1 (HNP-1) to HNP-4, in which primarystructures of HNP-1 to HNP-3 are similar; Ala and Asp are the first residue of HNP-1 (Code 4271) and HNP-3(Code 4416), respectively, whereas HNP-2 (Code 4428) lacks the corresponding amino acid residue at position
1. In contrast to these HNPs, α-defensin-4 (HNP-4) shows marked difference in its primary structure although
all six Cys residues are conserved1,2).
Activities of HNP-4 reported so far include: i) inhibition of the ACTH action in rat adrenal cell suspension(ID50 = 7.0 X 10-7 M)1), ii) distinct antimicrobial activity3,4), iii) antiviral activity against X4 and R5 HIV-1
strains5), and iv) inhibition of Bacillus anthracis lethal factor (IC50 = 811 nM)6). In the HIV-1 inhibition, it is
proposed that HNP-4 exerts the activity by the lectin-independent property with CD4 and/or gp120, which isdifferent from that of HNP-1 to HNP-35).
Although the research using HNP-4 seems to be relatively slowly proceeding at moment, partly because
HNP-4 is a minor component in the granulocytes HNPs, our synthetic HNP-4 will contribute significantly toclarify the total activity of HNPs in the body.
1) A. Singh, A. Bateman, Q. Zhu, S. Shimasaki, F. Esch, and S. Solomon, Biochem. Biophys. Res. Commun., 155, 524(1988). (Original; Primary Structure / Anti-ACTH Activity)
2) C.G. Wilde, J.E. Griffith, M.N. Marra, J.L. Snable, and R.W. Scott, J. Biol. Chem., 264, 11200 (1989).
(Original; Structure / HNP-4 / Antimicrobial Activity)
3) Z. Wu, B. Ericksen, K. Tucker, J. Lubkowski, and W. Lu, J. Pept. Res., 64, 118 (2004).
(Pharmacol; Antimicrobial Activity)
4) B. Ericksen, Z. Wu, W. Lu, and R.I. Lehrer, Antimicrob. Agents Chemother., 49, 269 (2005).
(Pharmacol; Antimicrobial Activity)
5) Z. Wu, F. Cocchi, D. Gentles, B. Ericksen, J. Lubkowski, A. DeVico, R.I. Lehrer, and W. Lu, FEBS Lett., 579, 162(2005). (Pharmacol.; HIV-1 Inhibitory Activity)
6) G. Wei, E. de Leeuw, M. Pazgier, W. Yuan, G. Zou, J. Wang, B. Ericksen, W.-Y. Lu, R.I. Lehrer, and W. Lu,
J. Biol. Chem., 284, 29180 (2009). (Pharmacol.;Iinhibition of Bacillus anthracis Lethal Factor)– 48 –

Defensins (continued)
4415-sα-Defensin-5 (Human)
HD-5 (Human Defensin-5)
Ala-Thr-Cys-Tyr-Cys-Arg-Thr-Gly-Arg-CysAla-Thr-Arg-Glu-Ser-Leu-Ser-Gly-Val-CysGlu-Ile-Ser-Gly-Arg-Leu-Tyr-Arg-Leu-CysCys-Arg-20

Price:Yen
Vial

0.1 mg22,000(Disulfide bonds between Cys3-Cys31, Cys5-Cys20, and Cys10-Cys30)(M.W. 3582.1)

C144H238N50O45S6

Antimicrobial Peptide in Paneth Cells
HD-5 is expressed in Paneth cells in intestinal epithelium, thus, falls into a distinct subclass of humanα-defensin1, 2). The in vivo role of HD-5 was studied in transgenic mouse models injected by an HD-5
minigene, confirming that HD-5 expression was specific to Paneth cells and resulted in resistance to bacterial
challenge3). In patients with HIV-related cryptosporidiosis, HD-5 immunoreactivity was reduced in association
with Paneth cell granule depletion4). In inflammatory bowel disease, HD-5 was expressed in metaplastic
Paneth cells in the colon5). These evidences together point to HD-5 as being an essential factor in the defense
against intestinal inflammation.
1) D.E. Jones and C.L. Bevins, J. Biol. Chem., 267, 23216 (1992). (Original; Human Defensin-5)2) E.M. Porter, M.A. Poles, J.S. Lee, J. Naitoh, C.L. Bevins, amd T. Ganz, FEBS Lett., 434, 272 (1998).
(Pharmacol.; Endogenous Form)
3) N.H. Salzman, D. Ghosh, K.M. Huttner, Y. Paterson, and C.L. Bevins, Nature, 422, 522 (2003). (Pharmacol.)4) P. Kelly, R. Feakins, P. Domizio, J. Murphy, C. Bevins, J. Wilson, G. Mcphail, R. Poulsom, and W. Dhaliwal,
Clin. Exp. Immunol., 135, 303 (2004). (Histochem.; Location in AIDS Patients)
5) R.N. Cunliffe, Mol. Immunol., 40, 463 (2003). (Histochem.; α -Defensin in Gastrointestinal Tract)6) S. Kubo, K. Tanimura, H. Nishio, N. Chino, T. Teshima, T. Kimura, and Y. Nishiuchi, Int. J. Pept. Res. Ther., 14,341 (2008). (Chem. Synthesis & Pharmacol.)– 49 –and Proteins

CompoundBiologically Active Peptides

CodeDefensins (continued)
Code

Compound4458-sα-Defensin-6 (Human)
HD-6 (Human Defensin-6)
Ala-Phe-Thr-Cys-His-Cys-Arg-Arg-Ser-CysTyr-Ser-Thr-Glu-Tyr-Ser-Tyr-Gly-Thr-CysThr-Val-Met-Gly-Ile-Asn-His-Arg-Phe-CysCys-Leu

New

-20

Price:Yen
Vial

0.1 mg22,000(Disulfide bonds between Cys4-Cys31, Cys6-Cys20, and Cys10-Cys30)(M.W. 3708.2)

C156H228N46O46S7

Antimicrobial Peptide in Paneth Cells
Six α-defensins have been identified in the human; four of which are found in neutrophiles and thus named
human neutrophil peptide-1 (HNP-1, Code 4271-s), HNP-2 (Code 4428-s), HNP-3 (Code 4416-s) and HNP-4(Code 4431-s). The remaining two are called human defensin-5 (HD-5, Code 4415-s) and human defensin-6(HD-6)1), which are identified in intestinal Paneth cells.
HD-6 was isolated from ileal neobladder urine as a 32-residue peptide2). It appeared in the initial study that
HD-6 was practically inactive against some bacteria and fungi3). However, the experimental results proving
HD-6 to be an antimicrobial peptide have been accumulating: i) Helicobacter pylori infection increases HD-6
expression in the fundus4), ii) HD-6 inhibits herpes simplex virus infection5), iii) HD-6 has influenza A virus
neutralizing ability6), and iv) the HD-6 level is reduced in small intestinal Crohn's disease7). In contrast to these
positive effects in the host defense system, Neisseria gonorrhoeae-induced HD-6 enhances HIV infectivity,
showing how complex HD-6 activity may be8).
Anyhow, these specific characteristics observed in HD-6 are attractive in the study of human innate
immunity.
1) D.E. Jones and C.L. Bevins, FEBS Lett., 315, 187 (1993). (Original; mRNA Seq.)
2) E.M. Porter, M.A. Poles, J.S. Lee, J. Naitoh, C.L. Bevins, and T. Ganz, FEBS Lett., 434, 272 (1998). (Endogenous Form)
3) B. Ericksen, Z. Wu, W. Lu, and R.I. Lehrer, Antimicrob. Agents Chemother., 49, 269 (2005).
(Pharmacol.; No Antibacterial Activity)
4) J. Wehkamp, K. Schmidt, K.R. Herrlinger, S. Baxmann, S. Behling, C. Wohlschlager, A.C. Feller, E.F. Stange, and
K. Fellermann, J. Clin. Pathol., 56, 352 (2003). (Pharmacol.; Enhanced Expression in Helicobacter pylori Infection)5) E. Hazrati, B. Galen, W. Lu, W. Wang, Y. Ouyang, M.J. Keller, R.I. Lehrer. and B.C. Herold, J. Immunol., 177, 8658
(2006). (Pharmacol.; Inhibition of Herpes Simplex Virus Infection)6) M. Doss, M.R. White, T. Tecle, D. Gantz, E.C. Crouch, G. Jung, P. Ruchala, A.J. Waring, R.I. Lehrer,
and K.L. Hartshorn, J. Immunol., 182, 7878 (2009). (Pharmacol.; Influenza A Virus Neutralizing Activity)7) M.J. Koslowski, J. Beisner, E.F. Stange, and J. Wehkamp, Int. J. Med. Microbiol., 300, 34 (2010).
(Minireview; Antimicrobial Host Defense in Small Intestinal Crohn's Disease)8) M.E. Klotman, A. Rapista, N. Teleshova, A. Micsenyi, G.A. Jarvis, W. Lu, E. Porter, and T.L. Chang, J. Immunol., 180,
6176 (2008). (Pharmacol.; Enhancement of HIV Infectivity)– 50 –

Defensins (continued)
4337-sβ-Defensin-1 (Human)
hBD-1
Asp-His-Tyr-Asn-Cys-Val-Ser-Ser-Gly-GlyGln-Cys-Leu-Tyr-Ser-Ala-Cys-Pro-Ile-PheThr-Lys-Ile-Gln-Gly-Thr-Cys-Tyr-Arg-GlyLys-Ala-Lys-Cys-Cys-Lys-20

Price:Yen
Vial

0.1 mg22,000(Disulfide bonds between Cys5-Cys34, Cys12-Cys27, and Cys17-Cys35)(M.W. 3928.5)

C167H256N48O50S6

Antimicrobial Peptide
1) K.W. Bensch, M. Raida, H.-J. Ma
gert, P. Schulz-Knappe, and W.-G. Forssmann, FEBS Lett., 368, 331 (1995).
(Original)
2) M.J. Goldman, G.M. Anderson, E.D. Stolzenberg, U.P. Kari, M. Zasloff, and J.M. Wilson, Cell, 88, 553 (1997).
(Pharmacol.; Inactivated in Cystic Fibrosis)
3) T. Hiratsuka, M. Nakazato, T. Ihi, T. Minematsu, N. Chino, T. Nakanishi, A. Shimizu, K. Kangawa, and S. Matsukura,
Nephron, 85, 34 (2000). (Pharmacol.)4) N. Chino, S. Kubo, H. Nishio, Y. Nishiuchi, M. Nakazato, and T. Kimura, Int. J. Pept. Res. Ther., 12, 203 (2006).
(Chem. Synthesis & Pharmacol.)4338-s-20

β-Defensin-2 (Human)
hBD-2
Gly-Ile-Gly-Asp-Pro-Val-Thr-Cys-Leu-LysSer-Gly-Ala-Ile-Cys-His-Pro-Val-Phe-CysPro-Arg-Arg-Tyr-Lys-Gln-Ile-Gly-Thr-CysGly-Leu-Pro-Gly-Thr-Lys-Cys-Cys-Lys-LysPro

Vial

0.1 mg23,000(Disulfide bonds between Cys8-Cys37, Cys15-Cys30, and Cys20-Cys38)(M.W. 4328.2)

C188H305N55O50S6

Antimicrobial Peptide Specific for Gram-Negative Bacteria / Also Effective for Candida albicans
1) J. Harder, J. Bartels, E. Christophers, and J.-M. Schroder, Nature, 387, 861 (1997). (Original)
2) T. Hiratsuka, M. Nakazato, Y. Date, J. Ashitani, T. Minematsu, N. Chino, and S. Matsukura, Biochem. Biophys. Res.
Commun., 249, 943 (1998). (Pharmacol.)3) D.M. Hoover, K.R. Rajashankar, R. Blumenthal, A. Puri, J.J. Oppenheim, O. Chertov, and J. Lubkowski,
J. Biol. Chem., 275, 32911 (2000). (S-S Bond)
4) T. Hiratsuka, H. Mukae, H. Iiboshi, J. Ashitani, K. Nabeshima, T. Minematsu, N. Chino, T. Ihi, S. Kohno,
and M. Nakazato, Thorax, 58, 425 (2003). (Pharmacol.; Activity against Pseudomonas aeruginosa)5) S. Yanagi, J.-i. Ashitani, H. Ishimoto, Y. Date, H. Mukae, N. Chino, and M. Nakazato, Respiratory Res., 6, 130 (2005).
(Pharmacol. & Immunohistochem.)
6) N. Chino, S. Kubo, H. Nishio, Y. Nishiuchi, M. Nakazato, and T. Kimura, Int. J. Pept. Res. Ther., 12, 203 (2006).
(Chem. Synthesis & Pharmacol.)– 51 –and Proteins

CompoundBiologically Active Peptides

CodeDefensins (continued)
Code

Compound4382-sβ-Defensin-3 (Human)
hBD-3
Gly-Ile-Ile-Asn-Thr-Leu-Gln-Lys-Tyr-TyrCys-Arg-Val-Arg-Gly-Gly-Arg-Cys-Ala-ValLeu-Ser-Cys-Leu-Pro-Lys-Glu-Glu-Gln-IleGly-Lys-Cys-Ser-Thr-Arg-Gly-Arg-Lys-CysCys-Arg-Arg-Lys-Lys-20

Price:Yen
Vial

0.1 mg24,000(Disulfide bonds between Cys11-Cys40, Cys18-Cys33, and Cys23-Cys41)(M.W. 5155.1)

C216H371N75O59S6

Antimicrobial Peptide / Staphylococcus aureus-Killing Factor
The human defensins represent an important family of antimicrobial peptides. They are composed of two
subclasses: α-defensins and β-defensins (hBD), which are characterized by their distinct arrangement of three
disulfide bonds. Following the discovery of hBD-1 (Code 4337-s) and hBD-2 (Code 4338-s) in 1995 and 1997,
respectively, hBD-3 was included in 20011).
hBD-3 was identified in lesional psoriatic scales, from which hBD-2 was also isolated. Peptide and DNA
chemistry revealed hBD-3 to be a 45 amino acid residue peptide. The antimicrobial activity of hBD-3 ischaracterized by: i) a broad spectrum of antimicrobial activity against many pathogenic microbes such as
multi-resistant Staphylococcus aureus and vancomycin-resistant Enterococcus faecium without hemolytic
activity, ii) salt-insensitivity up to 200 mM NaCl, iii) expression of activity through cell wall perforation, and iv)
regulation by TNF- α and contact with bacteria 1) . Later, although the data was obtained using theamino-terminally truncated peptide, hBD-3 (6-45), the following interesting findings were reported: i) hBD-3 isstimulated by interferon-γ, and ii) hBD-3 has monocyte activating function and elicits ion channel activity2). It isalso reported that unlike hBD-1 and hBD-2, hBD-3 mRNA expression is inhibited by corticosteroids3).
Significant amounts of these peptides are distributed in the following tissues: skin, tonsil, trachea, placenta,
testis, thymus, and heart 1,2,4). With respect to the structural aspects of hBD-3, an amphipathic dimeric structure
was proposed in solution, which is different from those of hBD-1 and hBD-2. This might be responsible for thebactericidal activity against Staphylococcus aureus 5).
Thus, the hBD-3, as well as the other defensins, are useful tools for understanding their defense mechanisms
against various microorganisms.
1) J. Harder, J. Bartels, E. Christophers, and J.-M. Schroder, J. Biol. Chem., 276, 5707 (2001). (Original)
2) J.-R.C. Garc́a, F. Jaumann, S. Schulz, A. Krause, J. Rodr́nguez-Jiménez, U. Forssmann, K. Adermann, E. Klu
ver,
C. Vogelmeier, D. Becker, R. Hedrich, W.-G. Forssmann, and R. Bals, Cell Tissue Res., 306, 257 (2001).
(Original; Amino-Terminally Truncated Peptide)3) L.A. Duits, M. Rademaker, B. Ravensbergen, M.A.J.A. van Sterkenburg, E. van Strijen, P.S. Hiemstra, and
P.H. Nibbering, Biochem. Biophys. Res. Commun., 280, 522 (2001). (Pharmacol.)4) H.P. Jia, B.C. Schutte, A. Schudy, R. Linzmeier, J.M. Guthmiller, G.K. Johnson, B.F. Tack, J.P. Mitros, A. Rosenthal,
T. Ganz, and P.B. McCray, Jr., Gene, 263, 211 (2001). (DNA Seq. / Tissue Distribution)5) D.J. Schibli, H.N. Hunter, V. Aseyev, T.D. Starner, J.M. Wiencek, P.B. McCray, Jr., B.F. Tack, and H.J. Vogel,
J. Biol. Chem., 277, 8279 (2002). (Solution Structure)6) S. Yanagi, J.-i. Ashitani, H. Ishimoto, Y. Date, H. Mukae, N. Chino, and M. Nakazato, Respiratory Res., 6, 130 (2005).
(Pharmacol. & Immunohistochem.)
7) N. Chino, S. Kubo, H. Nishio, Y. Nishiuchi, M. Nakazato, and T. Kimura, Int. J. Pept. Res. Ther., 12, 203 (2006).
(Chem. Synthesis & Pharmacol.)– 52 –

Defensins (continued)
4406-sβ-Defensin-4 (Human)
hBD-4
Prepro-hBD-4 (Human, 25-61)
Glu-Leu-Asp-Arg-Ile-Cys-Gly-Tyr-Gly-ThrAla-Arg-Cys-Arg-Lys-Lys-Cys-Arg-Ser-GlnGlu-Tyr-Arg-Ile-Gly-Arg-Cys-Pro-Asn-ThrTyr-Ala-Cys-Cys-Leu-Arg-Lys-20

Price:Yen
Vial

0.1 mg22,000(Disulfide bonds between Cys6-Cys33, Cys13-Cys27, and Cys17-Cys34)(M.W. 4366.0)

C180H295N63O52S6

Purity Information: Q E See page IV (XVI)

Antimicrobial Peptide / Chemoattractant for Monocytes
28 Human β-defensins were predicted in five gene clusters using a computational search approach1).
Among others, hBD-4, was proposed based on the cDNA sequence analysis, the precursor of which iscomposed of 72 amino acid residues. Although natural hBD-4, as far as we know, has not yet been isolated,
hBD-4 was tentatively designed as the peptide corresponding to the positions between 25 and 61 in the
precursor sequence [hereafter the term "hBD-4" is used for this peptide. Chemically synthesized hBD-4 was
confirmed to share the conserved disulfide connectivity of the β-defensin family of peptides by the combinationof enzymatic digestions and Edman degradation reaction2).
Using this chemically synthesized hBD-4, the following observations were reported2): i) hBD-4 elicits
salt-sensitive antimicrobial activities against both Gram-positive and Gram-negative bacteria in humanrespiratory epithelial cells; ii) the most active antimicrobial activity is detected against Pseudomonas aeruginosa
at 4.1 µg/ml; and iii) hBD-4 is a chemoattractant for human blood monocytes at 10 nM, but not for neutrophilesand eosinophiles. Interestingly, antimicrobial activities in the lungs were inducible by the infection andsubsequent activation of protein kinase C, thus differing from the activation mechanism from hBD-2 and hBD-3,
which are induced in response to the stimulation by TNF-α, IL-1α, IL-6 or interferon α. hBD-4 mRNA wasexpressed abundantly in testis and the stomach, and to a lesser extent but significantly in the uterus,
neutrophiles thyroid, lungs, and kidney.
hBD-4, which is regulated by specific stimulation that differs from those in hBD-2 and hBD-3, should be an
essential component in clarifying the host defense mechanism in humans. Later, the existence of theimmunoreactive hBD-4 in the body was reported3). Also, hBD-4 induces mast cell degranulation, prostaglandin
D2 production, intracellular Ca2+ mobilization and chemotaxis4).

1) B.C. Schutte, J.P. Mitros, J.A. Bartlett, J.D. Walters, H. Peng Jia, M.J. Welsh, T.L. Casavant, and P.B. McCray, Jr.,
Proc. Natl. Acad. Sci. U.S.A., 99, 2129 (2002). (β -Defensin Family Peptides)
2) J.-R.C. Garc́a, A. Krause, S. Schulz, F.-J. Rodr́guez-Jiménez, E. Klu
ver, K. Adermann, U. Forssmann,
A. Frimpong-Boateng, R. Bals, and W.-G. Forssmann, FASEB J., 15, 1819 (2001). (Original; hBD-4 & S-S Bond)
3) S. Yanagi, J.-i. Ashitani, H. Ishimoto, Y. Date, H. Mukae, N. Chino, and M. Nakazato, Respiratory Res.,6, 130 (2005). (Pharmacol. & Immunohistochem.)
4) X. Chen, F. Niyonsaba, H. Ushio, M. Hara, H. Yokoi, K. Matsumoto, H. Saito, I. Nagaoka, S. Ikeda, K. Okumura, andH. Ogawa, Eur. J. Immunol., 37, 434 (2007). (Pharmacol.)5) N. Chino, S. Kubo, H. Nishio, Y. Nishiuchi, M. Nakazato, and T. Kimura, Int. J. Pept. Res. Ther., 12, 203 (2006).
(Chem. Synthesis & Pharmacol.)– 53 –and Proteins

CompoundBiologically Active Peptides

CodeDelta Sleep-Inducing Peptide (DSIP)
Code

Compound4054-v

Delta Sleep-Inducing Peptide
DSIP
Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu-20

(M.W. 848.81)

4054
-20

Price:Yen

C35H48N10O15

0.5 mg

4,300

Bulk

25 mg

50,000[62568-57-4]

Delta Sleep-Inducing Peptide
DSIP
Trp-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu • 4H2O
(M.W. 848.81 • 72.06)

Vial

C35H48N10O15 • 4H2O

[62568-57-4]

1) G.A. Schoenenberger and M. Monnier, Proc. Natl. Acad. Sci. U.S.A., 74, 1282 (1977). (Original)
2) M. Monnier, L. Dudler, R. Gachter, P.F. Maier, H.J. Tobler, and G.A. Schoenenberger, Experientia, 33, 548 (1977).
(Pharmacol.)Dendrotoxin
4330-s-20

Dendrotoxin I(Black mamba, Dendroaspis polylepis polylepis)
Pyr-Pro-Leu-Arg-Lys-Leu-Cys-Ile-Leu-HisArg-Asp-Pro-Gly-Arg-Cys-Tyr-Gln-Lys-IlePro-Ala-Phe-Tyr-Tyr-Asn-Gln-Lys-Lys-LysGln-Cys-Glu-Gly-Phe-Thr-Trp-Ser-Gly-CysGly-Gly-Asn-Ser-Asn-Arg-Phe-Lys-Thr-IleGlu-Glu-Cys-Arg-Arg-Thr-Cys-Ile-Arg-Lys

Vial

0.1 mg30,000(Disulfide bonds between Cys7-Cys57, Cys16-Cys40, and Cys32-Cys53)(M.W. 7133.2)

C312H487N97O84S6[107950-33-4]

Voltage-Dependent K+ Channel Blocker
1) D.J. Strydom, Nature New Biol., 243, 88 (1973). (Original)
2) J.-N. Bidard, C. Mourre, and M. Lazdunski, Biochem. Biophys. Res. Commun., 143, 383 (1987). (Pharmacol.)3) A.L. Harvey, D.L. Marshall, F.A. De-Allie, and P.N. Strong, Biochem. Biophys. Res. Commun., 163, 394 (1989).
(Pharmacol.)4) H. Nishio, T. Inui, Y. Nishiuchi, C.L.C. De Medeiros, E.G. Rowan, A.L. Harvey, E. Katoh, T. Yamazaki, T. Kimura,and S. Sakakibara, J. Pept. Res., 51, 355 (1998). (Chem. Synthesis & Correction of Sequence; Asp12)

Deamino-Dicarba-Arginine Vasopressin See Code 4026 [Asu1,6, Arg8]-Vasopressin on page 150
Deamino-Dicarba-Arginine Vasotocin See Code 4027 [Asu1,6, Arg8]-Vasotocin on page 151
Deamino-Dicarba-Oxytocin See Code 4025 [Asu1,6]-Oxytocin on page 117
Diabetes-Associated Peptide (DAP) See Code 4219 Amylin (Human) and Code 4220 Amylin (Rat) on page 10– 54 –

Dermcidin-1L / DCD
4454-s

Dermcidin-1L (Human)
DCD-1L (Human)
Ser-Ser-Leu-Leu-Glu-Lys-Gly-Leu-Asp-GlyAla-Lys-Lys-Ala-Val-Gly-Gly-Leu-Gly-LysLeu-Gly-Lys-Asp-Ala-Val-Glu-Asp-Leu-GluSer-Val-Gly-Lys-Gly-Ala-Val-His-Asp-ValLys-Asp-Val-Leu-Asp-Ser-Val-Leu

New

-20

(M.W. 4818.4)

Price:Yen
Vial

0.1 mg20,000C210H359N57O71

Antimicrobial Peptide in Sweat Glands
Dermcidin is a constitutively secreted antimicrobial peptide in human sweat1). Dermcidin is revealed to bea 110-residue protein by cDNA analysis, which is proteolytically processed to several components withvariable charges. Dermcidin-1L is one of such processed peptides with anionic property, which corresponds tothe carboxyl-terminal 48-residues of the precursor protein1,2). Studies using dermcidin-1L reported so far
include: i) dermcidin-1L is active against Gram-positive and negative bacteria and fungus (1-100 µg/ml) 1), ii) in
patients with atopic dermatitis the amounts of dermicidin-1L and other dermcidin-derived peptides are
reduced3), and iii) dermcidin-1L activates human keratinocytes, inducing the generation of cytokines andchemokines (2.5-20 µg/ml)4). Dermcidin-1L does not show membrane permeability, thus, the mechanism
exerting antimicrobial activity of dermcidin-1L is distinct from that of other antimicrobial peptide, LL-37 (Code4445-s)5).
Dermcidin-1L in sweat may be essential for the battle with infectious pathogens on the human body surface,
therefore it will be an important tool in the host defense research.
1) B. Schittek, R. Hipfel, B. Sauer, J. Bauer, H. Kalbacher, S. Stevanovic, M. Schirle, K. Schroeder, N. Blin, F. Meier,G. Rassner, and C. Garbe, Nat. Immunol., 2, 1133 (2001). (Original; Antimicrobial Peptide)2) S. Rieg, H. Steffen, S. Seeber, A. Humeny, H. Kalbacher, K. Dietz, C. Garbe, and B. Schittek, J. Immunol., 174, 8003
(2005) (Endogenous Form)
3) H. Steffen, S. Rieg, I. Wiedemann, H. Kalbacher, M. Deeg, H.-G. Sahl, A. Peschel, F. Go
tz, C. Garbe, and B. Schittek,
Antimicrob. Agents Chemother., 50, 2608 (2006). (Pharmacol.)4) F. Niyonsaba, A. Suzuki, H. Ushio, I. Nagaoka, H. Ogawa, and K. Okumura, Br. J. Dermatol., 160, 243 (2009).
(Pharmacol.)5) I. Senyu
rek, M. Paulmann, T. Sinnberg, H. Kalbacher, M. Deeg, T. Gutsmann, M. Hermes, T. Kohler, F. Gotz,
C. Wolz, A. Peschel, and B. Schittek, Antimicrob. Agents Chemother., 53, 2499 (2009). (Pharmacol.)– 55 –and Proteins

CompoundBiologically Active Peptides

CodeDynorphins
1) J. Hughes, Br. Med. Bull., 39, 17 (1983). (Review)2) A.P. Smith and N.M. Lee, Annu. Rev. Pharmacol. Toxicol., 28, 123 (1988). (Review)3) M. Simonato and P. Romualdi, Prog. Neurobiol., 50, 557 (1996). (Review)

Code

Compound4080-v

Dynorphin A (Human, 1-13)(Porcine, Rat, Bovine)
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-ProLys-Leu-Lys-20

(M.W. 1604.0)

Price:Yen

C75H126N24O15

Vial

0.5 mg6,600[72957-38-1]

1) A. Goldstein, S. Tachibana, L.I. Lowney, M. Hunkapiller, and L. Hood, Proc. Natl. Acad. Sci. U.S.A., 76, 6666
(1979). (Original; Porcine)2) S. Horikawa, T. Takai, M. Toyosato, H. Takahashi, M. Noda, H. Kakidani, T. Kubo, T. Hirose, S. Inayama,
H. Hayashida, T. Miyata, and S. Numa, Nature, 306, 611 (1983). (Nucleotide Seq.; Human)

4108-v-20

Dynorphin A (Human)(Porcine, Rat, Bovine)
Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-ProLys-Leu-Lys-Trp-Asp-Asn-Gln(M.W. 2147.5)

C99H155N31O23

Vial

0.5 mg12,500[80448-90-4]

1) S. Tachibana, K. Araki, S. Ohya, and S. Yoshida, The 1981 International Narcotic Research Conference, Kyoto,
July 1981. (Original)
2) A. Goldstein, W. Fischli, L.I. Lowney, M. Hunkapiller, and L. Hood, Proc. Natl. Acad. Sci. U.S.A., 78, 7219 (1981).
(Original; Porcine)3) S. Horikawa, T. Takai, M. Toyosato, H. Takahashi, M. Noda, H. Kakidani, T. Kubo, T. Hirose, S. Inayama,
H. Hayashida, T. Miyata, and S. Numa, Nature, 306, 611 (1983). (Nucleotide Seq.; Human)4) O. Civelli, J. Douglass, A. Goldstein, and E. Herbert, Proc. Natl. Acad. Sci. U.S.A., 82, 4291 (1985).
(Nucleotide Seq.; Rat)

Elafin4243-v-20

Elafin (Human)
Ala-Gln-Glu-Pro-Val-Lys-Gly-Pro-Val-SerThr-Lys-Pro-Gly-Ser-Cys-Pro-Ile-Ile-LeuIle-Arg-Cys-Ala-Met-Leu-Asn-Pro-Pro-AsnArg-Cys-Leu-Lys-Asp-Thr-Asp-Cys-Pro-GlyIle-Lys-Lys-Cys-Cys-Glu-Gly-Ser-Cys-GlyMet-Ala-Cys-Phe-Val-Pro-Gln

Vial

20 µg

20,000(Disulfide bonds between Cys16-Cys45,Cys23-Cys49,Cys32-Cys44,and Cys38-Cys53)(M.W. 5999.1)

C254H416N72O75S10

Elastase-Specific Inhibitor from Human Skin / Innate Immune Factor
1) O. Wiedow, J.-M. Schroder, H. Gregory, J.A. Young, and E. Christophers, J. Biol. Chem., 265, 14791 (1990).
(Original)
2) O. Wiedow, J.-M. Schroder, H. Gregory, J.A. Young, and E. Christophers, J. Biol. Chem., 266, 3356 (1991).
(Correction of Seq.)
3) M. Tsunemi, H. Kato, Y. Nishiuchi, S. Kumagaye, and S. Sakakibara, Biochem. Biophys. Res. Commun.,
185, 967 (1992). (Chem. Synthesis & Biochem.)
4) M. Tsunemi, Y. Matsuura, S. Sakakibara, and Y. Katsube, Biochemistry, 35, 11570 (1996).
(Biochem.; Crystal Structure of Elafin-Pancreatic Elastase Complex)5) L. Marischen, D. Wesch, J.-M. Schroder, O. Wiedow, and D. Kabelitz, Scand. J. Immunol., 70, 547 (2009).
(Pharmacol.)6) S.M. Iqbal, T.B. Ball, P. Levinson, L. Maranan, W. Jaoko, C. Wachihi, B.J. Pak, V.N. Podust, K. Broliden, T. Hirbod,
R. Kaul, and F.A. Plummer, AIDS, 23, 1669 (2009). (Pharmacol.)– 56 –

Eledoisin Related Peptide
4003-vEledoisin Related Peptide
Lys-Phe-Ile-Gly-Leu-Met-NH2-20

(M.W. 706.94)

4003
-20

Price:Yen

C34H58N8O6S

Vial

0.5 mg

2,600

Bulk

25 mg
100 mg25,00071,000[2990-43-4]

Eledoisin Related Peptide
Lys-Phe-Ile-Gly-Leu-Met-NH2 • 2AcOH • 3H2O
(M.W. 706.94 • 120.10 • 54.05)

C34H58N8O6S • 2CH3COOH • 3H2O
1) S. Sakakibara and M. Fujino, Bull. Chem. Soc. Jpn., 39, 947 (1966). (Chem. Synthesis)

Endokinins
4411-v-20

Endokinin C (Human)
Lys-Lys-Ala-Tyr-Gln-Leu-Glu-His-Thr-PheGln-Gly-Leu-Leu-NH2(M.W. 1674.9)

Vial

0.5 mg

8,000

C78H123N21O20

Peptide in α -Tachykinin Precursor 41) N.M. Page, N.J. Bell, S.M. Gardiner, I.T. Manyonda, K.J. Brayley, P.G. Strange, and P.J. Lowry,
Proc. Natl. Acad. Sci. U.S.A., 100, 6245 (2003). (Original)
2) J.N. Pennefather, A. Lecci, M.L. Candenas, E. Patak, F.M. Pinto, and C.A. Maggi, Life Sci., 74, 1445 (2004). (Review)3) N.M. Page, Cell. Mol. Life Sci.; 61, 1652 (2004). (Review)4) R. Naono, T. Nakayama, T. Ikeda, O. Matsushima, and T. Nishimori, Brain Res., 1165, 71 (2007). (Pharmacol.)5) Y. Yang and S. Dong, Peptides, 31, 94 (2010). (Pharmacol.)4412-v-20

Endokinin D (Human)
Val-Gly-Ala-Tyr-Gln-Leu-Glu-His-Thr-PheGln-Gly-Leu-Leu-NH2(M.W. 1574.8)

Vial

0.5 mg

8,000

C73H111N19O20

Peptide in β -Tachykinin Precursor 41) N.M. Page, N.J. Bell, S.M. Gardiner, I.T. Manyonda, K.J. Brayley, P.G. Strange, and P.J. Lowry,
Proc. Natl. Acad. Sci. U.S.A., 100, 6245 (2003). (Original)
2) J.N. Pennefather, A. Lecci, M.L. Candenas, E. Patak, F.M. Pinto, and C.A. Maggi, Life Sci., 74, 1445 (2004). (Review)3) N.M. Page, Cell. Mol. Life Sci.; 61, 1652 (2004). (Review)4) R. Naono, T. Nakayama, T. Ikeda, O. Matsushima, and T. Nishimori, Brain Res., 1165, 71 (2007). (Pharmacol.)5) Y. Yang and S. Dong, Peptides, 31, 94 (2010). (Pharmacol.)Endomorphins
1) J. Fichna, A. Janecka, J. Costentin, and J.-C. do Rego, Pharmacol. Rev., 59, 88 (2007). (Review)

4333-v-20

Endomorphin-1*(Human, Bovine)
Tyr-Pro-Trp-Phe-NH2(M.W. 610.70)

4333
-20

C34H38N6O5

0.5 mg

2,100

Bulk

25 mg

48,000[189388-22-5]

Endomorphin-1*(Human, Bovine)
Tyr-Pro-Trp-Phe-NH2 • AcOH • H2O(M.W. 610.70 • 60.05• 18.01)

Vial

C34H38N6O5 • CH3COOH• H2O

Endogenous µ -Opiate Receptor Selective Agonist
1) J.E. Zadina, L. Hackler, L.-J. Ge, and A.J. Kastin, Nature, 386, 499 (1997). (Original; Bovine)
2) H.C. Champion, J.E. Zadina, A.J. Kastin, L. Hackler, L.J. Ge, and P.J. Kadowitz, Biochem. Biophys. Res. Commun.,
235, 567 (1997). (Pharmacol.)3) L.S. Stone, C.A. Fairbanks, T.M. Laughlin, H.O. Nguyen, T.M. Bushy, M.W. Wessendorf, and G.L. Wilcox,
Neuroreport, 8, 3131 (1997). (Pharmacol.)4) L. Hackler, J.E. Zadina, L.J. Ge, and A.J. Kastin, Peptides, 18, 1635 (1997). (Isolation from Human Brain)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 57 –and Proteins

CompoundBiologically Active Peptides

CodeEndomorphins (continued)
Code

Compound4334-v

Endomorphin-2*(Human, Bovine)
Tyr-Pro-Phe-Phe-NH2-20

(M.W. 571.67)

4334
-20

Price:Yen

C32H37N5O5

Vial

0.5 mg

2,100

Bulk

25 mg

48,000[141801-26-5]

Endomorphin-2*(Human, Bovine)
Tyr-Pro-Phe-Phe-NH2 • AcOH • H2O(M.W. 571.67 • 60.05• 18.01)

C32H37N5O5 • CH3COOH• H2O

Endogenous µ -Opiate Receptor Selective Agonist
1) J.E. Zadina, L. Hackler, L.-J. Ge, and A.J. Kastin, Nature, 386, 499 (1997). (Original; Bovine)
2) H.C. Champion, J.E. Zadina, A.J. Kastin, L. Hackler, L.J. Ge, and P.J. Kadowitz, Biochem. Biophys. Res. Commun.,
235, 567 (1997). (Pharmacol.)3) L.S. Stone, C.A. Fairbanks, T.M. Laughlin, H.O. Nguyen, T.M. Bushy, M.W. Wessendorf, and G.L. Wilcox,
Neuroreport, 8, 3131 (1997). (Pharmacol.)4) L. Hackler, J.E. Zadina, L.J. Ge, and A.J. Kastin, Peptides, 18, 1635 (1997). (Isolation from Human Brain)

Endorphins
1) A. Goldstein, Ann. N. Y. Acad. Sci., 311, 49 (1978). (Review)2) F. Bloom, A. Bayon, E. Battenberg, E. French, L. Koda, G. Koob, M. Le Moal, J. Rossier, and W. Shoemaker, Adv. Biochem.
Psychopharmacol., 22, 619 (1980). (Review)3) P.A. Berger, H. Akil, S.J. Watson, and J.D. Barchas, Annu. Rev. Med., 33, 397 (1982). (Review)4) F.E. Bloom, Annu. Rev. Pharmacol. Toxicol., 23, 151 (1983). (Review)

4055-v-20

α-Endorphin
β-Lipotropin (61-76)
Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-SerGln-Thr-Pro-Leu-Val-Thr(M.W. 1745.9)

C77H120N18O26S

Vial

0.5 mg

9,500[59004-96-5]

1) N. Ling, R. Burgus, and R. Guillemin, Proc. Natl. Acad. Sci. U.S.A., 73, 3942 (1976). (Original; Porcine)

4060-v-20

β-Endorphin (Human)
β-Lipotropin (Human, 61-91)
Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-SerGln-Thr-Pro-Leu-Val-Thr-Leu-Phe-Lys-AsnAla-Ile-Ile-Lys-Asn-Ala-Tyr-Lys-Lys-GlyGlu(M.W. 3465.0)

C158H251N39O46S

Vial

0.5 mg17,0000.5 mg11,500[61214-51-5]

1) C.H. Li and D. Chung, Nature, 260, 622 (1976). (Original; Human)2) C.H. Li, D. Yamashiro, L.-F. Tseng, and H.H. Loh, J. Med. Chem., 20, 325 (1977).
(Chem. Synthesis & Biological Activity)

4089-v-20

γ-Endorphin
β-Lipotropin (61-77)
Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-SerGln-Thr-Pro-Leu-Val-Thr-Leu(M.W. 1859.1)

Vial

C83H131N19O27S

1) N. Ling, R. Burgus, and R. Guillemin, Proc. Natl. Acad. Sci. U.S.A., 73, 3942 (1976). (Original; Porcine)*The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 58 –

Endothelins
2) T. Sakurai, M. Yanagisawa, and T. Masaki, Trends Pharmacol. Sci., 13, 103 (1992). (Review)
Cardiovasc. Drug Rev., 11, 253 (1993). (Review)

List of Endothelin and Related Peptides
Code

CompoundQuantity

Price: Yen

Page

0.1 mg vial
0.5 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial
0.5 mg vial
0.1 mg vial

15,00043,00020,00015,00015,00043,00015,000

below
below
60
60
60
60
63

0.1 mg vial
0.5 mg vial
0.1 mg vial
0.5 mg vial
0.1 mg vial

21,00056,00021,00056,00022,000

61
61
61
61
61

0.1 mg vial
0.1 mg vial

21,00022,00061
62

0.1 mg vial
0.1 mg vial

22,00022,0006262

0.5 mg vial

13,00062

0.1 mg vial
0.1 mg vial

15,00015,000138
138

Endothelin
4198-sEndothelin-1 (Human)4198-vEndothelin-1 (Human)
Endothelin-1 (1-31) (Human)
4360-s4209-sEndothelin-2 (Human)
4199-sEndothelin-3 (Human)
Endothelin-3 (Human)
4199-v
4211-s
VIC (Mouse)
Big Endothelin-1
4208-sBig Endothelin-1 (Human, 1-38)
Big Endothelin-1 (Human, 1-38)
4208-v
4207-sBig Endothelin-1 (Porcine, 1-39)
4207-v
Big Endothelin-1 (Porcine, 1-39)
Big Endothelin-1 (Rat, 1-39)
4266-sBig Endothelin-2
4222-sBig Endothelin-2 (Human, 1-37)
4253-sBig Endothelin-2 (Human, 1-38)
Big Endothelin-3
4223-sBig Endothelin-3 (Human, 1-41 Amide)4267-sBig Endothelin-3 (Rat, 1-41 Amide)
ETB Receptor Agonist
4285-v
Suc-[Glu9, Ala11,15]-Endothelin-1 (8-21)
Sarafotoxin
4206-sSarafotoxin S6b
4246-sSarafotoxin S6c★
★

Sarafotoxin S6c is also known as an ETB receptor agonist.

Code

Compound4198-sEndothelin-1 (Human)*(Porcine, Canine, Rat, Mouse, Bovine)
Cys-Ser-Cys-Ser-Ser-Leu-Met-Asp-Lys-GluCys-Val-Tyr-Phe-Cys-His-Leu-Asp-Ile-IleTrp-20

Price:Yen
Vial

0.1 mg15,000Vial

0.5 mg43,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 2491.9)

4198-v-20

C109H159N25O32S5[117399-94-7]

Endothelin-1 (Human)*(Porcine, Canine, Rat, Mouse, Bovine)

1) M. Yanagisawa, H. Kurihara, S. Kimura, Y. Tomobe, M. Kobayashi, Y. Mitsui, Y. Yazaki, K. Goto, and M. Masaki,
Nature, 332, 411 (1988). (Original)
2) A. Inoue, M. Yanagisawa, S. Kimura, Y. Kasuya, T. Miyauchi, K. Goto, and T. Masaki, Proc. Natl. Acad. Sci. U.S.A.,
86, 2863 (1989). (Naming)3) T.X. Watanabe, Y. Itahara, K. Nakajima, S. Kumagaye, T. Kimura, and S. Sakakibara, J. Cardiovasc. Pharmacol.,17 (Suppl. 7), S5 (1991). (Pharmacol.)*The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 59 –and Proteins

3) A.F. James, Y. Urade, R.L. Webb, H. Karaki, I. Umemura, Y. Fujitani, K. Oda, T. Okada, R.W. Lappe, and M. Takai,

Biologically Active Peptides

1) M. Yanagisawa and T. Masaki, Trends Pharmacol. Sci., 10, 374 (1989). (Review)

Endothelins (continued)
Code

Compound4360-sEndothelin-1 (1-31) (Human)*
Cys-Ser-Cys-Ser-Ser-Leu-Met-Asp-Lys-GluCys-Val-Tyr-Phe-Cys-His-Leu-Asp-Ile-IleTrp-Val-Asn-Thr-Pro-Glu-His-Val-Val-ProTyr-20

Price:Yen
Vial

0.1 mg20,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 3628.2)

C162H236N38O47S5[133972-52-8]

1) A. Nakano, F. Kishi, K. Minami, H. Wakabayashi, Y. Nakaya, and H. Kido, J. Immunol., 159, 1987 (1997).
(Original; New Endogenous Form)
2) F. Kishi, K. Minami, N. Okishima, M. Murakami, S. Mori, M. Yano, Y. Niwa, Y. Nakaya, and H. Kido,
Biochem. Biophys. Res. Commun., 248, 387 (1998). (Pharmacol.)3) M. Yoshizumi, D. Inui, N. Okishima, H. Houchi, K. Tsuchiya, H. Wakabayashi, H. Kido, and T. Tamaki,
Eur. J. Pharmacol., 348, 305 (1998). (Pharmacol.)4) M. Yoshizumi, S. Kim, S. Kagami, A. Hamaguchi, K. Tsuchiya, H. Houchi, H. Iwao, H. Kido, and T. Tamaki,
Br. J. Pharmacol., 125, 1019 (1998). (Pharmacol.)4209-s-20

Endothelin-2 (Human)*(Canine)Cys-Ser-Cys-Ser-Ser-Trp-Leu-Asp-Lys-GluCys-Val-Tyr-Phe-Cys-His-Leu-Asp-Ile-IleTrp

Vial

0.1 mg15,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 2546.9)

C115H160N26O32S4[123562-20-9]

1) A. Inoue, M. Yanagisawa, S. Kimura, Y. Kasuya, T. Miyauchi, K. Goto, and T. Masaki, Proc. Natl. Acad. Sci. U.S.A.,
86, 2863 (1989). (Original; Human Nucleotide Seq.)
2) Y. Itoh, C. Kimura, H. Onda, and M. Fujino, Nucleic Acid Res., 17, 5389 (1989). (Original; Canine cDNA)• This compound is distributed through Peptide Institute, Inc. under the license of Takeda Pharmaceutical Company
Limited.

4199-s-20

Endothelin-3 (Human)*(Porcine, Rat, Rabbit, Mouse)
Cys-Thr-Cys-Phe-Thr-Tyr-Lys-Asp-Lys-GluCys-Val-Tyr-Tyr-Cys-His-Leu-Asp-Ile-IleTrp

Vial

0.1 mg15,000Vial

0.5 mg43,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 2643.0)

4199-v-20

C121H168N26O33S4[117399-93-6]

Endothelin-3 (Human)*(Porcine, Rat, Rabbit, Mouse)
Purity Information : QX See page IV (XVI)

1) M. Yanagisawa, A. Inoue, T. Ishikawa, Y. Kasuya, S. Kimura, S. Kumagaye, K. Nakajima, T.X. Watanabe,
S. Sakakibara, K. Goto, and T. Masaki, Proc. Natl. Acad. Sci. U.S.A., 85, 6964 (1988). (Original)
2) A. Inoue, M. Yanagisawa, S. Kimura, Y. Kasuya, T. Miyauchi, K. Goto, and T. Masaki, Proc. Natl. Acad. Sci. U.S.A.,
86, 2863 (1989). (Naming)3) K. Nakajima, S. Kumagaye, H. Nishio, H. Kuroda, T.X. Watanabe, Y. Kobayashi, H. Tamaoki, T. Kimura, and
S. Sakakibara, J. Cardiovasc. Pharmacol., 13 (Suppl.5), S8 (1989). (Chem. Synthesis & S-S Bond)4) K. Saida, N. Kometani, Y. Hirano, S. Oka, N. Tomizuka, and Y. Mitsui, Peptide Chemistry 1996, 133 (1997).
(cDNA Seq.; Mouse)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 60 –

Endothelins (continued)
4208-sBig Endothelin-1 (Human, 1-38)*
Cys-Ser-Cys-Ser-Ser-Leu-Met-Asp-Lys-GluCys-Val-Tyr-Phe-Cys-His-Leu-Asp-Ile-IleTrp-Val-Asn-Thr-Pro-Glu-His-Val-Val-ProTyr-Gly-Leu-Gly-Ser-Pro-Arg-Ser-20

Price:Yen
Vial

0.1 mg21,000Vial

0.5 mg56,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 4282.9)

4208-v

C189H282N48O56S5[120796-97-6]

Big Endothelin-1 (Human, 1-38)*-20

1) Y. ltoh, M. Yanagisawa, S. Ohkubo, C. Kimura, T. Kosaka, A. Inoue, N. Ishida, Y. Mitsui, H. Onda, M. Fujino, andT. Masaki, FEBS Lett., 231, 440 (1988). (Original)
2) T. Kashiwabara, Y. Inagaki, H. Ohta, A. Iwamatsu, M. Nomizu, A. Morita, and K. Nishikori, FEBS Lett.,
247, 73 (1989). (Pharmacol.)4207-s-20

Big Endothelin-1 (Porcine, 1-39)*
Cys-Ser-Cys-Ser-Ser-Leu-Met-Asp-Lys-GluCys-Val-Tyr-Phe-Cys-His-Leu-Asp-Ile-IleTrp-Val-Asn-Thr-Pro-Glu-His-Ile-Val-ProTyr-Gly-Leu-Gly-Ser-Pro-Ser-Arg-Ser

Vial

0.1 mg21,000Vial

0.5 mg56,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 4384.0)

4207-v

C193H289N49O58S5[120796-99-8]

Big Endothelin-1 (Porcine, 1-39)*-201) M. Yanagisawa, H. Kurihara, S. Kimura, Y. Tomobe, M. Kobayashi, Y. Mitsui, Y. Yazaki, K. Goto, and T. Masaki,
Nature, 332, 411 (1988). (Original)
2) T. Kashiwabara, Y. Inagaki, H. Ohta, A. Iwamatsu, M. Nomizu, A. Morita, and K. Nishikori, FEBS Lett.,
247, 73 (1989). (Pharmacol.)4266-s-20

Big Endothelin-1 (Rat, 1-39)*
Cys-Ser-Cys-Ser-Ser-Leu-Met-Asp-Lys-GluCys-Val-Tyr-Phe-Cys-His-Leu-Asp-Ile-IleTrp-Val-Asn-Thr-Pro-Glu-Arg-Val-Val-ProTyr-Gly-Leu-Gly-Ser-Pro-Ser-Arg-Ser

Vial

0.1 mg22,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 4389.0)

C192H292N50O58S5

1) T. Sakurai, M. Yanagisawa, A. Inoue, U.S. Ryan, S. Kimura, Y. Mitsui, K. Goto, and T. Masaki,
Biochem. Biophys. Res. Commun., 175, 44 (1991). (Original; cDNA)

4222-s-20

Big Endothelin-2 (Human, 1-37)*
Cys-Ser-Cys-Ser-Ser-Trp-Leu-Asp-Lys-Glu-CysVal-Tyr-Phe-Cys-His-Leu-Asp-Ile-Ile-Trp-ValAsn-Thr-Pro-Glu-Gln-Thr-Ala-Pro-Tyr-Gly-LeuGly-Asn-Pro-Pro

Vial

0.1 mg21,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 4183.7) C188H269N45O56S4 [132699-72-0]
Purity Information: Qx See page IV (XVI)
1) S. Ohkubo, K. Ogi, M. Hosoya, H. Matsumoto, N. Suzuki, C. Kimura, H. Onda, and M. Fujino, FEBS Lett.,

274, 136 (1990). (Original; cDNA)* The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 61 –and Proteins

CompoundBiologically Active Peptides

CodeEndothelins (continued)
Code

Compound4253-sBig Endothelin-2 (Human, 1-38)*
Cys-Ser-Cys-Ser-Ser-Trp-Leu-Asp-Lys-Glu-CysVal-Tyr-Phe-Cys-His-Leu-Asp-Ile-Ile-Trp-ValAsn-Thr-Pro-Glu-Gln-Thr-Ala-Pro-Tyr-Gly-LeuGly-Asn-Pro-Pro-Arg-20

Price:Yen
Vial

0.1 mg22,000(Disulfide bonds between Cys1-Cys15 and Cys3Cys11) (M.W. 4339.9) C194H281N49O57S4
Purity Information: Qx See page IV (XVI)
1) S. Ohkubo, K. Ogi, M. Hosoya, H. Matsumoto, N. Suzuki, C. Kimura, H. Onda, and M. Fujino, FEBS Lett.,
274, 136 (1990). (Original; cDNA)2) T. Kosaka, N. Suzuki, Y. Ishibashi, H. Matsumoto, Y. Itoh, S. Ohkubo, K. Ogi, C. Kitada, H. Onda, and M. Fujino,
J. Biochem., 116, 443 (1994). (Biosynthesis)4223-s-20

Big Endothelin-3 (Human, 1-41 Amide)*
Cys-Thr-Cys-Phe-Thr-Tyr-Lys-Asp-Lys-GluCys-Val-Tyr-Tyr-Cys-His-Leu-Asp-Ile-IleTrp-Ile-Asn-Thr-Pro-Glu-Gln-Thr-Val-ProTyr-Gly-Leu-Ser-Asn-Tyr-Arg-Gly-Ser-PheArg-NH2

Vial

0.1 mg22,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 4923.5)

C223H322N56O63S41) K.D. Bloch, R.L. Eddy, T.B. Shows, and T. Quertermous, J. Biol. Chem., 264, 18156 (1989). (Original; cDNA)2) T. Kosaka, N. Suzuki, Y. Ishibashi, H. Matsumoto, Y. Itoh, S. Ohkubo, K. Ogi, C. Kitada, H. Onda, and M. Fujino,
J. Biochem., 116, 443 (1994). (Original; Biosynthesis)• This compound is distributed through Peptide Institute, Inc. under the license of Takeda Pharmaceutical Company
Limited.

4267-s-20

Big Endothelin-3 (Rat, 1-41 Amide)*
Cys-Thr-Cys-Phe-Thr-Tyr-Lys-Asp-Lys-GluCys-Val-Tyr-Tyr-Cys-His-Leu-Asp-Ile-IleTrp-Ile-Asn-Thr-Pro-Glu-Gln-Thr-Val-ProTyr-Gly-Leu-Ser-Asn-His-Arg-Gly-Ser-LeuArg-NH2

Vial

0.1 mg22,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 4863.5)

C217H322N58O62S41) R. Shiba, T. Sakurai, G. Yamada, H. Morimoto, A. Saito, T. Masaki, and K. Goto, Biochem. Biophys. Res. Commun.,
186, 588 (1992). (Original; cDNA)

4285-v-20

Suc-[Glu9, Ala11,15]-Endothelin-1 (8-21)*
IRL 1620
Suc-Asp-Glu-Glu-Ala-Val-Tyr-Phe-Ala-HisLeu-Asp-Ile-Ile-Trp

Vial

0.5 mg13,000(Suc: Succinyl)(M.W. 1820.9)

C86H117N17O27[142569-99-1]

ETB Receptor Selective Agonist
1) M. Takai, I. Umemura, K. Yamasaki, T. Watakabe, Y. Fujitani, K. Oda, Y. Urade, T. Inui, T. Yamamura, and T. Okada,
Biochem. Biophys. Res. Commun., 184, 953 (1992). (Original)
2) S.S. Shetty, T. Okada, R.L. Webb, D. DelGrande, and R.W. Lappe, Biochem. Biophys. Res. Commun.,
191, 459 (1993). (Pharmacol.)3) W.G. Haynes, A.P. Davenport, and D.J. Webb, Trends Pharmacol. Sci., 14, 225 (1993).
(Report; 3rd Int. Conf. Endothelin)
4) A.F. James, Y. Urade, R.L. Webb, H. Karaki, I. Umemura, Y. Fujitani, K. Oda, T. Okada, R.W. Lappe, and M. Takai,
Cardiovasc. Drug Rev., 11, 253 (1993). (Review)* The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 62 –

Endothelins (continued)
4211-s

VIC (Mouse)*
Vasoactive Intestinal Contractor (Mouse)
Cys-Ser-Cys-Asn-Ser-Trp-Leu-Asp-Lys-GluCys-Val-Tyr-Phe-Cys-His-Leu-Asp-Ile-IleTrp-20

Price:Yen
Vial

0.1 mg15,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 2573.9)

C116H161N27O32S41) N. Ishida, K. Tsujioka, M. Tomoi, K. Saida, and Y. Mitsui, FEBS Lett., 247, 337 (1989). (Original)
2) K. Saida, Y. Mitsui, and N. Ishida, J. Biol. Chem., 264, 14613 (1989). (Original; Nucleotide Seq.)

Endothelin Related Peptides
Sarafotoxin S6b See Code 4206 on page 138
Sarafotoxin S6c See Code 4246 on page 138
Endothelium-Derived Relaxing Factor Inhibitor (Synthetic) (Nitric Oxide Synthase Inhibitor)
See Code 2005 Arg(NO2) on page 301

Enkephalins
4043-v-20

Leucine-Enkephalin(Human, Porcine, Bovine, Rat, Mouse)
Tyr-Gly-Gly-Phe-Leu(M.W. 555.62)

4043
-20

C28H37N5O7Vial

0.5 mg

2,100

Bulk

25 mg
100 mg11,00031,000[58822-25-6]

Leucine-Enkephalin(Human, Porcine, Bovine, Rat, Mouse)
Tyr-Gly-Gly-Phe-Leu • H2O(M.W. 555.62 •18.02)

C28H37N5O7 • H2O [58822-25-6]
1) J. Hughes, T.W. Smith, H.W. Kosterlitz, L.A. Fothergill, B.A. Morgan, and H.R. Morris, Nature, 258, 577 (1975).
(Original; Porcine)2) M. Comb, P.H. Seeburg, J. Adelman, L. Eiden, and E. Herbert, Nature, 295, 663 (1982). (cDNA Seq.; Human)3) M. Noda, Y. Furutani, H. Takahashi, M. Toyosato, T. Hirose, S. Inayama, S. Nakanishi, and S. Numa, Nature,
295, 202 (1982). (cDNA Seq.; Bovine)
4) K. Yoshikawa, C. Williams, and S.L. Sabol, J. Biol. Chem., 259, 14301 (1984). (cDNA Seq.; Rat)

4118-v-20

Leucine-Enkephalin (Sulfated Form)
Tyr(SO3H)-Gly-Gly-Phe-Leu(M.W. 635.69)

C28H37N5O10S

Vial

0.5 mg

4,600

Vial

0.5 mg

2,100

Bulk

25 mg
100 mg15,00044,000[80632-52-6]

1) C.D. Unsworth and J. Hughes, Nature, 295, 519 (1982). (Original)

4042-v-20

Methionine-Enkephalin(Human, Porcine, Bovine, Rat, Mouse)
Tyr-Gly-Gly-Phe-Met(M.W. 573.66)

4042
-20

C27H35N5O7S[58569-55-4]

Methionine-Enkephalin(Human, Porcine, Bovine, Rat, Mouse)
Tyr-Gly-Gly-Phe-Met • H2O(M.W. 573.66 • 18.02)

C27H35N5O7S • H2O [58569-55-4]
1) J. Hughes, T.W. Smith, H.W. Kosterlitz, L.A. Fothergill, B.A. Morgan, and H.R. Morris, Nature, 258, 577 (1975).
(Original; Porcine)2) M. Comb, P.H. Seeburg, J. Adelman, L. Eiden, and E. Herbert, Nature, 295, 663 (1982). (cDNA Seq.; Human)3) M. Noda, Y. Furutani, H. Takahashi, M. Toyosato, T. Hirose, S. Inayama, S. Nakanishi, and S. Numa, Nature,
295, 202 (1982). (cDNA Seq.; Bovine)
4) K. Yoshikawa, C. Williams, and S.L. Sabol, J. Biol. Chem., 259, 14301 (1984). (cDNA Seq.; Rat)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 63 –and Proteins

CompoundBiologically Active Peptides

CodeEnkephalins (continued)
Code

Compound4115-v[D-Ala2,D-Leu5]-Enkephalin
Tyr-D-Ala-Gly-Phe-D-Leu-20

(M.W. 569.65)

4115
-20

Price:Yen

C29H39N5O7

Vial

0.5 mg

2,400

Bulk

25 mg
100 mg23,00065,000Vial

0.5 mg

2,400

Bulk

25 mg

23,000[63631-40-3][D-Ala2,D-Leu5]-Enkephalin
Tyr-D-Ala-Gly-Phe-D-Leu • AcOH • H2O(M.W. 569.65 • 60.05 • 18.02)

C29H39N5O7 • CH3COOH • H2O [94825-57-7]
1) E.T. Wei, L.F. Tseng, H.H. Loh, and C.H. Li, Life Sci., 21, 321 (1977). (Original)

4116-v-20

[D-Ala2,Met5]-Enkephalin
Tyr-D-Ala-Gly-Phe-Met(M.W. 587.69)

4116
-20

C28H37N5O7S[61370-87-4][D-Ala2,Met5]-Enkephalin
Tyr-D-Ala-Gly-Phe-Met • AcOH • H2O(M.W. 587.69 • 60.05 • 18.02)

C28H37N5O7S • CH3COOH • H2O[100929-62-2]

1) D.H. Coy, A.J. Kastin, A.V. Schally, O. Morin, N.G. Caron, F. Labrie, J.M. Walker, R. Fertel, G.G. Berntson, andC.A. Sandman, Biochem. Biophys. Res. Commun., 73, 632 (1976). (Original; Chem. Synthesis)

4117-v-20

[D-Ala2,Met5]-Enkephalinamide
Tyr-D-Ala-Gly-Phe-Met-NH2(M.W. 586.70)

C28H38N6O6S

Vial

0.5 mg2,400[61090-95-7]

1) C.B. Pert, A. Pert, J.-K. Chang, and B.T.W. Fong, Science, 194, 330 (1976). (Original)
2) D.H. Coy, A.J. Kastin, A.V. Schally, O. Morin, N.G. Caron, F. Labrie, J.M. Walker, R. Fertel, G.G. Berntson, andC.A. Sandman, Biochem. Biophys. Res. Commun., 73, 632 (1976). (Original; Chem. Synthesis)

Exendin4345-v-20

Exendin (5-39)(Lizard, Heloderma horridum)
Thr-Phe-Thr-Ser-Asp-Leu-Ser-Lys-Gln-MetGlu-Glu-Glu-Ala-Val-Arg-Leu-Phe-Ile-GluTrp-Leu-Lys-Asn-Gly-Gly-Pro-Ser-Ser-GlyAla-Pro-Pro-Pro-Ser-NH2(M.W. 3806.2)

Vial

0.5 mg30,000C169H262N44O54S

GLP-1 Receptor Antagonist
1) C. Montrose-Rafizadeh, H. Yang, B.D. Rodgers, A. Beday, L.A. Pritchette, and J. Eng, J. Biol. Chem.,
272, 21201 (1997). (Original; Potent Antagonist)
2) J.-I. Oka, E. Suzuki, and Y. Kondo, Brain Res., 878, 194 (2000). (Pharmacol.)– 64 –

Feeding-Regulatory Peptides
CompoundQuantity

Price: Yen

Page

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30,00012,50017,00033,00033,00029,00020,00020,00012,00015,00012,00012,00020,00010,00010,00013,000

8
56
58
66
66
67
69
69
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93
108
108
114
115
115
134

Food Intake Stimulator
4366-s4108-v
4060-v
4245-v
4244-v
4391-s4372-s4373-s
4127-s4369-v
4158-s4162-s4346-s4348-s4347-s4419-sAgouti-Related Protein (Human, 86-132)
Dynorphin A (Human)β-Endorphin (Human)
Galanin (Human)
Galanin (Rat)
Galanin-like Peptide (Human, 1-60)
Ghrelin (Human)
Ghrelin (Rat)
GRF (Human)
Melanin-Concentrating Hormone (Human)
NPY (Human, Rat)
NPY (Porcine, Bovine)
Orexin-A (Human)
Orexin-B (Human)
Orexin-B (Rat, Mouse)
Pyroglutamylated RFamide Peptide (Human)

Food Intake Suppressor
4421-s4422-s4219-v
4086-v
4350-s
4351-s4100-v
4160-s4163-s4136-s
4111-s4344-v
4376-v
4088-s4057-v
4426-s4427-s4377-v
4425-v
4029-v
4429-s4430-s
4400-v
4352-v
4353-v
4387-s4388-s4011-v
4328-s4327-s4383-sAdrenomedullin 2 / Intermedin (Human)
Adrenomedullin 2 / Intermedin (Rat)
Amylin (Human)
Bombesin
CART (Human, 55-102)
CART (Rat, 55-102)
CCK-Octapeptide (26-33) (Sulfated Form)
CGRP (Human)
CGRP (Rat)
CRF (Human, Rat)
CRF (Ovine)
GLP-1 (Human, 7-36 Amide)
GLP-2 (Human)
Insulin (Human)
α-MSH
Neuromedin S (Human)
Neuromedin S (Rat)
Neuromedin U (Rat)
Neuropeptide S (Human)
Neurotensin
Obestatin (Human)
Obestatin (Rat, Mouse)
Peptide YY (Human, 3-36)
Prolactin-Releasing Peptide (Human)
Prolactin-Releasing Peptide (Rat)Stresscopin (Human)
Stresscopin-Related Peptide (Human)
TRH
Urocortin (Human)
Urocortin (Rat)
Urocortin II (Mouse)

0.1 mg vial
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24,00024,00041,000
5,200
30,00030,00012,00011,50011,50012,00012,00029,00029,00013,0005,700
11,00012,00020,00021,000
3,300
8,000
8,000
39,00025,00025,00016,00018,0001,900
14,00014,00014,000

4
4
10
24
33
33
36
34
35
43
43
71
72
84
94
103
103
104
107
110
113
113
124
129
129
142
143
147
143
143
144

4436-s4437-s4178-s4403-v
4404-v
4023-v

Des-Acyl Ghrelin (Human)
Des-Acyl Ghrelin (Rat)
GIP (Human)
Neuropeptide W-30 (Human)
Neuropeptide W-30 (Rat)
Somatostatin

0.1 mg vial
0.1 mg vial
0.1 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial

12,00012,00012,00033,00033,000
9,000

70
70
68
109
109
141

Others– 65 –and Proteins

Code

Biologically Active Peptides

List of Feeding-Regulatory Peptides

Fibronectin Active Fragment
See Code 4171 Arg-Gly-Asp-Ser on page 23 and 246
See Code 4189 Gly-Arg-Gly-Asp-Ser on page 23
FMRF-Amide See Code 4142 Molluscan Cardioexcitatory Neuropeptide on page 95 and 246

Galanin and Related Peptides
1) J.N. Crawley and G.L. Wenk, Trends Neurosci., 12, 278 (1989). (Review)
2) T. Bartfai, G. Fisone, and 
U. Langel, Trends Pharmacol. Sci., 13, 312 (1992). (Review)3) R. Lang, A.L. Gundlach, and B. Kofler, Pharmacol. Ther., 115, 177 (2007). (Review)4) I. Mechenthaler, Cell. Mol. Life Sci., 65, 1826 (2008). (Review)

Code

Compound4245-v

Galanin (Human)*
Gly-Trp-Thr-Leu-Asn-Ser-Ala-Gly-Tyr-LeuLeu-Gly-Pro-His-Ala-Val-Gly-Asn-His-ArgSer-Phe-Ser-Asp-Lys-Asn-Gly-Leu-Thr-Ser-20

(M.W. 3157.4)

Price:Yen

C139H210N42O43

Vial

0.5 mg33,000[119418-04-1]

1) M. Bersani, A.H. Johnsen, P. Hjrup, B.E. Dunning, J.J. Andreasen, and J.J. Holst, FEBS Lett., 283, 189 (1991).
(Original)

4244-v-20

Galanin (Rat)*(Mouse)Gly-Trp-Thr-Leu-Asn-Ser-Ala-Gly-Tyr-LeuLeu-Gly-Pro-His-Ala-Ile-Asp-Asn-His-ArgSer-Phe-Ser-Asp-Lys-His-Gly-Leu-Thr-NH2(M.W. 3164.4)

C141H211N43O41

Vial

0.5 mg33,000[114547-31-8]1) M.E. Vrontakis, L.M. Peden, M.L. Duckworth, and H.G. Friesen, J. Biol. Chem., 262, 16755 (1987). (Original; Rat
Pituitary Tumoral cDNA)
2) L.M. Kaplan, E.R. Spindel, K.J. Isselbacher, and W.W. Chin, Proc. Natl. Acad. Sci. U.S.A., 85, 1065 (1988).
(Original; Rat Hypothalamic cDNA)
3) J. Lundkvist, T. Land, U. Kahl, K. Bedecs, and T. Bartfai, Neurosci. Lett., 200, 121 (1995).
(Original; Mouse Hypothalamic cDNA)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 66 –

Galanin and Related Peptides (continued)
4391-sGalanin-like Peptide (Human, 1-60)
GALP (Human, 1-60)
Ala-Pro-Ala-His-Arg-Gly-Arg-Gly-Gly-TrpThr-Leu-Asn-Ser-Ala-Gly-Tyr-Leu-Leu-GlyPro-Val-Leu-His-Leu-Pro-Gln-Met-Gly-AspGln-Asp-Gly-Lys-Arg-Glu-Thr-Ala-Leu-GluIle-Leu-Asp-Leu-Trp-Lys-Ala-Ile-Asp-GlyLeu-Pro-Tyr-Ser-His-Pro-Pro-Gln-Pro-Ser-20

(M.W. 6500.3)

Price:Yen
Vial

0.1 mg29,000C292H451N83O84S

Ligand for Galanin Receptor 2 / Target Peptide for Feeding Regulation by Leptin
Galanin [Code 4245-v (human) and Code 4244-v (rat)] is one of the brain-gut peptides having various
biological activities including feeding regulation. This peptide is known to be a food intake stimulator whichinteracts with both of the galanin receptor subtypes 1 and 2 (GalR1 and GalR2, respectively) in a
relatively non-selective manner. GalR1 is primarily expressed in the central nervous system (CNS), whereas
GalR2 is expressed in both peripheral tissue and the CNS.
In 1999, scientists at Takeda Pharmaceutical Company Limited discovered the GalR2-selective ligand in
porcine hypothalamus. At the same time, they proposed the primary structures of the rat and humanorthologues from the corresponding cDNA sequences1). This newly identified peptide, known as galanin-like
peptide (GALP), is composed of 60 amino acid residues. GALP (9-21) is identical to galanin (1-13) and thesequence homology among the species is high. When 125I-labeled rat galanin is used as a ligand, porcine GALPinteracts with GalR2 with an IC50 value of 0.24 nM, while the corresponding value for GalR1 is 4.3 nM, clearly
indicating the receptor selectivity of GALP. Since then, additional data concerning the role of rat GALP in
feeding have been reported dealing with: i) stimulation of food intake in rats2,3), ii) control of its expression byleptin4), and iii) crossing the blood brain barrier5). Recently review articles concerning the function of GALP in
relation to galanin and the galanin receptor have also been published6)-8).
1) T. Ohtaki, S. Kumano, Y. Ishibashi, K. Ogi, H. Matsui, M. Harada, C. Kitada, T. Kurokawa, H. Onda, and M. Fujino,
J. Biol. Chem., 274, 37041 (1999). (Original)
2) Y. Matsumoto, T. Watanabe, Y. Adachi, T. Itoh, T. Ohtaki, H. Onda, T. Kurokawa, O. Nishimura, and M. Fujino,
Neurosci. Lett., 322, 67 (2002). (Pharmacol.; Stimulation of Food Intake)3) H.-M. Tan, A.L. Gundlach, and M.J. Morris, Neuropeptides, 39, 333 (2005). (Pharmacol.; Exaggerated Feeding
Response)
4) A. Juréus, M.J. Cunningham, M.E. Mcclain, D.K. Clifton, and R.A. Steiner, Endocrinology, 141, 2703 (2000).
(Pharmacol.)5) A.J. Kastin, V. Akerstrom, and L. Hackler, Neuroendocrinology, 74, 423 (2001). (Pharmacol.; Brain Entry)
6) A.L. Gundlach, Eur. J. Pharmacol., 440 255 (2002). (Review)7) P.S. Man and C.B. Lawrence, Neuropharmacology, 55, (2008). (Review)8) C.B. Lawrence, Physiol. Behav., 97, 515 (2009). (Review)• This compound is distributed through Peptide Institute, Inc. under the Iicense of Takeda Pharmaceutical Company
Limited.

GALP Splice Variant See Code 4449 Alarin on page 9– 67 –and Proteins

CompoundBiologically Active Peptides

CodeGastrin and Related Peptides
1) J.E. Jorpes and V. Mutt (eds.), Secretin, Cholecystokinin, Pancreozymin and Gastrin, Handbook of Experimental
Pharmacology, Vol. 34, Springer-Verlag, Berlin, 1973. (Review)

Code

CompoundPrice:Yen

4183-sBig Gastrin (Human)-20

(Ammonium Form)

Vial

0.1 mg13,000

Pyr-Leu-Gly-Pro-Gln-Gly-Pro-Pro-His-LeuVal-Ala-Asp-Pro-Ser-Lys-Lys-Gln-Gly-ProTrp-Leu-Glu-Glu-Glu-Glu-Glu-Ala-Tyr-GlyTrp-Met-Asp-Phe-NH2(M.W. 3849.2)

C176H251N43O53S[60675-77-6]

1) A.M. Choudhury, G.W. Kenner, S. Moore, K.L. Ramachandran, W.D. Thorpe, R. Ramage, G.J. Dockray,
R.A. Gregory, L. Hood, and M. Hunkapiller, Hoppe-Seyler's Z. Physiol. Chem., 361, 1719 (1980).
(Original; Chem. Synthesis)4143-v

Gastrin I (Human)-20

(Ammonium Form)

Vial

0.5 mg26,000Pyr-Gly-Pro-Trp-Leu-Glu-Glu-Glu-Glu-GluAla-Tyr-Gly-Trp-Met-Asp-Phe-NH2(M.W. 2098.2)

C97H124N20O31S[10047-33-3]

1) H. Gregory, P.M. Hardy, D.S. Jones, G.W. Kenner, and R.C. Sheppard, Nature, 204, 931 (1964). (Original)
2) J.C. Anderson, M.A. Barton, R.A. Gregory, P.M. Hardy, G.W. Kenner, J.K. MacLeod, J. Preston, R.C. Sheppard, andJ.S. Morley, Nature, 204, 933 (1964). (Chem. Synthesis)

4004
-20

Bulk

Gastrin Related Peptide
Aoc-Trp-Met-Asp-Phe-NH2

25 mg
100 mg

9,600
25,000Vial

0.1 mg12,000Vial

0.5 mg41,000(Aoc: t-Amyloxycarbonyl)(M.W. 710.84)

C35H46N6O8S

1) Y. Ishii and H. Shinozaki, Jpn. J. Pharmacol., 18, 93 (1968). (Pharmacol.)4178-s-20

GIP (Human)
Gastric Inhibitory Polypeptide (Human)
Glucose-dependent Insulinotropic Polypeptide (Human)
Tyr-Ala-Glu-Gly-Thr-Phe-Ile-Ser-Asp-TyrSer-Ile-Ala-Met-Asp-Lys-Ile-His-Gln-GlnAsp-Phe-Val-Asn-Trp-Leu-Leu-Ala-Gln-LysGly-Lys-Lys-Asn-Asp-Trp-Lys-His-Asn-IleThr-Gln(M.W. 4983.5)

4178-v-20

C226H338N60O66S[100040-31-1]

GIP (Human)
Gastric Inhibitory Polypeptide (Human)
Glucose-dependent Insulinotropic Polypeptide (Human)

1) A.J. Moody, L. Thim, and I. Valverde, FEBS Lett., 172, 142 (1984). (Original)
2) N. Fujii, M. Sakurai, K. Akaji, M. Nomizu, H. Yajima, K. Mizuta, M. Aono, M. Moriga, K. Inoue, R. Hosotani,
and T. Tobe, Chem. Pharm. Bull., 34, 2397 (1986). (Glucose-dependent Insulinotropic Polypeptide)

4164-v-20

GRP (Human)
Gastrin Releasing Peptide (Human)
Val-Pro-Leu-Pro-Ala-Gly-Gly-Gly-Thr-ValLeu-Thr-Lys-Met-Tyr-Pro-Arg-Gly-Asn-HisTrp-Ala-Val-Gly-His-Leu-Met-NH2(M.W. 2859.4)

C130H204N38O31S2

Vial

0.5 mg32,000[93755-85-2]

1) E.R. Spindel, W.W. Chin, J. Price, L.H. Rees, G.M. Besser, and J.F. Habener, Proc. Natl. Acad. Sci. U.S.A.,
81, 5699 (1984). (Original; cDNA)

Gastrin Releasing Peptide (Human, 18-27) See Code 4153 Neuromedin C on page 102– 68 –

Ghrelins and Des-Acyl Ghrelins
Price:Yen

4372-sGhrelin (Human)-20

(Trifluoroacetate Form)

Vial

0.1 mg20,000Gly-Ser-Ser(n-Octanoyl)-Phe-Leu-Ser-Pro-Glu-His-GlnArg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-LysPro-Pro-Ala-Lys-Leu-Gln-Pro-Arg(M.W. 3370.9)

C149H249N47O42[258279-04-8]

Appetite Stimulating Peptide with Energy Homeostasis Regulation• This compound is distributed through Peptide Institute, Inc. under the license of Dr. K. Kangawa.

4373-s-20

Vial

Ghrelin (Rat)(Mouse)0.1 mg20,000(Trifluoroacetate Form)

Gly-Ser-Ser(n-Octanoyl)-Phe-Leu-Ser-Pro-Glu-His-GlnLys-Ala-Gln-Gln-Arg-Lys-Glu-Ser-Lys-LysPro-Pro-Ala-Lys-Leu-Gln-Pro-Arg(M.W. 3314.8)

C147H245N45O42[258338-12-4]

Appetite Stimulating Peptide with Energy Homeostasis Regulation• This compound is distributed through Peptide Institute, Inc. under the license of Dr. K. Kangawa.

Ghrelin was discovered in 1999 as the endogenous ligand of growth-hormone secretagogue receptor1):i) ghrelin is a 28 residue peptide with an n-octanoyl group on Ser3 and ii) the major ghrelin producing organ isthe stomach. Since then, many researches have been carried out using synthetic ghrelin, clarifying that ghrelinis a multifunctional peptide. These functions include i) regulation of appetite, ii) cardiovascular functions, andso on, which are summarized as review articles3)-12).
1) M. Kojima, H. Hosoda, Y. Date, M. Nakazato, H. Matsuo, and K. Kangawa, Nature, 402, 656 (1999). (Original)
2) P.L. Jeffery, R.P. Duncan, A.H. Yeh, R.A. Jaskolski, D.S. Hammond, A.C. Herington, and L.K. Chopin, Endocrinology,
146, 432 (2005). (Mouse RNA Seq.)
3) C. Dieguez and F.F. Casanueva, Eur. J. Endocrinol., 142, 413 (2000). (Review)4) G. Muccioli, M. Tschop, M. Papotti, R. Deghenghi, M. Heiman, and E. Ghigo, Eur. J. Pharmacol., 440, 235 (2002). (Review)5) G. Wang, H.-M. Lee, E. Englander, and G.H. Greeley, Jr., Regul. Pept., 105, 75 (2002). (Review)6) A.J. van der Lely, M. Tschop, M.L. Heiman, and E. Ghigo, Endocr. Rev., 25, 426 (2004). (Review)7) M. Kojima and K. Kangawa, Physiol. Rev., 85, 495 (2005). (Review)8) P. Pusztai, B. Sarman, E. Ruzicska, J. Toke, K. Racz, A. Somogyi, and Z. Tulassay, Diabetes Metab. Res. Rev., 24, 343(2008). (Review)9) P.K. Olszewski, H.B. Schioth, and A.S. Levine, Brain Res. Rev., 58, 160 (2008). (Review)
10) F. Ferrini, C. Salio, L. Lossi, and A. Merighi, Curr.Neuropharmacol., 7, 37 (2009). (Review)11) I. Depoortere, Regul.Pept., 156, 13 (2009). (Review)
12) T. Lorenzi, R. Meli, D. Marzioni, M. Morroni, A. Baragli, M. Castellucci, O. Gualillo, and G. Muccioli, Cytokine
Growth Factor Rev., 20, 137 (2009). (Review)– 69 –and Proteins

CompoundBiologically Active Peptides

CodeGhrelins and Des-Acyl Ghrelins (continued)
Code

Compound4436-s

Des-Acyl Ghrelin (Human)
Des-n-Octanoyl Ghrelin (Human)-20

Price:Yen
Vial

0.1 mg12,000Vial

0.1 mg12,000(Trifluoroacetate Form)

Gly-Ser-Ser-Phe-Leu-Ser-Pro-Glu-His-GlnArg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-LysPro-Pro-Ala-Lys-Leu-Gln-Pro-Arg(M.W. 3244.7)

C141H235N47O41

Des-Octanoylated Ghrelin with Distinct Effect on Food Intake
4437-s-20

Des-Acyl Ghrelin (Rat)
Des-n-Octanoyl Ghrelin (Rat)(Trifluoroacetate Form)

Gly-Ser-Ser-Phe-Leu-Ser-Pro-Glu-His-GlnLys-Ala-Gln-Gln-Arg-Lys-Glu-Ser-Lys-LysPro-Pro-Ala-Lys-Leu-Gln-Pro-Arg(M.W. 3188.6)

C139H231N45O41

Des-Octanoylated Ghrelin with Distinct Effect on Food Intake
In the survey of the endogenous form(s) of ghrelin, two major peptides were found to exist in tissues andplasma, which are ghrelin itself and des-octanoylated ghrelin (des-acyl ghrelin)1). Very interestingly, the plasma
level of des-acyl ghrelin is excessive, so that the possible function of this particular form of the ghrelin peptide,
des-acyl ghrelin, has been considered although growth hormone (GH) releasing activity of ghrelin through GH
secretagogue receptor (GHSR) was abrogated by removing the octanoyl group. In the accumulating
publications dealing with the function of des-acyl ghrelin, the following interesting aspects were pointed out by
utilizing either rat or human peptide: des-acyl ghrelin may i) affect the insulin and glucose level in the body2,3),ii) be an anorexic peptide through corticotropin-releasing factor type 2 receptor activation upon i.p.
administration4,5), and iii) be an orexigenic peptide6). In this last paper reported by Dr. Nakazato's group, theyclarified that stimulation of food intake is observed upon i.c.v. injection of the peptide, and that this effect isgenerated through the orexin A neuron. Thus, they evaluated this effect to be afforded through a different target
protein other than GHSR.
As is obvious from these findings, functional roles of des-acyl ghrelin in the regulation of food consumption
seem to be largely conflicting. Therefore, further studies using synthetic des-acyl ghrelin are
required to reach concrete conclusions about the actual role of des-acyl ghrelin in the body.
1) H. Hosoda, M. Kojima, H. Matsuo, and K. Kangawa, Biochem. Biophys. Res. Commun., 279, 909 (2000).
(Endogenous Form)
2) F. Broglio, C. Gottero, F. Prodam, C. Gauna, G. Muccioli, M. Papotti, T. Abribat, A.J. Van Der Lely, and E. Ghigo,
J. Clin. Endocrinol. Metab., 89, 3062 (2004). (Pharmacol.; Antagonistic Effect)3) H. Iwakura, K. Hosoda, C. Son, J. Fujikura, T. Tomita, M. Noguchi, H. Ariyasu, K. Takaya, H. Masuzaki, Y. Ogawa,
T. Hayashi, G. Inoue, T. Akamizu, H. Hosoda, M. Kojima, H. Itoh, S. Toyokuni, K. Kangawa, and K. Nakao,
J. Biol. Chem., 280, 15247 (2005). (Pharmacol.; Effect on Glucose Metabolism)
4) A. Asakawa, A. Inui, M. Fujimiya, R. Sakamaki, N. Shinfuku, Y. Ueta, M.M. Meguid, and M. Kasuga, Gut, 54, 18(2005). (Pharmacol.; Anorexic Peptide)5) C.-Y. Chen, A. Inui, A. Asakawa, K. Fujino, I. Kato, C.-C. Chen, N. Ueno, and M. Fujimiya, Gastroenterology, 129, 8(2005). (Pharmacol.; Anorexic Peptide)6) K. Toshinai, H. Yamaguchi, Y. Sun, R.G. Smith, A. Yamanaka, T. Sakurai, Y. Date, M.S. Mondal, T. Shimbara,
T. Kawagoe, N. Murakami, M. Miyazato, K. Kangawa, and M. Nakazato, Endocrinology, 147, 2306 (2006).
(Pharmacol.; Orexigenic Peptide)7) J.-B. Soares, and A.F. Leite-Moreira, Peptides, 29, 1255 (2008). (Review)8) T. Inhoff, B. Wiedenmann, B.F. Klapp, H. Moennikes, and P. Kobelt, Peptides, 30, 991 (2009). (Review)

GIF See Code 4023 Somatostatin on page 141
GIP See Code 4178 GIP (Human) on page 68– 70 –

Glucagon
4098-sGlucagon (Human)
His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-TyrSer-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-GlnAsp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-20

(M.W. 3482.7)

Price:Yen

C153H225N43O49S

Vial

0.1 mg12,000[16941-32-5]

1) P.J. Lefebvre and R.H. Unger (eds.), Glucagon, Pergamon Press, Oxford, 1972. (Review)

Glucagon-like Peptides
1) E. Blázquez, E. Alvarez, M. Navarro, I. Roncero, F. Rodri́guez-Fonseca, J.A. Chowen, and J.A. Zueco, Mol. Neurobiol.,18, 157 (1998). (Review)2) G. van Dijk and T.E. Thiele, Neuropeptides, 33, 406 (1999). (Review)3) D.J. Drucker, Gut, 50, 428 (2002). (Review)

4344-v-20

Glucagon-like Peptide 1 (Human, 7-36 Amide)
GLP-1 (Human, 7-36 Amide)(Bovine, Canine, Rat, Guinea pig)
His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-ValSer-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-LysGlu-Phe-Ile-Ala-Trp-Leu-Val-Lys-Gly-Arg-NH2(M.W. 3297.6)

C149H226N40O45

Vial

0.5 mg29,000[107444-51-9]1) M.D. Turton, D. O'Shea, I. Gunn, S.A. Beak, C.M.B. Edwards, K. Meeran, S.J. Choi, G.M. Taylor, M.M. Heath,
P.D. Lambert, J.P.H. Wilding, D.M. Smith, M.A. Ghatei, J. Herbert, and S.R. Bloom, Nature, 379, 69 (1996).
(Original; CNS Effect on Feeding)2) M. Tang-Christensen, P.J. Larsen, R. Go
ke, A. Fink-Jensen, D.S. Jessop, M. Mller, and S.P. Sheikh,
Am. J. Physiol., 271, R848 (1996). (Original; CNS Effect on Drinking)3) G.van Dijk, T.E. Thiele, R.J. Seeley, S.C. Woods, and I.L. Bernstein, Nature, 385, 214 (1997). (Correspondence)

4280-v-20

Glucagon-like Peptide 1 (Human, 7-37)
GLP-1 (Human, 7-37)(Bovine, Canine, Rat, Guinea pig)
His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-ValSer-Ser-Tyr-Leu-Glu-Gly-Gln-Ala-Ala-LysGlu-Phe-Ile-Ala-Trp-Leu-Val-Lys-Gly-ArgGly(M.W. 3355.7)

C151H228N40O47

Vial

0.5 mg29,000[106612-94-6]

1) G.G. Holz IV, W.M. Ku
htreiber, and J.F. Habener, Nature, 361, 362 (1993). (Original)
2) G.S. Meneilly, C.H.S. McIntosh, R.A. Pederson, J.F. Habener, R. Gingerich, J.M. Egan, and D. Elahi, Diabetes Care,24, 964 (2001). (Pharmacol.)– 71 –and Proteins

CompoundBiologically Active Peptides

CodeGlucagon-like Peptides (continued)
Code

Compound4376-v

Glucagon-like Peptide 2 (Human)
GLP-2 (Human)
His-Ala-Asp-Gly-Ser-Phe-Ser-Asp-Glu-MetAsn-Thr-Ile-Leu-Asp-Asn-Leu-Ala-Ala-ArgAsp-Phe-Ile-Asn-Trp-Leu-Ile-Gln-Thr-LysIle-Thr-Asp-20

(M.W. 3766.1)

Price:Yen

C165H254N44O55S

Vial

0.5 mg29,000[223460-79-5]

Food Intake Suppressor
The proglucagon gene encodes glucagon, glucagon-like peptide 1 (GLP-1) and GLP-2 tandemly. Amongthese, the location and function of GLP-1 have long been studied, showing that GLP-1 is one of the typicalbrain-gut peptides and has pleiotropic functions, including stimulation of insulin gene expression, regulation offood and water intake, etc.
The chemical structure of GLP-2 in human ileum was reported to be identical to the 33 amino acid residue
peptide corresponding to proglucagon (126-158)1). GLP-2 is present in human plasma, the concentration ofwhich was shown to be elevated 3- to 4-fold after ingestion of a meal1). Further studies revealed that GLP-2's
immunoreactivity was distributed in rat brain, especially in the ventral part of the dorsomedial hypothalamic
nucleus (DMH) (and also found in the paraventricular and arcuate nuclei). Central administration of GLP-2
decreases food intake in ad libitum-fed rats at concentrations above 5 µg2). This inhibition is effective for ashort-duration. Surprisingly the GLP-1 receptor antagonist, exendin (9-39), reverses the GLP-2 induced
anorexia, although the GLP-2 receptor is expressed in the compact part of the DMH. In addition, GLP-2
decreases NPY-induced food intake by 40%, but this peptide does not affect angiotensin II-induced drinking
behavior2).
1) B. Hartmann, A.H. Johnsen, C. rskov, K. Adelhorst, L. Thim, and J.J. Holst, Peptides, 21, 73 (2000). (Pharmacol.)2) M. Tang-Christensen, P.J. Larsen, J. Thulesen, J. Rmer, and N. Vrang, Nat. Med., 6, 802 (2000). (Pharmacol.)3) D.J. Drucker, Gut, 50, 428 (2002). (Review)4) K. Wallis, J.R.F. Walters, and A. Forbes, Aliment. Pharmacol. Ther., 25, 365 (2007). (Review)5) P.E. Dubé and P.L. Brubaker, Am. J. Physiol. Endocrinol, Metab., 293, E460 (2007). (Review)6) K.J. Rowland and P.L. Brubaker, Mol. Cell. Endocrinol., 288, 63 (2008). (Review)7) R. Yazbeck, G.S. Howarth, and C.A. Abbott, Cytokine Growth Factor Rev., 20, 175 (2009). (Review)8) R. Yazbeck, C.A. Abbott, and G.S. Howarth, Curr. Opin. Investig. Drugs, 11, 440 (2010). (Review)

Glucose-dependent Insulinotropic Polypeptide (Human) See Code 4178 GIP (Human) on page 68
GnRH (Human) See Code 4013 LH-RH (Human) on page 90– 72 –

Growth Hormone Releasing Factor (GRF, GH-RH)
4127-sGRF (Human)
Growth Hormone Releasing Factor (Human)
Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-TyrArg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-ArgLys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-GlnGln-Gly-Glu-Ser-Asn-Gln-Glu-Arg-Gly-AlaArg-Ala-Arg-Leu-NH2-20

(M.W. 5039.7)

4127-v-20

Price:Yen

C215H358N72O66S

Vial

0.1 mg12,000Vial

0.5 mg41,000[83930-13-6]

GRF (Human)
Growth Hormone Releasing Factor (Human)

1) R. Guillemin, P. Brazeau, P. Bo
hlen, F. Esch, N. Ling, and W.B. Wehrenberg, Science, 218, 585 (1982).
(Original; Pancreatic Tumor)
2) N. Ling, F. Esch, P. Bo
hlen, P. Brazeau, W.B. Wehrenberg, and R. Guillemin, Proc. Natl. Acad. Sci. U.S.A.,
81, 4302 (1984). (Original; Hypothalamus)• This compound is distributed through Peptide Institute, Inc. under the license of The Salk Institute.

GRP See Code 4164 GRP (Human) on page 68
GRP (18-27) See Code 4153 Neuromedin C on page 102– 73 –and Proteins

CompoundBiologically Active Peptides

CodeGsMTx-4
CodeCompound4393-sGsMTx-4(Chilean Rose Tarantula, Grammostola spatulata)
Gly-Cys-Leu-Glu-Phe-Trp-Trp-Lys-Cys-AsnPro-Asn-Asp-Asp-Lys-Cys-Cys-Arg-Pro-LysLeu-Lys-Cys-Ser-Lys-Leu-Phe-Lys-Leu-CysAsn-Phe-Ser-Phe-NH2-20

Price:Yen
Vial

0.1 mg22,000(Reported disulfide bonds between Cys2-Cys17, Cys9-Cys23, and Cys16-Cys30)(M.W. 4095.8)

C185H273N49O45S6

Inhibitor for Cation-Selective Stretch-Activated Channels / Atrial Fibrillation Inhibiting Peptide
Mechanosensitive ion channels (MSCs) are ubiquitous from unicellular to multicellular organisms andparticipate in numerous physiological processes including touch and pain sensation, salt and fluid balance,
blood pressure control, cell volume regulation, and turgor control1). Analysis of the functions mediated by thesechannels can be performed by utilizing a specific blocker with high selectivity to the particular channels. In the
research of stretch-activated ion channels (SACs), one of MSCs, cationic metal, Gd 3+ , and cationiccompounds including amiloride, and cationic antibiotics were used as blockers, but reported to be
non-selective (lack of specificity). In 2000, Professor F. Sachs of State University of New York at Buffalo
discovered a peptidic toxin named GsMTx-4 in the venom of the tarantula Grammostola spatulata and reported
it to possess a specific blocking activity for stretch-activated currents2). GsMTx-4 blocks: i) SAC current inoutside-out patches from adult rat astrocytes (Kd=630 nM); ii) swelling-activated whole cell current (aninwardly rectifying cation selective current) in cardiac myocytes at 400 nM, (but not an outwardly rectifying
Cl- current); and iii) MSC current in normal rat kidney cells at 5 µM2, 3). Also, this peptide inhibits the atrial
fibrillation associated with dilatation at 170 nM (anti-arrhythmic activity)1, 4).
Primary sequence of GsMTx-4 was clarified by cDNA cloning to be a 34-residue peptide possessing a
post-translationally modified amide structure at its carboxyl-terminus3). Three disulfide linkages in themolecule were connected in the pattern of Cys1-Cys4, Cys2-Cys5, and Cys3-Cys6 (Cys numbering from theamino-terminus) during the determination of its solution structure, indicating that GsMTx-4 is a member of"inhibitor cystine knot" peptides5). GsMTx-4 should prove to be a useful tool for the study of the biologicalevents initiated by the activation and inactivation of SACs. GsMTx–4 also blocked the activation of TRPC6(transient receptor potential channel 6) channels, expressed widely in vascular smooth muscle, is also reported6).
1) O.P. Hamill and B. Martinac, Physiol. Rev., 81, 685 (2001). (Review; MSCs)
2) T.M. Suchyna, J.H. Johnson, K. Hamer, J.F. Leykam, D.A. Gage, H.F. Clemo, C.M. Baumgarten, and F. Sachs,
J. Gen. Physiol., 115, 583 (2000). (Original)
3) K.L. Ostrow, A. Mammoser, T. Suchyna, F. Sachs, R. Oswald, S. Kubo, N. Chino, and P.A. Gottlieb,
Toxicon, 42, 263 (2003). (Primary structure; cDNA Seq. & Pharmacol.)4) F. Bode, F. Sachs, and M.R. Franz, Nature, 409, 35 (2001). (Pharmacol.)5) R.E. Oswald, T.M. Suchyna, R. McFeeters, P. Gottlieb, and F. Sachs, J. Biol. Chem., 277, 34443 (2002).
(Solution Structure & S-S Bond)6) M.A. Spassova, T. Hewavitharana, W. Xu, J. Soboloff, and D.L. Gill, Proc. Natl. Acad. Sci. U.S.A., 103, 16586 (2006).
(Pharmacol.)7) C.L. Bowman, P.A. Gottlieb, T.M. Suchyna, Y.K. Murphy, and F. Sachs, Toxicon, 49, 249 (2007). (Review)• This product is distributed under the license of the Research Foundation of State University of New York. Its use forany purpose other than research is strictly prohibited.

– 74 –

Guangxitoxin-1E
4433-sGuangxitoxin-1E
GxTX-1E(Tarantula, Plesiophrictus guangxiensis sp. nov.)-20

Price:Yen
Vial

0.1 mg22,000(Trifluoroacetate Form)

Glu-Gly-Glu-Cys-Gly-Gly-Phe-Trp-Trp-LysCys-Gly-Ser-Gly-Lys-Pro-Ala-Cys-Cys-ProLys-Tyr-Val-Cys-Ser-Pro-Lys-Trp-Gly-LeuCys-Asn-Phe-Pro-Met-Pro(Reported disulfide bonds between Cys4-Cys19, Cys11-Cys24, and Cys18-Cys31)(M.W. 3948.6)

C178H248N44O45S7
Purity Information: Q E See page IV (XVI)

Kv2.1/Kv2.2 Channel Blocker / Enhancer of Glucose-Dependent Insulin Secretion
Peptides with selective channel blocking activity have been used to clarify the specific function of thechannels. Among them, guangxitoxin-1E ( GxTX-1E ), which was isolated from the venom of spider(Plesiophrictus guangxiensis sp. nov.), was identified as a unique blocker for the K+ channels1).
GxTX-1E blocks Kv2.1 and Kv2.2 (and to a lesser extent Kv4.3) selectively, with a half-maximal
concentration of less than 1 nM. Furthermore, this peptide does not significantly affect the other K+ channels, Ca2+
channels, nor Na+ channels. In mouse β-cells, GxTX-1E inhibits 90% of delayed-rectifier K+ current (IDR) and, as
for Kv2.1, shifts the voltage dependence of channel activation to more depolarized potentials, acharacteristic of gating-modifier peptide. Kv2.1 voltage-dependent K+ channels are known to be involved in i)enhancement of glucose-dependent insulin secretion2) and ii) regulation of the pancreatic β-cell Ca2+ response
to glucose3).
All these effects are attractive characteristics in relation to an investigation into the etiology of type 2
diabetes. Therefore, GxTX-1E would be useful tool for the diabetic research.
1) J. Herrington, Y.-P. Zhou, R.M. Bugianesi, P.M. Dulski, Y. Feng, V.A. Warren, M.M. Smith, M.G. Kohler, V.M.
Garsky, M. Sanchez, M. Wagner, K. Raphaelli, P. Banerjee, C. Ahaghotu, D. Wunderler, B.T. Priest, J.T. Mehl,
M.L. Garcia, O.B. McManus, G.J. Kaczorowski, and R.S. Slaughter, Diabetes, 55, 1034 (2006). (Original)
2) P.E. MacDonald, S. Sewing, J. Wang, J.W. Joseph, S.R. Smukler, G. Sakellaropoulos, J. Wang, M.C. Saleh, C.B. Chan,
R.G. Tsushima, A.M.F. Salapatek, and M.B. Wheeler, J. Biol. Chem., 277, 44938 (2002). (Pharmacol.; Role of Kv2.1
in Glucose-Dependent Insulin Secretion)3) N.A. Tamarina, A. Kuznetsov, L.E. Fridlyand, and L.H. Philipson, Am. J. Physiol. Endocrinol. Metab., 289, E578
(2005). (Pharmacol.; Role of Kv2.1 in Glucose-Dependent Ca2+ response)
4) J. Herrington, Toxicon, 49, 231 (2007). (Review)5) S. Lee, M. Milescu, H.H. Jung, J.Y. Lee, C.H. Bae, C.W. Lee, H.H. Kim, K.J. Swartz, and J.I. Kim, Biochemistry, 49,5134 (2010). (Solution Structure & S-S Bond)– 75 –and Proteins

CompoundBiologically Active Peptides

CodeGuanylins and Uroguanylins
1) L.R. Forte and M.G. Currie, FASEB J., 9, 643 (1995). (Review)2) L.R. Forte, X.H. Fan, and F.K. Hamra, Am. J. Kidney Dis., 28, 296 (1996). (Review)3) L.R. Forte, Jr., Pharmacol. Ther., 104, 137 (2004). (Review)

Code

Compound4274-sGuanylin (Human)
Pro-Gly-Thr-Cys-Glu-Ile-Cys-Ala-Tyr-AlaAla-Cys-Thr-Gly-Cys-20

Price:Yen
Vial

0.1 mg10,000(Disulfide bonds between Cys4-Cys12 and Cys7-Cys15)(M.W. 1458.7)

C58H87N15O21S4[183200-12-6]

Guanylate Cyclase C Activator
1) R.C. Wiegand, J. Kato, M.D. Huang, K.F. Foc, J.F. Kachur, and M.G. Currie, FEBS Lett., 311, 150 (1992).
(Original; cDNA)2) F.J. de Sauvage, S. Keshav, W.-J. Kuang, N. Gillett, W. Henzel, and D.V. Goeddel, Proc. Natl. Acad. Sci. U.S.A.,89, 9089 (1992). (Original; cDNA)3) M. Kuhn, M. Raida, K. Adermann, P. Schulz-Knappe, R. Gerzer, J.-M. Heim, and W.-G. Forssmann, FEBS Lett.,
318, 205 (1993). (Circulating Form)
4) O. Hill, M. Kuhn, H.-D. Zucht, Y. Cetin, H. Kulaksiz, K. Adermann, G. Klock, G. Rechkemmer, W.-G. Forssmann,and H.-J. Maegert, Proc. Natl. Acad. Sci. U.S.A., 92, 2046 (1995). (Immunohistochem.)

4275-s-20

Guanylin (Rat, Mouse)
Pro-Asn-Thr-Cys-Glu-Ile-Cys-Ala-Tyr-AlaAla-Cys-Thr-Gly-Cys

Vial

0.1 mg10,000(Disulfide bonds between Cys4-Cys12 and Cys7-Cys15)(M.W. 1515.7)

C60H90N16O22S4

Guanylate Cyclase C Activator
1) M.G. Currie, K.F. Fok, J. Kato, R.J. Moore, F.K. Hamra, K.L. Duffin, and C.E. Smith, Proc. Natl. Acad. Sci. U.S.A.,89, 947 (1992). (Original; Rat )2) R.C. Wiegand, J. Kato, and M.G. Currie, Biochem. Biophys. Res. Commun., 185, 812 (1992). (Original; Rat cDNA)
3) S. Schults, T.D. Chrisman, and D.L. Garbers, J. Biol. Chem., 267, 16019 (1992). (Tissue Distribution)4) F.J. de Sauvage, S. Keshav, W.-J. Kuang, N. Gillett, W. Henzel, and D.V. Goeddel, Proc. Natl. Acad. Sci. U.S.A.,89, 9089 (1992). (Original; Mouse cDNA)

4354-s-20

Uroguanylin (Rat)
Thr-Asp-Glu-Cys-Glu-Leu-Cys-Ile-Asn-ValAla-Cys-Thr-Gly-Cys

Vial

0.1 mg10,000(Disulfide bonds between Cys4-Cys12 and Cys7-Cys15)(M.W. 1569.8)

C60H96N16O25S4Guanylate Cyclase C Activator / Natriuretic Factor
1) M. Nakazato, H. Yamaguchi, Y. Date, M. Miyazato, K. Kangawa, M.F. Goy, N. Chino, and S. Matsukura,
Endocrinology, 139, 5247 (1998). (Original)
2) H. Ieda, S. Naruse, M. Kitagawa, H. Ishiguro, and T. Hayakawa, Regul. Pept., 79, 165 (1999). (Pharmacol.)3) H. Fukae, H. Kinoshita, S. Fujimoto, T. Kita, M. Nakazato, and T. Eto, Nephron, 92, 373 (2002).
(Pharmacol.; Natriuretic Activity)4) M. Kikuchi, S. Fujimoto, H. Fukae, H. Kinoshita, T. Kita, M. Nakazato, and T. Eto, J. Am. Soc. Nephrol., 16, 392(2005). (Pharmacol.; Natriuretic Activity)– 76 –

Guanylins and Uroguanylins (continued)
Price:Yen

4295-sUroguanylin Isomer A (Human)-20

(Trifluoroacetate Form)

Vial

0.1 mg9,000

Asn-Asp-Asp-Cys-Glu-Leu-Cys-Val-Asn-ValAla-Cys-Thr-Gly-Cys-Leu(Disulfide bonds between Cys4-Cys12 and Cys7-Cys15)(M.W. 1667.9)

C64H102N18O26S4[154525-25-4]

Purity Information: Qz See page IV (XVI)

Guanylate Cyclase C Activator
1) T. Kita, C.E. Smith, K.F. Fok, K.L. Duffin, W.M. Moore, P.J. Karabatsos, J. F. Kachur, F.K. Hamra, N.V. Pidhorodeckyj,
L.R. Forte, and M.G. Currie, Am. J. Physiol., 266, F342 (1994). (Original)
2) M. Nakazato, H. Yamaguchi, H. Kinoshita, K. Kangawa, H. Matsuo, N. Chino, and S. Matsukura, Biochem. Biophys.
Res. Commun., 220, 586 (1996). (GC-C Stimulating Activity of Topological Isomers)3) H. Kinoshita, S. Fujimoto, M. Nakazato, N. Yokota, Y. Date, H. Yamaguchi, S. Hisanaga, and T. Eto , Kidney Int.,52, 1028 (1997). (Urine/Plasma Level; Renal Disease)4) N. Chino, S. Kubo, T. Kitani, T. Yoshida, R. Tanabe, Y. Kobayashi, M. Nakazato, K. Kangawa, and T. Kimura,
FEBS Lett., 421, 27 (1998). (Interconversion of Topological Isomers)5) N.G. Moss, D.A. Riguera, R.M. Solinga, M.M. Kessler, D.P. Zimmer, W.J. Arendshorst, M.G. Currie, and M.F. Goy,
Hypertension, 53, 867 (2009). (Natriuretic Activity of Topological Isomers)– 77 –and Proteins

CompoundBiologically Active Peptides

CodeGuanylins and Uroguanylins (continued)
Code

Compound4463-sUroguanylin Isomer B (Human)

New

-20

Price:Yen
Vial

0.1 mg9,000(Trifluoroacetate Form)

Asn-Asp-Asp-Cys-Glu-Leu-Cys-Val-Asn-ValAla-Cys-Thr-Gly-Cys-Leu(Disulfide bonds between Cys4-Cys12 and Cys7-Cys15)(M.W. 1667.9)

C64H102N18O26S4Natriuretic Factor
Uroguanylin is a well-known activator of guanylyl cyclase-C (GC-C) in the intestine. Regulation of
natriuresis in the kidney postprandial is another important function of this peptide1). In the case of humanuroguanylin2), the so-called topological isomers (isomer A and isomer B in this catalog) are generated becauseof the carboxyl-terminal extension of Leu residue from the core structure formed by two disulfide bonds in a
1-3/2-4 pattern resulting in the stabilization of two topological stereoisomers. Isomer A (Code 4295-s)
stimulates GC-C, whilst isomer B is a weak agonist in this assay3). What is the biological role of isomer B? The
answer was obtained recently, that is, isomer B possesses natriuretic activity4) with a sigmoidal dose-response
curve (ED50 = 20 nmol/kg in rats). It is of interest that isomer A also shows natriuretic activity at 25 nmol/kg,
however, a distinct bell-shaped dose-response curve was observed. Furthermore, co-administration of isomer A(100 nmol/kg) and isomer B (35 nmol/kg) induced almost as efficient natriuretic response as that of a mere
administration of isomer A, indicating that a large amount of coexisting isomer A antagonize, even in part, thenatriuretic activity of isomer B. Considering the report that uroguanylin and guanlylin exert natriuretic activity
in mice even lacking the GC-C receptor5), the natriuresis of uroguanylin might be mediated by a novel receptor
other than GC-C.
The availability of synthetic human uroguanylin isomer A and isomer B should allow for more precise
research to help clarify the complicated biological response of the individual topological isomers.
Please note: It has been reported that isomer A and isomer B of human uroguanylin are interconvertible insolution6). Keeping the prepared solution at low temperature (below 4 ) should help avoid this possible
interconversion.
1) L.R. Forte, J. Clin. Invest., 112. 1138 (2003). (Review: Natriuretic Factor)
2) T. Kita, C.E. Smith, K.F. Fok, K.L. Duffin, W.M. Moore, P.J. Karabatsos, J. F. Kachur, F.K. Hamra, N.V. Pidhorodeckyj,
L.R. Forte, and M.G. Currie, Am. J. Physiol., 266, F342 (1994). (Original)
3) M. Nakazato, H. Yamaguchi, H. Kinoshita, K. Kangawa, H. Matsuo, N. Chino, and S. Matsukura,
Biochem. Biophys. Res. Commun., 220, 586 (1996). (GC-C Stimulating Activity of Topological Isomers)4) N.G. Moss, D.A. Riguera, R.M. Solinga, M.M. Kessler, D.P. Zimmer, W.J. Arendshorst, M.G. Currie, and M.F. Goy,
Hypertension, 53, 867 (2009). (Natriuretic Activity of Topological Isomers)5) S.L. Carrithers, C.E. Ott, M.J. Hill, B.R. Johnson, W. Cai, J.J. Chang, R.G. Shah, C. Sun, E.A. Mann, M.C. Fonteles,
L.R. Forte, B.A. Jackson, R.A. Giannella, and R.N. Greenberg, Kidney Int., 65, 40 (2004).
(GC-C-Independent Natriuretic Activity)
6) N. Chino, S. Kubo, T. Kitani, T. Yoshida, R. Tanabe, Y. Kobayashi, M. Nakazato, K. Kangawa, and T. Kimura,
FEBS Lett., 421, 27 (1998). (Interconversion of Topological Isomers)– 78 –

Hepcidins
4392-s

Hepcidin / LEAP-1 (Human)
Liver-Expressed Antimicrobial Peptide 1 (Human)
Asp-Thr-His-Phe-Pro-Ile-Cys-Ile-Phe-CysCys-Gly-Cys-Cys-His-Arg-Ser-Lys-Cys-GlyMet-Cys-Cys-Lys-Thr-20

Price:Yen
Vial

0.1 mg18,000(Reported disulfide bonds between Cys7-Cys23, Cys10-Cys13, Cys11-Cys19, and Cys14-Cys22)(M.W. 2789.4)

C113H170N34O31S9[342790-21-0]

Iron-Regulatory Hormone / Liver-Specific Antimicrobial Peptide
Hepcidin/LEAP-1 (Human) contains 8 Cys residues, disulfide connectivity of which was first determined to
be Cys7-Cys23, Cys10-Cys22, Cys11-Cys19, and Cys13-Cys14 based on the results from NMR analysis of the synthetic
peptide4). Recently, this connectivity has been revised to be Cys7-Cys23, Cys10-Cys13, Cys11-Cys19, andCys14-Cys22 using the natural peptide from urine, two recombinant peptides expressed in CHO cells or E. coli,
and the chemically synthesized peptide5). Methods applied to determine this newly reported connectivity
include: NMR, X-ray crystallography of the anti-hepcidin/LEAP-1 antibody Fab complex, and disulfide mappingby partial reduction/alkylation procedure. Based on these experimental facts, we have now changed thedisulfide connectivity of our hepcidin/LEAP-1 (Human) to the newly reported one, that is, (Reported disulfide
bonds between Cys7-Cys23, Cys10-Cys13, Cys11-Cys19, and Cys14-Cys22).
1) A. Krause, S. Neitz, H.-J. Ma
gert, A. Schulz, W.-G. Forssmann, P. Schulz-Knappe, and K. Adermann,
FEBS Lett., 480, 147 (2000). (Original; LEAP-1)
2) C.H. Park, E.V. Valore, A.J. Waring, and T. Ganz, J. Biol. Chem., 276, 7806 (2001). (Original; Hepcidin)
3) T. Ganz and E. Nemeth, Am. J. Physiol. Gastrointest. Liver Physiol., 290, G199 (2006). (Review)4) H.N. Hunter, D.B. Fulton, T. Ganz, and H.J. Vogel, J. Biol. Chem., 277, 37597 (2002).
(Previously published S-S Bond Connectivity)
5) J.B. Jordan, L. Poppe, M. Haniu, T. Arvedson, R. Syed, V. Li, H. Kohno, H. Kim, P.D. Schnier, T.S. Harvey,
L.P. Miranda, J. Cheetham, and B.J. Sasu, J. Biol. Chem., 284, 24155 (2009).
(Newly published S-S Bond Connectivity)• Note about the Description of Disulfide Bondage: In this catalog we use three descriptions, from i) to iii),
to show the disulfide connectivity of our items.
i) (Disulfide bond(s) between .....) = disulfide connectivity of our synthetic peptide is ascertained byourselves.
ii) (Reported disulfide bonds between .....) = disulfide connectivity of our synthetic peptides has not yet
been determined by us and consequently, the disulfide connectivity in reported literature is shown after
confirming the biological activity and/or chromatographic behavior of our synthetic products to be
identical to those of the natural peptides.
iii) (Disulfide bonds undetermined) = as far as we know, disulfide connectivity of the titled peptide has not
yet been reported in the literature.

– 79 –and Proteins

CompoundBiologically Active Peptides

CodeHepcidins (continued)
Code

Compound4434-s

Hepcidin 1 (Mouse)
Asp-Thr-Asn-Phe-Pro-Ile-Cys-Ile-Phe-CysCys-Lys-Cys-Cys-Asn-Asn-Ser-Gln-Cys-GlyIle-Cys-Cys-Lys-Thr-20

Price:Yen
Vial

0.1 mg22,000(Disulfide bonds undetermined)(M.W. 2754.2)

C111H169N31O35S8

Iron-Regulatory Hormone
Liver-expressed antimicrobial peptide 1 (LEAP-1), isolated from the ultrafiltrate of human plasma, was firstreported in 20001). The same peptide with another name, hepcidin2), appeared in 2001 soon after LEAP-1 hadbeen reported, which was followed by the discovery of mouse hepcidin3). In mouse, two hepcidins, hepcidin 1
and 2, were identified, where the amino acid sequence homology of hepcidin 1 to human hepcidin/LEAP-1(Code 4392-s) is higher than that of hepcidin 23,4). Human LEAP-2 (Code 4405-s) was also reported as thesecond component of the LEAP peptide5), in which both primary structure and the number of disulfide bonds inthe molecule differ significantly from those of human hepcidin/LEAP-1, as well as hepcidin 1 and 2 in mouse.
Hepcidin/LEAP-1 was found to be a member of antimicrobial peptides when human peptide was isolated1,2).
In contrast to this, mouse hepcidin (hepcidin 1) was discovered from the search of the gene that is up-regulated
in the liver under the iron overloaded conditions3). Now, it is generally accepted that hepcidin is linked to theiron homeostasis in the body. Ferroportin, an iron exporter on the cell surface, was revealed to have an ironreleasing function from the store (thus it is suggested to be a plausible receptor for hepcidin)6). Taken together,hepcidin is considered to be an iron regulatory hormone7). Secretion of hepcidin/LEAP-1 is modulated byinflammation as well as iron status in the body8), indicating that the hepcidin/LEAP-1 peptides clearly possess atleast two distinct functions essential for the life of the humans.
We introduced synthetic Hepcidin 1 (Mouse) as one of our items, by which the research for investing themechanism of the function of the hepcidin/LEAP-1 peptides, especially the role of these peptides in theiron-related disease should be stimulated.
1) A. Krause, S. Neitz, H.-J. Ma
ert, A. Schulz, W.-G. Forssmann, P. Schulz-Knappe, and K. Adermann, FEBS Lett., 480,
147 (2000). (Original; LEAP-1)
2) C.H. Park, E.V. Valore, A.J. Waring, and T. Ganz, J. Biol. Chem., 276, 7806 (2001). (Original; Hepcidin)
3) C. Pigeon, G. Ilyin, B. Courselaud, P. Leroyer, B. Turlin, P. Brissot, and O. Loréal, J. Biol. Chem., 276, 7811 (2001).
(Original; Mouse Hepcidin 1 & 2 / Fe Regulatory Hormone)4) G. Ilyin, B. Courselaud, M.-B. Troadec, C. Pigeon, M. Alizadeh, P. Leroyer, P. Brissot, and O. Loréal, FEBS Lett., 542,
22 (2003). (Original; Mouse Hepcidin 1 & 2)
5) A. Krause, R. Sillard, B. Kleemeier, E. Klu
er, E. Maronde, J.R. Conejo-Garc́a, W.G. Forssmann, P. Schulz-Knappe,
M.C. Nehls, F. Wattler, S. Wattler, and K. Adermann, Protein Sci., 12, 143 (2003). (Original; LEAP-2)
6) E. Nemeth, M.S. Tuttle, J. Powelson, M.B. Vaughn, A. Donovan, D. McVey Ward, T. Ganz, and J. Kaplan, Science,
306, 2090 (2004). (Ferroportin; Hepcidin Receptor)
7) T. Ganz and E. Nemeth, Am. J. Physiol. Gastrointest. Liver Physiol., 290, G199 (2006). (Review; Hepcidin)8) G. Nicolas, C. Chauvet, L. Viatte, J.L. Danan, X. Bigard, I. Devaux, C. Beaumont, A. Kahn, and S. Vaulont,
J. Clin. Invest., 110, 1037 (2002). (Pharmacol.; Regulation of Hepcidin mRNA)– 80 –

Histatin
4270-sHistatin 5 (Human)
Asp-Ser-His-Ala-Lys-Arg-His-His-Gly-TyrLys-Arg-Lys-Phe-His-Glu-Lys-His-His-SerHis-Arg-Gly-Tyr-20

(M.W. 3036.3)

Price:Yen

C133H195N51O33

Vial

0.1 mg14,000[104339-66-4]

Parotid Histidine–rich Protein / Salivary Antimicrobial Peptide
1) F.G. Oppenheim, T. Xu, F.M. McMillian, S. M.Levitz, R.D. Diamond, G.D. Offner, and R.F. Troxler, J. Biol. Chem.,
263, 7472 (1988). (Original)
2) P.A. Raj, M. Edgerton, and M.J. Levine, J. Biol. Chem., 265, 3898 (1990). (Pharmacol.)3) Y. Murakami, T. Takeshita, S. Shizukuishi, A. Tsunemitsu, and S. Aimoto, Arch. Oral Biol., 35, 775 (1990).
(Pharmacol.)4) M. Nishikata, T. Kanehira, H. Oh, H. Tani, M. Tazaki, and Y. Kuboki, Biochem. Biophys. Res. Commun.,
174, 625 (1991). (Pharmacol.)hBD-1 See Code 4337 β-Defensin-1 (Human) on page 51
hBD-2 See Code 4338 β-Defensin-2 (Human) on page 51
hBD-3 See Code 4382 β-Defensin-3 (Human) on page 52
hBD-4 See Code 4406 β-Defensin-4 (Human) on page 53
HD-5 See Code 4415 α-Defensin-5 (Human) on page 49
HD-6 See Code 4458 α-Defensin-6 (Human) on page 50
hL8C See Code 4403 Neuropeptide W-30 (Human) on page 109
HNP-1 See Code 4271 α-Defensin-1 (Human) on page 46
HNP-2 See Code 4428 α-Defensin-2 (Human) on page 46
HNP-3 See Code 4416 α-Defensin-3 (Human) on page 47
HNP-4 See Code 4431 α-Defensin-4 (Human) on page 48– 81 –and Proteins

CompoundBiologically Active Peptides

CodeHumanins
1) I. Nishimoto, M. Matsuoka, and T. Niikura, Trends Mol. Med., 10, 102 (2004). (Review)
2) T. Arakawa, Y. Kita, and T. Niikura, Curr. Med. Chem., 15, 2086 (2008). (Review)

Code

CompoundPrice:Yen

4384-v

Humanin-20

(Trifluoroacetate Form)

Vial

0.5 mg25,000Vial

0.5 mg10,000

Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-LeuLeu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-ValLys-Arg-Arg-Ala(M.W. 2687.2)

C119H204N34O32S2[330936-69-1]

Purity Information: Qz See page IV (XVI)

Endogenous Rescue Factor Abolishing Neuronal Cell Death4385-v[Gly14]-Humanin-20

(Trifluoroacetate Form)

Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-LeuLeu-Leu-Thr-Gly-Glu-Ile-Asp-Leu-Pro-ValLys-Arg-Arg-Ala(M.W. 2657.2) C118H202N34O31S2 [330936-70-4]
Purity Information: Qz See page IV (XVI)

Potent Rescue Factor Abolishing Neuronal Cell Death1) Y. Hashimoto, T. Niikura, H. Tajima, T. Yasukawa, H. Sudo, Y. Ito, Y. Kita, M. Kawasumi, K. Kouyama, M. Doyu,
G. Sobue, T. Koide, S. Tsuji, J. Lang, K. Kurokawa, and I. Nishimoto, Proc. Natl. Acad. Sci. U.S.A., 98, 6336 (2001).
(Original)
2) Y. Hashimoto, Y. Ito, T. Niikura, Z. Shao, M. Hata, F. Oyama, and I. Nishimoto, Biochem. Biophys. Res. Commun.,
283, 460 (2001). (Pharmacol.)3) T. Mamiya and M. Ukai, Br. J. Pharmacol., 134, 1597 (2001). (Pharmacol.)4) S. Kariya, N. Takahashi, N. Ooba, M. Kawahara, H. Nakayama, and S. Ueno, Neurochemistry, 13, 903 (2002).
(Pharmacol.)5) S.S. Jung and W.E. Van Nostrand, J. Neurochem., 84, 266 (2003). (Pharmacol.)IAPP See Code 4219 Amylin (Human) and Code 4220 Amylin (Rat) on page 10– 82 –

Huwentoxin
4455-sHuwentoxin-IV
HWTX-IV(Chinese Bird Spider, Ornithoctonus huwena)

New

-20

Price:Yen
Vial

0.1 mg22,000(Trifluoroacetate Form)

Glu-Cys-Leu-Glu-Ile-Phe-Lys-Ala-Cys-AsnPro-Ser-Asn-Asp-Gln-Cys-Cys-Lys-Ser-SerLys-Leu-Val-Cys-Ser-Arg-Lys-Thr-Arg-TrpCys-Lys-Tyr-Gln-Ile-NH2(Disulfide bonds between Cys2-Cys17, Cys9-Cys24, and Cys16-Cys31)(M.W. 4106.8)

C174H278N52O51S6

Purity Information : QE See page IV (XVI)

Neuronal Tetrodotoxin-Sensitive Na+Channel Blocker
Huwentoxin-IV was isolated from the venom of the Chinese bird spider Ornithoctonus huwena. Its structure
was elucidated to be a 35-residue peptide with three disulfide linkages which are arranged to form the inhibitor
cystine knot1,2). Huwentoxin-IV is a potent inhibitor of neuronal tetrodotoxin-sensitive Na+ channels with IC50
= 30 nM1). Further studies clarified that i) among neuronal voltage-gated Na+ channels, human Nav1.7 is mostsensitive to huwentoxin-IV where site 4 of the channel is the interacting site (IC50 = 26 nM)3), and ii)
huwentoxin-IV interacts with central Na+ channel isoforms from rat hippocampus neurons, while the affinity islow (IC50 = ～ 0.4 µM)4). Interestingly, huwentoxin-IV fails to partition into the artificial membrane bilayers,
indicating that the mechanism for blocking Na+ channels by huwentoxin-IV is distinct from that of ProTx-II(Code 4450-s), another Na+ channel blocker isolated from the tarantula4).
Our list of Na+ channel blocker (see page on 42) may facilitate the research of antinociceptive drug
discovery.
1) K. Peng, Q. Shu, Z. Liu, and S. Liang, J. Biol. Chem., 277, 47564 (2002). (Original)
2) J. Diao, Y. Lin, J. Tang, and S. Liang, Toxicon, 42, 715 (2003). (cDNA Seq.)
3) Y. Xiao, J.-P. Bingham, W. Zhu, E. Moczydlowski, S. Liang, and T.R. Cummins, J. Biol. Chem., 283, 27300 (2008).
(Pharmacol.)4) Y. Xiao, X. Luo, F. Kuang, M. Deng, M. Wang, X. Zeng, and S. Liang, Toxicon, 51, 230 (2008). (Pharmacol.)Iberiotoxin
4235-s-20

Iberiotoxin*
IbTX(Scorpion, Buthus tamulus)
Pyr-Phe-Thr-Asp-Val-Asp-Cys-Ser-Val-SerLys-Glu-Cys-Trp-Ser-Val-Cys-Lys-Asp-LeuPhe-Gly-Val-Asp-Arg-Gly-Lys-Cys-Met-GlyLys-Lys-Cys-Arg-Cys-Tyr-Gln

Vial

0.1 mg23,000(Disulfide bonds between Cys7-Cys28, Cys13-Cys33, and Cys17-Cys35)(M.W. 4230.8)
2+

C179H274N50O55S7[129203-60-7]+

Ca -Activated K Channel Blocker (Maxi-K+ Channel Blocker)
1) A. Galvez, G. Gimenez-Gallego, J.P. Reuben, L. Roy-Contancin, P. Feigenbaum, G.J. Kaczorowski, and M.L. Garcia,
J. Biol. Chem., 265, 11083 (1990). (Original)
2) M.L. Garcia, A. Galvez, M. Garcia-Calvo, V.F. King, J. Vazquez, and G. J. Kaczorowski, J. Bioenerg. Biomembr.,23, 615 (1991). (Review)3) K.M. Giangiacomo, M.L. Garcia, and O.B. McManus, Biochemistry, 31, 6719 (1992). (Pharmacol.)4) G. J. Kaczorowski, H.-G. Kaus, R.J. Leonard, O.B. McManus, and M.L. Garcia, J. Bioenerg. Biomembr.,28, 255 (1996). (Review)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 83 –and Proteins

CompoundBiologically Active Peptides

CodeImperatoxin
Code

Compound4343-sImperatoxin A
IpTXa(Scorpion, Pandinus imperator)
Gly-Asp-Cys-Leu-Pro-His-Leu-Lys-Arg-CysLys-Ala-Asp-Asn-Asp-Cys-Cys-Gly-Lys-LysCys-Lys-Arg-Arg-Gly-Thr-Asn-Ala-Glu-LysArg-Cys-Arg-20

Price:Yen
Vial

0.1 mg22,000(Reported disulfide bonds between Cys3-Cys17, Cys10-Cys21, and Cys16-Cys32)(M.W. 3758.4) C148H254N58O45S6
Purity: higher than 94% by HPLC

[172451-37-5]

Activator of Ca2+ Release Channels / Ryanodine Receptors
1) H.H. Valdivia, M.S. Kirby, W.J. Lederer, and R.Coronado, Proc. Natl. Acad. Sci. U.S.A., 89, 12185 (1992).
(Pharmacol.)2) R. El-Hayek, A.J. Lokuta, C. Arévalo, and H.H. Valdivia, J. Biol. Chem., 270, 28696 (1995). (Pharmacol.)3) F.Z. Zamudio, G.B. Gurrola, C. Arévalo, R. Sreekumar, J.W. Walker, H.H. Valdivia, and L.D. Possani, FEBS Lett.,
405, 385 (1997). (Original; Structure)4) K. Takeuchi, J.I. Kim, H. Takahashi, K. Sato, and I. Shimada, Peptide Science 1999, 307 (2000). (S-S Bond)

Insulin
1) E. Dorzbach (ed.), Insulin I, Handbook of Experimental Pharmacology, Vol. 32 (1), Springer-Verlag, Berlin, 1971. (Review)2) A. Hasselblatt and F.V. Bruchhausen (eds.), Insulin II, Handbook of Experimental Pharmacology, Vol. 32 (2), Springer-Verlag,
Berlin, 1975. (Review)

4088-s-20

Insulin (Human)
Vial
0.1 mg13,000
Enzymatically Derived from Porcine Insulin
A-chain:
Gly-Ile-Val-Glu-Gln-Cys-Cys-Thr-Ser-Ile-Cys-Ser-Leu-Tyr-Gln-Leu-Glu-Asn-Tyr-Cys-Asn
B-chain:
Phe-Val-Asn-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val-Cys-GlyGlu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Thr(Disulfide bonds between CysA6-CysA11, CysA7-CysB7, and CysA20-CysB19)(M.W. 5807.6)

4088-v-20

C257H383N65O77S6[11061-68-0]

Insulin (Human)
Enzymatically Derived from Porcine Insulin

Vial

0.5 mg44,000Purity Information : Q E See page IV (XVI)
1) K. Morihara, T. Oka, and H. Tsuzuki, Nature, 280, 412 (1979). (Semi-Synthesis)2) K. Morihara, T. Oka, H. Tsuzuki, Y. Tochino, and T. Kanaya, Biochem. Biophys. Res. Commun., 92, 396 (1980).
(Semi-Synthesis)Intermedin (Human) See Code 4421 Adrenomedullin 2 / Intermedin (Human) on page 4Intermedin (Rat) See Code 4422 Adrenomedullin 2 / Intermedin (Rat) on page 4
IpTXa See Code 4343 Imperatoxin A above
IRL 1620 See Code 4285 Suc-[Glu9, Ala11,15]-Endothelin-1 (8-21) on page 62– 84 –

Joining Peptide
4288-v

Joining Peptide (Rat)
Ala-Glu-Glu-Glu-Thr-Ala-Gly-Gly-Asp-GlyArg-Pro-Glu-Pro-Ser-Pro-Arg-Glu-NH2-20

(M.W. 1882.9)

Price:Yen
Vial

0.5 mg20,000

C75H119N25O32

Pivotal Neuropeptide in Cardiovascular Regulation
1) T. Hamakubo, M. Yoshida, K. Nakajima, T.X. Watanabe, R. Mosqueda-Garcia, and T. Inagami, Am. J. Physiol.,
265, R1184 (1993). (Original)
2) M. Yoshida, T. Hamakubo, and T. Inagami, Am. J. Physiol., 266, R802 (1994). (Pharmacol.)Kallidin See Code 4008 Lysyl-Bradykinin on page 28

Kaliotoxin
4259-s-20

Kaliotoxin (1-37)*(Scorpion, Androctonus mauretanicus mauretanicus)
Gly-Val-Glu-Ile-Asn-Val-Lys-Cys-Ser-GlySer-Pro-Gln-Cys-Leu-Lys-Pro-Cys-Lys-AspAla-Gly-Met-Arg-Phe-Gly-Lys-Cys-Met-AsnArg-Lys-Cys-His-Cys-Thr-Pro

Vial

0.1 mg22,000(Reported disulfide bonds between Cys8-Cys28, Cys14-Cys33, and Cys18-Cys35)(M.W. 4021.8)

C165H271N53O48S8High Conductance Ca2+-Activated K+ Channel Blocker
1) M. Crest, G. Jacquet, M. Gola, H. Zerrouk, A. Benslimane, H. Rochat, P. Mansuelle, and M.-F. Martin-Eauclaire,
J. Biol. Chem., 267, 1640 (1992). (Original)
2) R. Romi, M. Crest, M. Gola, F. Sampieri, G. Jacquet, H. Zerrouk, P. Mansuelle, O. Sorokine, A.V. Dorsselaer,
H. Rochat, M.-F. Martin-Eauclaire, and J.V. Rietschoten, J. Biol. Chem., 268, 26302 (1993).
(Chem. Synthesis & Pharmacol.)3) F.R. Romi, S. Szendeffy, M.F. Martin-Eauclaire, H. Rochat, J.V. Rietschoten, M. Pons, and E. Giralt, Biochemistry,
33, 14256 (1994). (Unique Structure)4) A.L. Harvey, H. Vatanpour, E.G. Rowan, S. Pinkasfeld, C. Vita, A. Menez, and M.-F. Martin-Eauclaire, Toxicon,
33, 425 (1995). (Pharmacol.)*The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 85 –and Proteins

CompoundBiologically Active Peptides

CodeKisspeptins / Metastins
List of Kisspeptin / Metastin and Related Peptide

New
New
New
New

Code

CompoundQuantity

Price: Yen

Page4446-sKisspeptin-54 (Human) / Metastin (Human, 1-54)

0.1 mg vial

22,000874447-sKisspeptin-52 (Rat) / Metastin (Rat, 1-52)

0.1 mg vial

28,000874389-v

Kisspeptin-10 (Human) / Metastin (Human, 45-54)

0.5 mg vial

7,200

below

4453-v

Kisspeptin-10 (Rat) / Metastin (Rat, 43-52)

0.5 mg vial

7,200

88

4460-v

Peptide 234 (antagonist)

0.5 mg vial

7,200

122

Code

Compound4389-v

Kisspeptin-10 (Human) / Metastin (Human, 45-54)
Vial
Kp-10 (Human) / KiSS-1 Gene Product (Human, 112-121 Amide)
Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Phe-NH2-20

(M.W. 1302.4)

Price:Yen

C63H83N17O14

0.5 mg7,200[374675-21-5]

Ligand for OT7T175 / GPR54
1) T. Ohtaki, Y. Shintani, S. Honda, H. Matsumoto, A. Hori, K. Kanehashi, Y. Terao, S. Kumano, Y. Takatsu, Y. Masuda,
Y. Ishibashi, T. Watanabe, M. Asada, T. Yamada, M. Suenaga, C. Kitada, S. Usuki, T. Kurokawa, H. Onda,
O. Nishimura, and M. Fujino, Nature, 411, 613 (2001). (Original; Metastin)
2) A.I. Muir, L. Chamberlain, N.A. Elshourbagy, D. Michalovich, D.J. Moore, A. Calamari, P.G. Szekeres, H.M. Sarau,
J.K. Chambers, P. Murdock, K. Steplewski, U. Shabon, J.E. Miller, S.E. Middleton, J.G. Darker, C.G.C. Larminie,
S. Wilson, D.J. Bergsma, P. Emson, R. Faull, K.L. Philpott, and D.C. Harrison, J. Biol. Chem., 276, 28969 (2001).
(Original; Peptide Kiss–1)
3) M. Kotani, M. Detheux, A. Vandenbogaerde, D. Communi, J.-M. Vanderwinden, E. Le Poul, S. Brezillon,
R. Tyldesley, N. Suarez-Huerta, F. Vandeput, C. Blanpain, S. N. Schiffmann, G. Vassart, and M. Parmentier,J. Biol. Chem., 276, 34631 (2001). (Original; Kisspeptin)
4) A. Hori, S. Honda, M. Asada, T. Ohtaki, K. Oda, T. Watanabe, Y. Shintani, T. Yamada, M. Suenaga, C. Kitada,
H. Onda, T. Kurokawa, O. Nishimura, and M. Fujino, Biochem. Biophys. Res. Commun., 286, 958 (2001).
(Pharmacol.)5) M. Kinoshita, H. Tsukamura, S. Adachi, H. Matsui, Y. Uenoyama, K. Iwata, S. Yamada, K. Inoue, T. Ohtaki,
H. Matsumoto, and K.-I. Maeda, Endocrinology, 146, 4431 (2005). (Pharmacol.)6) S. Ramaswamy, S.B. Seminara, C.R. Pohl, M.J. DiPietro, W.F. Crowley, Jr. and T.M. Plant, Endocrinology, 148, 3364
(2007). (Pharmacol.)7) S.B. Seminara and U.B. Kaiser, Endocrinology, 146, 1686 (2005). (Minireview)8) K.I. Maeda, S. Adachi, K. Inoue, S. Ohkura, and H. Tsukamura, Rev. Endocrinol. Metab. Disord., 8, 21 (2007).
(Review)• This compound is distributed through Peptide Institute, Inc. under the license of Takeda Pharmaceutical Company
Limited.

– 86 –

Kisspeptins / Metastins (continued)
4446-sKisspeptin-54 (Human) / Metastin (Human, 1-54)
Vial
Kp-54 (Human) / KiSS-1 Gene Product (Human, 68-121 Amide)
Gly-Thr-Ser-Leu-Ser-Pro-Pro-Pro-Glu-SerSer-Gly-Ser-Arg-Gln-Gln-Pro-Gly-Leu-SerAla-Pro-His-Ser-Arg-Gln-Ile-Pro-Ala-ProGln-Gly-Ala-Val-Leu-Val-Gln-Arg-Glu-LysAsp-Leu-Pro-Asn-Tyr-Asn-Trp-Asn-Ser-PheGly-Leu-Arg-Phe-NH2

New

-20

(M.W. 5857.4)

Price:Yen
0.1 mg22,0000.1 mg28,000C258H401N79O78

Stimulator of Hypothalamic-Pituitary Gonadal Axis
4447-sNew-20

Kisspeptin-52 (Rat) / Metastin (Rat, 1-52)
Kp-52 (Rat) / KiSS-1 Gene Product (Rat, 68-119 Amide)
Thr-Ser-Pro-Cys-Pro-Pro-Val-Glu-Asn-ProThr-Gly-His-Gln-Arg-Pro-Pro-Cys-Ala-ThrArg-Ser-Arg-Leu-Ile-Pro-Ala-Pro-Arg-GlySer-Val-Leu-Val-Gln-Arg-Glu-Lys-Asp-MetSer-Ala-Tyr-Asn-Trp-Asn-Ser-Phe-Gly-LeuArg-Tyr-NH2

Vial(Disulfide bond between Cys4-Cys18)(M.W. 5836.6)

C254H398N80O73S3

Stimulator of Hypothalamic-Pituitary Gonadal Axis
Kisspeptin-54 (Human) / Metastin (Human, 1-54) and Kisspeptin-52 (Rat) / Metastin (Rat, 1-52) are thepeptides encoded by the Kiss-1 gene1,2,3,4). These peptides are ligands for GPR54 (also known as hOT7T175
and AXOR12), the nomenclature of which was recommended recently to be KISS1R (for human receptors) andKiss1r (for non-human receptors)4). Since their discovery, several research reports suggest that kisspeptin /metastin functions in a regulatory capacity in reproductive systems through action on the hypothalamicpituitary-gonadal axis5,6).
It has been also clarified that the carboxyl-terminal 10-residue peptides of human and rat kisspeptin /metastin are the active center of the corresponding mature intact peptide; therefore, they are now recognized asa useful reagent in the study of reproductive systems (Code 4389 and 4453 for human and rat peptide,
respectively). However, there are some reports presenting differences in efficacy and characteristics of theactivity between the 10-residue peptide and the mature intact 54- and 52-amino acid residue peptides7,8,9,10).
We have now successfully synthesized Kisspeptin-54 (Human) / Metastin (Human, 1-54) and Kisspeptin-52(Rat) / Metastin (Rat, 1-52) and started to distribute them as our new catalog items. These peptides may
contribute to the progress in the study of reproductive systems. We hope that precise research will be possibleusing the longer mature peptides together with the shorter 10-residue peptides of both human and rat origins.
1) T. Ohtaki, Y. Shintani, S. Honda, H. Matsumoto, A. Hori, K. Kanehashi, Y. Terao, S. Kumano, Y. Takatsu, Y. Masuda,
Y. Ishibashi, T. Watanabe, M. Asada, T. Yamada, M. Suenaga, C. Kitada, S. Usuki, T. Kurokawa,
H. Onda, O. Nishimura, and M. Fujino, Nature, 411, 613 (2001). (Original; Human Metastin)
2) A.I. Muir, L. Chamberlain, N.A. Elshourbagy, D. Michalovich, D.J. Moore, A. Calamari, P.G. Szekeres, H.M. Sarau,
J.K. Chambers, P. Murdock, K. Steplewski, U. Shabon, J.E. Miller, S.E. Middleton, J.G. Darker, C.G.C. Larminie,
S. Wilson, D.J. Bergsma, P. Emson, R. Faull, K.L. Philpott, and D.C. Harrison, J. Biol. Chem., 276, 28969 (2001).
(Original; Human Kisspeptin)
3) Y. Terao, S. Kumano, Y. Takatsu, M. Hattori, A. Nishimura, T. Ohtaki, and Y. Shintani, Biochim. Biophys. Acta, 1678,
102 (2004). (Original; Rat Metastin)4) M.L. Gottsch, D.K. Clifton, and R.A. Steiner, Peptides, 30, 4 (2009). (Review; Recommendation in Nomenclature)5) C.N. Jayasena and W.S. Dhillo, Curr. Opin. Investig. Drugs, 10, 311 (2009). (Review)6) W.H. Colledge, Trends Endocrinol. Metab., 20, 115 (2009). (Review)7) E.L. Thompson, K.G. Murphy, M. Patterson, G.A. Bewick, G.W.H. Stamp, A.E. Curtis, J.H. Cooke, P.H. Jethwa,
J.F. Todd, M.A. Ghatei, and S.R. Bloom, Am. J. Physiol. Endocrinol. Metab., 291, 1074 (2006). (Pharmacol.)8) S. Tovar, M.J. Vázquez, V.M. Navarro, R. Fernández-Fernández, J.M. Castellano, E. Vigo, J. Roa, F.F. Casamueva,
E. Aguilar, L. Pinilla, C. Dieguez, and M. Tena-Sempere, Endocrinology, 147, 2696 (2006). (Pharmacol.)9) W.S. Dhillo, O.B. Chaudhri, E.L. Tnompson, K.G. Murphy, M. Patterson, R. Ramachandran, G.K. Nijher, V. Amber, A.
Kokkinos, M. Donaldson, M.A. Ghatei, and S.R. Bloom, J. Clin. Endocrinol. Metab., 92, 3958 (2007). (Phalmacol.)10) V. Pheng, Y. Uenoyama, T. Homma, Y. Inamoto, K. Takase, K. Yoshizawa-Kumagaye, S. Isaka, T.X. Watanabe,
S. Ohkura, J. Tomikawa, K.-i. Maeda, and H. Tsukamura, J. Reprod. Dev., 55, 378 (2009). (Pharmacol.)– 87 –and Proteins

CompoundBiologically Active Peptides

CodeKisspeptins / Metastins
Code

Compound4453-v

Kisspeptin-10 (Rat) / Metastin (Rat, 43-52)
Kp-10 (Rat) / KiSS-1 Gene Product (Rat, 110-119 Amide)
Tyr-Asn-Trp-Asn-Ser-Phe-Gly-Leu-Arg-Tyr-NH2

New

-20

(M.W. 1318.4)

Price:Yen
Vial

0.5 mg7,200

C63H83N17O15

Ligand for OT7T175 / GPR54
Metastasis suppressor gene KiSS-1 encodes a peptide with multiple biological functions such as inhibition ofcancer metastasis, vasoconstriction, reproduction, and so on. In human and rat, the encoded mature peptide iscomposed of 54 and 52 amino acid residues, respectively, which is named metastin or kisspeptin1,2,3).
Kisspeptin-10 (Human) / Metastin (Human, 45-54) is an active segment of the human peptide from the
C-terminal portion and is already available from our catalog (Code 4389-v).
Very recently, in collaboration with Dr. Tsukamura and her colleagues in Nagoya University, we havesuccessfully clarified that the corresponding rat 10-residue peptide, Kisspeptin-10 (Rat) / Metastin (Rat, 43-52),
exerts the luteinizing hormone (LH) releasing activity in male rats4). Actually, intracerebroventricular or
intravenously administration at a dose of 1 nmol/kg or 10 nmol/kg stimulates LH release and significantly
increases plasma LH level in male rats.
Now the precise experiment using Kisspeptin-10 (Rat) / Metastin (Rat, 43-52) is possible in rat studies.
1) T. Ohtaki, Y. Shintani, S. Honda, H. Matsumoto, A. Hori, K. Kanehashi, Y. Terao, S. Kumano, Y. Takatsu, Y. Masuda,
Y. Ishibashi, T. Watanabe, M. Asada, T. Yamada, M. Suenaga, C. Kitada, S. Usuki, T. Kurokawa, H. Onda,
O. Nishimura, and M. Fujino, Nature, 411, 613 (2001). (Metastin)2) M. Kotani, M. Detheux, A. Vandenbogaerde, D. Communi, J.-M. Vanderwinden, E. Le Poul, S. Brezillon,
R. Tyldesley, N. Suarez-Huerta, F. Vandeput, C. Blanpain, S.N. Schiffmann, G. Vassart, and M. Parmentier,J. Biol. Chem., 276, 34631 (2001). (Kisspeptin)
3) Y. Terao, S. Kumano, Y. Takatsu, M. Hattori, A. Nishimura, T. Ohtaki, and Y. Shintani, Biochim. Biophys. Acta, 1678,
102 (2004). (Original; Rat Metastin)4) V. Pheng, Y. Uenoyama, T. Homma, Y. Inamoto, K. Takase, K. Yoshizawa-Kumagaye, S. Isaka, T.X. Watanabe,
S. Ohkura, J. Tomikawa, K.-i. Maeda, and H. Tsukamura, J. Reprod. Dev., 55, 378 (2009). (Pharmacol.)5) M.L. Gottsch, D.K. Clifton, and R.A. Steiner, Peptides, 30, 4 (2009). (Review; Recommendation in Nomenclature)

Kurtoxin
4375-s-20

Kurtoxin(Scorpion, Parabuthus transvaalicus)
Lys-Ile-Asp-Gly-Tyr-Pro-Val-Asp-Tyr-TrpAsn-Cys-Lys-Arg-Ile-Cys-Trp-Tyr-Asn-AsnLys-Tyr-Cys-Asn-Asp-Leu-Cys-Lys-Gly-LeuLys-Ala-Asp-Ser-Gly-Tyr-Cys-Trp-Gly-TrpThr-Leu-Ser-Cys-Tyr-Cys-Gln-Gly-Leu-ProAsp-Asn-Ala-Arg-Ile-Lys-Arg-Ser-Gly-ArgCys-Arg-Ala

0.1 mg30,000(Disulfide bonds between Cys12-Cys61, Cys16-Cys37, Cys23-Cys44, and Cys27-Cys46)(M.W. 7386.4) C324H478N94O90S8
Purity Information: Qp See page IV (XVI)

T-type Ca2+ Channel Blocker
1) R.S-I. Chuang, H. Jaffe, L. Cribbs, E. Perez-Reyes, and K.J. Swartz, Nat. Neurosci., 1, 668 (1998). (Original)
2) S.S. Sidach and I.M. Mintz, J. Neurosci., 22, 2023 (2002).
(Pharmacol; Specificity for Ca2+ Channel Blocking Activity)
3) T. Olamendi-Portugal, B.I. Garc́a, I. López-González, J. Van Der Walt, K. Dyason, C. Ulens, J. Tytgat, R. Felix,
A. Darszon, and L.D. Possani, Biochem. Biophys. Res. Commun., 299, 562 (2002). (Pharmacol.)4) I. López-González, T. Olamendi-Portugal, J.L. De La Vega-Beltrán, J. Van der Walt, K. Dyason, L.D. Possani, R. Felix,and A. Darszon, Biochem. Biophys. Res. Commun., 300, 408 (2003). (Pharmacol.)5) H. Nis hio, Y. Nishiuchi, M. Is himaru, and T. Kimura, Lett. Pept. Sci., 10, 589 (2003). (Chem. Synthesis & S-S Bond)– 88 –

Laminin
4194-v

Laminin Pentapeptide YIGSR-NH2
Tyr-Ile-Gly-Ser-Arg-NH2-20

(M.W. 593.68)

4194
-20

Price:Yen

C26H43N9O7

Vial

0.5 mg

3,000

Bulk

25 mg
100 mg23,00065,000[110590-65-3]

Laminin Pentapeptide YIGSR-NH2
Tyr-Ile-Gly-Ser-Arg-NH2 • 2AcOH • 2H2O
(M.W. 593.68 • 120.10 • 36.03)

C26H43N9O7 • 2CH3COOH • 2H2O
1) Y. Iwamoto, F.A. Robey, J. Graf, M. Sasaki, H.K. Kleinman, Y. Yamada, and G.R. Martin, Science, 238, 1132 (1987).
(Original)

LEAP-1 See Code 4392 Hepcidin / LEAP-1 (Human) on page 79
LEAP-2 See Code 4405 Liver-Expressed Antimicrobial Peptide 2 (Human) on page 90
Leiurotoxin I See Code 4260 Scyllatoxin on page 139

Leu-Pro-Leu-Arg-Phe-NH2
4144

Leu-Pro-Leu-Arg-Phe-NH2 • 2AcOH • 2H2O*-20

(M.W. 643.82 • 120.10 • 36.03)

Bulk

C32H53N9O5 • 2CH3COOH • 2H2O

25 mg
100 mg25,00069,000Chicken Brain Peptide
1) G.J. Dockray, J.R. Reeve, Jr., J. Shively, R.J. Gayton, and C.S. Barnard, Nature, 305, 328 (1983). (Original)

β-Lipotropin (61-76) See Code 4055 α-Endorphin on page 58
β-Lipotropin (61-77) See Code 4089 γ-Endorphin on page 58
β-Lipotropin (Human, 61-91) See Code 4060 β-Endorphin (Human) on page 58

Liver-Cell Growth Factor
4022
-20

Bulk

Liver-Cell Growth Factor
Gly-His-Lys • AcOH • H2O(M.W. 340.38 • 60.05 • 18.02)

C14H24N6O4 • CH3COOH • H2O

25 mg
100 mg

7,500
15,400[72957-37-0]

1) L. Pickart, L. Thayer, and M.M. Thaler, Biochem. Biophys. Res. Commun., 54, 562 (1973). (Original)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 89 –and Proteins

CompoundBiologically Active Peptides

CodeLiver-Expressed Antimicrobial Peptide (LEAP)
CodeCompound4405-s

LEAP-2 (Human)
Liver-Expressed Antimicrobial Peptide 2 (Human)
Prepro-LEAP-2 (Human, 38-77)
Met-Thr-Pro-Phe-Trp-Arg-Gly-Val-Ser-LeuArg-Pro-Ile-Gly-Ala-Ser-Cys-Arg-Asp-AspSer-Glu-Cys-Ile-Thr-Arg-Leu-Cys-Arg-LysArg-Arg-Cys-Ser-Leu-Ser-Val-Ala-Gln-Glu-20

Price:Yen
Vial

0.1 mg22,000(Disulfide bonds between Cys17-Cys28 and Cys23-Cys33)(M.W. 4581.3)

C191H316N64O57S5

Antimicrobial Peptide
One method aimed at finding peptides and proteins is "the systematic analysis of polypeptides in humanblood ultrafiltrate", which has proven to be successful. Liver-expressed antimicrobial peptide 1 (LEAP-1)/
hepcidin is an example of such, which elicits antimicrobial activity as well as some functions in ironhomeostasis. Following LEAP-1, a cationic peptide termed LEAP-2 was discovered using the same method, the"peptide trapping" approach1).
The isolated peptides have variable chain lengths with the deletion of the longest peptide, composed of
40 amino acid residues, at both the amino- and carboxyl-termini. Its disulfide arrangement was determined to
be Cys1-Cys3 and Cys2-Cys4 (Cys numbering from the amino-terminus) by analyzing the molecular weight andsequence of the tryptic fragments. The cDNA cloning of LEAP-2 reveals the precursor of LEAP-2 to be a 77residue peptide, in which the longest form corresponds to the residues between the positions of 38 and 77 in the
precursor [prepro-LEAP-2(38-77)]. The primary structures of LEAP-2 of rhesus monkey, cow, pig, mouse, andguinea pig were also determined, and found to be highly conserved among these species. LEAP-2 mRNA is
predominantly expressed in the liver and small intestine.
LEAP-2 [ prepro-LEAP-2 (38-77) ] exerts antimicrobial activities against Gram-positive bacteria,
Gram-negative bacteria, and yeast (IC 50 value was around 5 µ M against Saccharomyces cerevisiae).
Interestingly, the amino-terminally truncated form, prepro-LEAP-2 (44-77), has not affected the viability of thegerms tested. The 40-residue peptide, LEAP-2, was reported to be circulating in human blood. LEAP-2 should
prove to be valuable in studying its role in self-defence in humans, as well as its role as anantimicrobial peptide in the family of the well-established α-/β-defensins.
1) A. Krause, R. Sillard, B. Kleemeier, E. Klu
ver, E. Maronde, J.R. Conejo-Garc́a, W.G. Forssmann, P. Schulz-Knappe,
M.C. Nehls, F. Wattler, S. Wattler, and K. Adermann, Protein Sci., 12, 143 (2003). (Original & S-S Bond)
2) A. Hocquellet, B. Odaert, C. Cabanne, A. Noubhani, W. Dieryck, G. Joucla, C. Le Senechal, M. Milenkov,
S. Chaignepain, J.M. Schmitter, S. Claverol, X. Santarelli, E.J. Dufourc, M. Bonneu, B. Garbay, and P. Costaglioli,
Peptides, 31, 58 (2010). (Review)

Luteinizing Hormone Releasing Hormone (LH-RH)
4013-v-20

Vial

0.5 mg2,700

LH-RH (Human)
Bulk
Luteinizing Hormone Releasing Hormone (Human)
GnRH (Gonadotropin-Releasing Hormone) (Human)(Porcine, Rat)
Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2 • 2AcOH • 4H2O

25 mg
100 mg36,00095,000

LH-RH (Human)
Luteinizing Hormone Releasing Hormone (Human)
GnRH (Gonadotropin-Releasing Hormone) (Human)(Porcine, Rat)
Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2(M.W. 1182.3)

4013
-20

C55H75N17O13(M.W. 1182.3 • 120.10 • 72.06)[33515-09-2]

C55H75N17O13 • 2CH3COOH • 4H2O

[71447-49-9]

1) H. Matsuo, Y. Baba, R.M.G. Nair, A. Arimura, and A.V. Schally, Biochem. Biophys. Res. Commun., 43, 1334 (1971).
(Original)

Lys-Lys-Lys-Leu-Arg-Arg-Gln-Glu-Ala-Phe-Asp-Ala-Tyr See Code 4374 on page 196
Lysenin See Code 4802 on page 152– 90 –

LL-374445-s

LL-37 (Human)
Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-LysGlu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-IleVal-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-AsnLeu-Val-Pro-Arg-Thr-Glu-Ser-20

(M.W. 4493.3)

Price:Yen
Vial

0.1 mg12,000C205H340N60O53

Cathelicidin Antimicrobial Peptide
Antimicrobial peptides (often abbreviated as AMPs) play essential roles in self-defense systems. Defensins
are potential protecting factors against microbial infection and members of AMPs in human: we have been
manufacturing α-defensin-1 (Code 4271), -2 (Code 4428), -3 (Code 4416), -4 (Code 4431), -5 (Code 4415), and-6 (Code 4458), as well as β-defensin-1 (Code 4337), -2 (Code 4338), -3 (Code 4382), and -4 (Code 4406) as ourcatalog items. Another member of AMP in human is LL-37, the so-called cathelicidin AMP1,2). Cathelicidins are
one family of multifunctional AMPs, characterized by conserved pro-peptide sequences that have been
identified in several mammalian species. On the contrary to disulfide cross-linked defensins, LL-37 is a linear,amphipathic peptide with α-helical structure.
LL-37 is reported to exert not only antimicrobial activity but also immunomodulatory activity2,3). Recent
papers describe the involvement of LL-37 in toll-like receptor (TLR) activation: i) vitamin D receptor-mediatedinduction of LL-37 through TLR2/1L activation was observed in human monocyte4) and ii) LL-37 interacts to
self-DNA in psoriasis, after which the complex formed triggers TLR9, resulting in the induction of interferon-α
production5). In the latter special case, LL-37 might be the pathogenic factor of psoriasis, one of the
autoimmune diseases, although LL-37, together with β-defensin-2, is reported to be highly expressed inpsoriasis to protect the infection with Staphylococcus aureus6).
Thus, LL-37 should be valuable in the research of human defense systems, especially to clarify themechanism of innate immunity and LL-37's role in autoimmunity and cancer7).
1) G.H. Gudmundsson, B. Agerberth, J. Odeberg, T. Bergman, B. Olsson, and R. Salcedo, Eur. J. Biochem., 238, 325(1996). (Original)
2) R. Bals and J.M. Wilson, Cell. Mol. Life Sci., 60, 711 (2003). (Review)3) M. Zanetti, J. Leukoc. Biol., 75, 39 (2004). (Review)4) P.T. Liu, S. Stenger, H. Li, L.Wenzel, B.H. Tan, S.R. Krutzik, M.T. Ochoa, J. Schauber, K. Wu, C. Meinken,
D.L. Kamen, M. Wagner, R. Bals, A. Steinmeyer, U. Zu
gel, R.L. Gallo, D. Eisenberg, M. Hewison, B.W. Hollis,
J.S. Adams, B.R. Bloom, and R.L. Modlin, Science, 311, 770 (2006). (Pharmacol.)5) R. Lande, J. Gregorio, V. Facchinetti, B. Chatterjee, Y.-H. Wang, B. Homey, W. Cao, Y.-H. Wang, B. Su, F.O. Nestle,
T. Zal, I. Mellman, J.-M. Schroder, Y.-J. Liu, and M. Gilliet, Nature, 449, 564 (2007). (Pharmacol.)6) P.Y. Ong, T. Ohtake, C. Brandt, I. Strickland, M. Boguniewicz, T. Ganz, R.L. Gallo, and, D.Y.M. Leung,
New Engl. J. Med., 347, 1151 (2002). (Pharmacol.)7) D.W. Hoskin and A. Ramamoorthy, Biochim. Biophys. Acta, 1778, 357 (2008). (Review)8) Y.P. Lai and R.L. Gallo, Trends Immunol., 30, 131 (2009). (Review)9) M.F. Burton and P.G. Steel, Nat. Prod. Rep., 26, 1572 (2009). (Review)– 91 –and Proteins

CompoundBiologically Active Peptides

CodeMagainin
Code

Compound4196-v

Magainin 1(Frog, Xenopus laevis)
Gly-Ile-Gly-Lys-Phe-Leu-His-Ser-Ala-GlyLys-Phe-Gly-Lys-Ala-Phe-Val-Gly-Glu-IleMet-Lys-Ser-20

(M.W. 2409.8)

Price:Yen

C112H177N29O28S

Vial

0.5 mg25,500Vial

0.1 mg22,000[108433-99-4]

Antimicrobial Peptide
1) M. Zasloff, Proc. Natl. Acad. Sci. U.S.A., 84, 5449 (1987). (Original)

Margatoxin
4290-s-20

Margatoxin
MgTX(Scorpion, Centruroides margaritatus)
Thr-Ile-Ile-Asn-Val-Lys-Cys-Thr-Ser-ProLys-Gln-Cys-Leu-Pro-Pro-Cys-Lys-Ala-GlnPhe-Gly-Gln-Ser-Ala-Gly-Ala-Lys-Cys-MetAsn-Gly-Lys-Cys-Lys-Cys-Tyr-Pro-His(Reported disulfide bonds between Cys7-Cys29, Cys13-Cys34, and Cys17-Cys36)(M.W. 4178.9)

C178H286N52O50S7[145808-47-5]+

Voltage-Dependent K Channel Blocker (Specific for Kv1.3 Channel )1) R.J. Leonard, M.L. Garcia, R.S. Slaughter, and J.P. Reuben, Proc. Natl. Acad. Sci. U.S.A., 89, 10094 (1992).
(Pharmacol.)2) M. Garcia-Calvo, R.J. Leonard, J. Novick, S.P. Stevens, W. Schmalhofer, G.J. Kaczorowski, and M.L. Garcia,
J. Biol. Chem., 268, 18866 (1993). (Original)
3) M.A. Bednarek, R.M. Bugianesti, R.J. Leonard, and J.P. Felix, Biochem. Biophys. Res. Commun., 198, 619 (1994).
(Chem. Synthesis & S-S Bond)
4) H.G. Knaus, R.O.A. Koch, A. Eberhart, G.J. Kaczorowski, M.L. Garcia, and R.S. Slaughter, Biochemistry,
34,13627 (1995). (Pharmacol.)Mastoparan
4107-v-20

Mastoparan(Wasp, Vespula lewisii)
Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-AlaLys-Lys-Ile-Leu-NH2(M.W. 1478.9)

4107
-20

C70H131N19O15

0.5 mg

6,200

Bulk

25 mg

110,000[72093-21-1]

Mastoparan(Wasp, Vespula lewisii)
Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-AlaLys-Lys-Ile-Leu-NH2 • 4AcOH • 6H2O
(M.W. 1478.9 • 240.21 • 108.09)

Vial

C70H131N19O15 • 4CH3COOH • 6H2O

1) Y. Hirai, T. Yasuhara, H. Yoshida, T. Nakajima, M. Fujino, and C. Kitada, Chem. Pharm. Bull., 27, 1942 (1979).
(Original; Chem. Synthesis)– 92 –

α-Mating Factor
4076-vα-Mating Factor(Yeast, Saccharomyces cerevisiae)
Trp-His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-GlnPro-Met-Tyr-20

(M.W. 1684.0)

Price:Yen

C82H114N20O17S

Vial

0.5 mg7,200[59401-28-4]

1) D. Stotzler, H.-H. Kilts, and W. Duntze, Eur. J. Biochem., 69, 397 (1976). (Original)
2) T. Tanaka, H. Kita, T. Murakami, and K. Narita, J. Biochem., 82, 1681 (1977). (Original)
3) Y. Masui, N. Chino, S. Sakakibara, T. Tanaka, T. Murakami, and H. Kita, Biochem. Biophys. Res. Commun.,78, 534 (1977). (Chem. Synthesis)

MCD-Peptide
4258-v-20

MCD-Peptide*
Mast Cell Degranulating Peptide(Honeybee, Apis mellifera)
Ile-Lys-Cys-Asn-Cys-Lys-Arg-His-Val-IleLys-Pro-His-Ile-Cys-Arg-Lys-Ile-Cys-GlyLys-Asn-NH2

Vial

0.5 mg25,000(Disulfide bonds between Cys3-Cys15 and Cys5-Cys19)(M.W. 2587.2)

C110H192N40O24S4[32908-73-9]+

Voltage-Dependent K Channel Blocker
1) E. Haberman, Science, 177, 314 (1972). (Review)2) M.R. Ziai, S. Russek, H.-C. Wang, B. Beer, and A.J. Blume, J. Pharm. Pharmacol., 42, 457 (1990). (Review)• This compound is distributed through Peptide Institute, Inc. under the license of The Salk Institute.

Melanin-Concentrating Hormone
4369-v-20

Melanin-Concentrating Hormone (Human)
MCH (Human)(Rat, Mouse)
Asp-Phe-Asp-Met-Leu-Arg-Cys-Met-Leu-GlyArg-Val-Tyr-Arg-Pro-Cys-Trp-Gln-Val

Vial

0.5 mg15,000(Disulfide bond between Cys7-Cys16)(M.W. 2386.8)

C105H160N30O26S4[128315-56-0]

Appetite Boosting Peptide
Melanin-Concentrating Hormone (MCH) was isolated from salmon pituitary and was found to induce
aggregation of melanin granules in melanophores. Later, a mammalian homolog was identified in rat
hypothalamus as a 19 amino acid peptide with a single disulfide bond [Endocrinology, 125, 1660 (1989)].
Subsequently, the human MCH sequence was found to be the same as that of the rat peptide1). Interestingly,
the MCH of hypothalamus was reported in 1996 to be involved in the regulation of body weight2). Actually,
the injection of MCH into the lateral ventricles increased food consumption in rats. Further evidence in theliterature indicates that MCH-deficient mice are lean due to hypophagia3).
1) K.M. Knigge, D. Baxter-Grillo, J. Speciale, and J. Wagner, Peptides, 17, 1063 (1996). (Review)2) D. Qu, D.S. Ludwig, S. Gammeltoft, M. Piper, M.A. Pelleymounter, M.J. Cullen, W.F. Mathes, J. Przypek, R. Kanarek,
and E. Maratos-Flier, Nature, 380, 243 (1996). (Pharmacol.)3) M. Shimada, N.A. Tritos, B.B. Lowell, J.S. Flier, and E. Maratos-Flier, Nature, 396, 670 (1998). (Pharmacol.)4) J. Chambers, R.S. Ames, D. Bergsma, A. Muir, L.R. Fitzgerald, G. Hervieu, G.M. Dytko, J.J. Foley, J. Martin, W.-S. Liu,
J. Park, C. Ellis, S. Ganguly, S. Konchar, J. Cluderay, R. Leslie, S. Wilson, and H.M. Sarau, Nature, 400, 261 (1999).
(Pharmacol.; Ligand for Orphan SLC-1 Receptor)5) Y, Saito, H.-P. Nothacker, Z. Wang, S.H.S. Lin, F. Leslie, and O. Civelli, Nature, 400, 265 (1999).
(Pharmacol.; Ligand for Orphan SLC-1 Receptor)• This compound is distributed through Peptide Institute, Inc. under the license of The Salk Institute.

*The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 93 –and Proteins

CompoundBiologically Active Peptides

CodeMelanocyte Stimulating Hormone (MSH) and Related Peptide
Code

Compound4057-v

α-MSH
α-Melanocyte Stimulating Hormone(Human, Porcine, Bovine, Rat, Mouse)
Ac-Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-GlyLys-Pro-Val-NH2-20

(M.W. 1664.9)

Price:Yen

C77H109N21O19S

Vial

0.5 mg5,700[581-05-5]

1) T.H. Lee and A.B. Lerner, J. Biol. Chem., 221, 943 (1956). (Original; Porcine)2) R.A. Boissonnas, St. Guttmann, R.L. Huguenin, P.-A. Jaquenoud, and E. Sandrin, Helv. Chim. Acta, 41, 1867 (1958).
(Chem. Synthesis)
3) R. Schwyzer, A. Costpanagiotis, and P. Sieber, Helv. Chim. Acta, 46, 870 (1963). (Chem. Synthesis)4) A.C.Y. Chang, M. Cochet, S.N. Cohen, Proc. Natl. Acad. Sci. U.S.A., 77, 4890 (1980). (Nucleotide Seq.; Human)

4024
-20

MSH-Release Inhibiting Factor
MIF
Pro-Leu-Gly-NH2 • 1/ 2 H2O

Bulk

25 mg
100 mg

2,200
5,000

Vial

50 µg

30,000(M.W. 284.35 • 9.01)

C13H24N4O3 • 1/2H2O [2002-44-0]
1) A. Vivas and M.E. Celis, J. Endocrinol., 78, 1 (1978). (Pharmacol.)Midkines4298-v-20

Midkine (Human)
Lys-Lys-Lys-Asp-Lys-Val-Lys-Lys-Gly-GlyPro-Gly-Ser-Glu-Cys-Ala-Glu-Trp-Ala-TrpGly-Pro-Cys-Thr-Pro-Ser-Ser-Lys-Asp-CysGly-Val-Gly-Phe-Arg-Glu-Gly-Thr-Cys-GlyAla-Gln-Thr-Gln-Arg-Ile-Arg-Cys-Arg-ValPro-Cys-Asn-Trp-Lys-Lys-Glu-Phe-Gly-AlaAsp-Cys-Lys-Tyr-Lys-Phe-Glu-Asn-Trp-GlyAla-Cys-Asp-Gly-Gly-Thr-Gly-Thr-Lys-ValArg-Gln-Gly-Thr-Leu-Lys-Lys-Ala-Arg-TyrAsn-Ala-Gln-Cys-Gln-Glu-Thr-Ile-Arg-ValThr-Lys-Pro-Cys-Thr-Pro-Lys-Thr-Lys-AlaLys-Ala-Lys-Ala-Lys-Lys-Gly-Lys-Gly-LysAsp(Disulfide bonds between Cys15-Cys39, Cys23-Cys48, Cys30-Cys52, Cys62-Cys94, and Cys72-Cys104)(M.W. 13240.1)

C570H915N177O167S10[170138-17-7]

Heparin-Binding Growth / Differentiation Factor(Neurotrophic Factor, Neurite Outgrowth-Promoting Factor)
Plasminogen Activator Activity Enhancer
1) J.-i. Tsutsui, K. Uehara, K. Kadomatsu, S. Matsubara, and T. Muramatsu, Biochem. Biophys. Res. Commun.,
176, 792 (1991). (Original)
2) H. Muramatsu, T. Inui, T. Kimura, S. Sakakibara, X.-j. Song, H. Maruta, and T. Muramatsu, Biochem. Biophys. Res.
Commun., 203, 1131 (1994). (Pharmacol.)3) T. Inui, J. Bódi, S. Kubo, H. Nishio, T. Kimura, S. Kojima, H. Maruta, T. Muramatsu, and S. Sakakibara, J. Peptide Sci.,
2, 28 (1996). (Chem. Synthesis)4) G.S.P. Yu, J. Hu, and H. Nakagawa, Neurosci. Lett., 254, 128 (1998). (Pharmacol.; Inhibition of β -amyloid
cytotoxicity)• This product is distributed under the license of Prof. Takashi Muramatsu. Its use for any purpose other than researchis strictly prohibited.

– 94 –

Midkines (continued)
4299-sMidkine (Human, 60-121)
Ala-Asp-Cys-Lys-Tyr-Lys-Phe-Glu-Asn-TrpGly-Ala-Cys-Asp-Gly-Gly-Thr-Gly-Thr-LysVal-Arg-Gln-Gly-Thr-Leu-Lys-Lys-Ala-ArgTyr-Asn-Ala-Gln-Cys-Gln-Glu-Thr-Ile-ArgVal-Thr-Lys-Pro-Cys-Thr-Pro-Lys-Thr-LysAla-Lys-Ala-Lys-Ala-Lys-Lys-Gly-Lys-GlyLys-Asp-20

Price:Yen
Vial

0.1 mg30,000(Disulfide bonds between Cys62-Cys94 and Cys72-Cys104)(M.W. 6788.8)

C292H483N91O87S4

Heparin-Binding Growth / Differentiation Factor Active-Domain(Neurite Outgrowth-Promoting Factor)
Plasminogen Activator Activity Enhancer
1) J.-i. Tsutsui, K. Uehara, K. Kadomatsu, S. Matsubara, and T. Muramatsu, Biochem. Biophys. Res. Commun.,
176, 792 (1991). (Original)
2) H. Muramatsu, T. Inui, T. Kimura, S. Sakakibara, X.-j. Song, H. Maruta, and T. Muramatsu, Biochem. Biophys. Res.
Commun., 203, 1131 (1994). (Pharmacol.)3) T. Inui, J. Bódi, S. Kubo, H. Nishio, T. Kimura, S. Kojima, H. Maruta, T. Muramatsu, and S. Sakakibara, J. Peptide Sci.,
2, 28 (1996). (Chem. Synthesis)4) G.S.P. Yu, J. Hu, and H. Nakagawa, Neurosci. Lett., 254, 128 (1998). (Pharmacol.; Inhibition of β -amyloid
cytotoxicity)• This product is distributed under the license of Prof. Takashi Muramatsu. Its use for any purpose other than researchis strictly prohibited.

Molluscan Cardioexcitatory Neuropeptide
4142-v-20

FMRF-Amide*
Molluscan Cardioexcitatory Neuropeptide
Phe-Met-Arg-Phe-NH2(M.W. 598.76)

4142
-20

C29H42N8O4S

Vial

0.5 mg

2,400

Bulk

25 mg
100 mg23,00065,000Bulk

25 mg
100 mg

4,100
11,400[64190-70-1]

FMRF-Amide*
Molluscan Cardioexcitatory Neuropeptide
Phe-Met-Arg-Phe-NH2 • 11/ 2 AcOH • 2H2O
C29H42N8O4S • 11/2 CH3COOH • 2H2O
1) D.A. Price and M.J. Greenberg, Science, 197, 670 (1977). (Original)(M.W. 598.76 • 90.08 • 36.03)

Morphine Tolerance Peptide
4070

Morphine Tolerance Peptide-20

cyclo (Leu-Gly)(M.W. 170.21)

C8H14N2O2 [5845-67-0]
1) R. Walter, R. Ritzmann, H.N. Bhargava, and L.B. Flexner, Proc. Natl. Acad. Sci. U.S.A., 76, 518 (1979). (Original)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 95 –and Proteins

CompoundBiologically Active Peptides

CodeMotilin
Code

Compound4147-v

Motilin (Human, Porcine)
Phe-Val-Pro-Ile-Phe-Thr-Tyr-Gly-Glu-LeuGln-Arg-Met-Gln-Glu-Lys-Glu-Arg-Asn-LysGly-Gln-20

(M.W. 2699.0)

Price:Yen

C120H188N34O35S

Vial

0.5 mg28,500[52906-92-0]

1) J.C. Brown, M.A. Cook, and J.R. Dryburgh, Can. J. Biochem., 51, 533 (1973). (Original; Porcine)2) H. Schubert and J.C. Brown, Can. J. Biochem., 52, 7 (1974). (Correction of Sequence; Gln14)3) Y. Seino, K. Tanaka, H. Takahashi, T. Mitani, M. Kurono, T. Kayano, G. Koh, H. Fukumoto, H. Yano, J. Fujita,
N. Inagaki, Y. Yamada, and H. Imura, FEBS Lett., 223, 74 (1987). (Original; Human-cDNA)
4) C.H.S. McIntosh and J.C. Brown, Adv. Metab. Dis., 11, 439 (1988). (Review)

MSH See Code 4057 α-MSH (α-Melanocyte Stimulating Hormone) on page 94
Muramyl Dipeptide See Code 4031 Adjuvant Peptide on page 2 and 258

Muscarinic Toxins
1) K.N. Bradley, Pharmacol. Ther., 85, 87 (2000). (Review)2) L.T. Potter, Life Sci., 68, 2541 (2001). (Review)3) D. Servent and C. Fruchart-Gaillard, J. Neurochem., 109, 1193 (2009). (Review)4) E. Karlsson, M. Jolkkonen, E. Mulugeta, P. Onali, and A. Adem, Biochimie, 82, 793 (2000). (Review)

List of Muscarinic Toxins

4341-s-20

CodeCompoundSpecificity

Quantity

Price: Yen

Page

4341-sMuscarinic Toxin 1 (MT1, MTX1)

M1/4

0.1 mg vial

30,000below

4410-sMuscarinic Toxin 3 (MT3, MTX3, m4-toxin)

M40.1 mg vial

30,00097

4340-sMuscarinic Toxin 7 (MT7, MTX7, m1-toxin1)

M1

0.1 mg vial

30,000974424-sMuscarinic Toxin α (MTα)

M3/4/50.1 mg vial

30,00098

Muscarinic Toxin 1
MT1, MTX1(Green Mamba, Dendroaspis angusticeps)
Leu-Thr-Cys-Val-Thr-Ser-Lys-Ser-Ile-PheGly-Ile-Thr-Thr-Glu-Asn-Cys-Pro-Asp-GlyGln-Asn-Leu-Cys-Phe-Lys-Lys-Trp-Tyr-TyrIle-Val-Pro-Arg-Tyr-Ser-Asp-Ile-Thr-TrpGly-Cys-Ala-Ala-Thr-Cys-Pro-Lys-Pro-ThrAsn-Val-Arg-Glu-Thr-Ile-Arg-Cys-Cys-GluThr-Asp-Lys-Cys-Asn-Glu

Vial

0.1 mg30,000(Disulfide bonds between Cys3-Cys24, Cys17-Cys42, Cys46-Cys58, and Cys59-Cys64)(M.W. 7509.5)

C326H499N87O101S8
Purity Information : QP See page IV (XVI)

Agonist for Muscarinic Acetylcholine Receptor-1/4 (M1 / M4) (Non-specific Ligand)1) M. Jolkkonen, A. Adem, U. Hellman, C. Wernstedt, and E. Karlsson,Toxicon, 33, 399 (1995). (Original-Structure)2) D. Jerusalinsky and A.L. Harvey, Trends Pharmacol. Sci., 15, 424 (1994). (Review; Toxin for Muscarinic Receptor)
3) A. Adem and E. Karlsson, Life Sci., 60, 1069 (1997). (Pharmacol.)4) H.Nishio, Y. Nishiuchi, T. Inui, K.N. Bradley, A.L. Harvey, and T. Kimura, Peptide Science 1999, 125 (2000).
(S-S Bond )– 96 –

Muscarinic Toxins (continued)
4410-sMuscarinic Toxin 3
MT3, MTX3, m4-toxin(Green Mamba, Dendroaspis angusticeps)
Leu-Thr-Cys-Val-Thr-Lys-Asn-Thr-Ile-PheGly-Ile-Thr-Thr-Glu-Asn-Cys-Pro-Ala-GlyGln-Asn-Leu-Cys-Phe-Lys-Arg-Trp-His-TyrVal-Ile-Pro-Arg-Tyr-Thr-Glu-Ile-Thr-ArgGly-Cys-Ala-Ala-Thr-Cys-Pro-Ile-Pro-GluAsn-Tyr-Asp-Ser-Ile-His-Cys-Cys-Lys-ThrAsp-Lys-Cys-Asn-Glu-20

Price:Yen
Vial

0.1 mg30,0000.1 mg30,000(Disulfide bonds between Cys3-Cys24, Cys17-Cys42, Cys46-Cys57, and Cys58-Cys63)(M.W. 7379.4)

C319H489N89O97S8

Specifc Ligand for Muscarinic Acetylcholine Receptor-4 (M4)
References: see page 98

4340-s-20

Muscarinic Toxin 7
MT7, MTX7, m1-toxin1(Green Mamba, Dendroaspis angusticeps)
Leu-Thr-Cys-Val-Lys-Ser-Asn-Ser-Ile-TrpPhe-Pro-Thr-Ser-Glu-Asp-Cys-Pro-Asp-GlyGln-Asn-Leu-Cys-Phe-Lys-Arg-Trp-Gln-TyrIle-Ser-Pro-Arg-Met-Tyr-Asp-Phe-Thr-ArgGly-Cys-Ala-Ala-Thr-Cys-Pro-Lys-Ala-GluTyr-Arg-Asp-Val-Ile-Asn-Cys-Cys-Gly-ThrAsp-Lys-Cys-Asn-Lys

Vial(Disulfide bonds between Cys3-Cys24, Cys17-Cys42, Cys46-Cys57, and Cys58-Cys63)(M.W. 7472.4)

C322H484N90O98S9Specific Ligand for Muscarinic Acetylcholine Receptor-1 (M1)
1) A. Adem and E. Karlsson, Life Sci., 60, 1069 (1997). (Original)
2) H.Nishio, Y. Nishiuchi, T. Inui, K.N. Bradley, A.L. Harvey, and T. Kimura, Peptide Science 1999, 125 (2000).
(S-S Bond)
3) J.M.Carsi and L.T. Potter, Toxicon, 38, 187 (2000). (Original; m1-toxin1)
4) Z. Gu, P. Zhong, and Z. Yan, J. Biol. Chem., 278, 17546 (2003). (Pharmacol; Inhibition of β -Amyloid signaling)– 97 –and Proteins

CompoundBiologically Active Peptides

CodeMuscarinic Toxins (continued)
Code

Compound4424-sMuscarinic Toxin αMTα(Black Mamba, Dendroaspis polylepis)
Leu-Thr-Cys-Val-Thr-Ser-Lys-Ser-Ile-PheGly-Ile-Thr-Thr-Glu-Asn-Cys-Pro-Asp-GlyGln-Asn-Leu-Cys-Phe-Lys-Lys-Trp-Tyr-TyrLeu-Asn-His-Arg-Tyr-Ser-Asp-Ile-Thr-TrpGly-Cys-Ala-Ala-Thr-Cys-Pro-Lys-Pro-ThrAsn-Val-Arg-Glu-Thr-Ile-His-Cys-Cys-GluThr-Asp-Lys-Cys-Asn-Glu-20

Price:Yen
Vial

0.1 mg30,000(Disulfide bonds between Cys3-Cys24, Cys17-Cys42, Cys46-Cys58, and Cys59-Cys64)(M.W. 7545.4)

C326H491N89O102S8

Ligand for Muscarinic Acetylcholine Receptor-3/4/5 (M3/M4/M5) (Non-specific Ligand)Muscarinic acetylcholine receptors have been classified into five subtypes (M1 to M5). These receptors are
involved in various biological functions, which can be studied using specific ligands to each receptor subtype,including the peptidic "muscarinic toxin" (abbreviated as MT in this short description). Muscarinic toxins are
isolated from the venom of the mamba species and are composed of 65 to 66 amino acid residues with four
intramolecular disulfide linkages1). It is indicated that the activation of muscarinic acetylcholine receptors canregulate the metabolism of amyloid precursor protein, and that muscarinic agonists led to a reduction ofamyloid β-protein production2, 3). For example, synthetic MT7 (Code 4340-s) has been used to study M1receptor's role in amyloid β-protein-induced signaling4).
We successfully synthesized another two muscarinic toxins bearing different receptor subtype selectivity.
These are muscarinic toxin 3 (MT3) and muscarinic toxin α (MTα). We determined the disulfide arrangementof synthetic MT35) and MTα, although the experimental details have not yet published for MTα. MT3 wasisolated from the green mamba Dendroaspis angusticeps and is composed of 65 amino acid residues. This
peptide shows selectivity for the M4 receptor with low affinity to M1 receptor, and no binding to M2, M3, and M5
receptors6-9). Another 66-residue peptide toxin, MTα is reported to be a component of the venomous toxins of
the black mamba Dendroaspis polylepis. This peptide possesses high affinity to all five subtypes;
inhibition constants for M1 through M5 are 23 nM, 44 nM, 3 nM, 5 nM, and 8 nM, respectively8, 10, 11). As far as
we know, a specific ligand to M3 and M5 does not exist, thus, MTα is attractive for this reason although thesubtype selectivity is rather low.
Combined utilization with already commercially available MT1 (Code 4341-s) and MT7, the researchconcerning biological functions elicited through muscarinic acetylcholine receptors should advancesignificantly, using these chemically synthesized MT3 and MTα.
1) K.N. Bradley, Pharmacol. Ther., 85, 87 (2000). (Review)
2) T.G. Beach, D.G. Walker, P.E. Potter, L.I. Sue, and A. Fisher, Brain Res., 905, 220 (2001). (Pharmacol.)3) C. Hock, A. Maddalena, A. Raschig, F. Mu
ller-Spahn, G. Eschweiler, K. Hager, I. Heuser, H. Hampel,
T. Mu
ller-Thomsen, W. Oertel M. Wienrich, A. Signorell, C. Gonzalez-Agosti, and R.M. Nitsch, J. Protein Folding
Disord., 10, 1 (2003). (Pharmacol.)4) Z. Gu, P. Zhong, and Z. Yan, J. Biol. Chem., 278, 17546 (2003). (Pharmacol.; Role in Aβ -Induced Signaling)5) S. Katayama, M. Ishimaru, H. Nishio, Y. Nishiuchi, and T. Kimura, Peptide Science 2004, 161 (2005).
(S-S Bond of MT3)
6) M. Jolkkonen, P.L.M. van Giersbergen, U. Hellman, C. Wernstedt, and E. Karlsson, FEBS Lett., 352, 91 (1994).
(Original; MT3)
7) J.-S. Liang, J. Carsi-Gabrenas, J.L. Krajewski, J.M. McCafferty, S.L. Purkerson, M.P. Santiago, W.L. Strauss, H.H.
Valentine, and L.T. Potter, Toxicon, 34, 1257 (1996). (Original; m4-toxin)
8) A. Adem and E. Karlsson, Life Sci., 60, 1069 (1997). (Pharmacol.; Muscarinic Receptor Subtype Specificity)9) M. C. Olianas, A. Adem, E. Karlsson, and P. Onali, Eur. J. Pharmacol., 357, 235 (1998).
(Pharmacol.; cAMP-Coupled M4 Receptor)10) M. Jolkkonen, P.L.M. van Giersbergen, U. Hellman, C. Wernstedt, A. Oras, N. Satyapan, A. Adem, and E. Karlsson,
Eur. J. Biochem., 234, 579 (1995). (Original; MTα)11) M. Jolkkonen, A. Oras, T. Toomela, E. Karlsson, J. Ja
rv, and K.E.O. Akerman, Toxicon, 39, 377 (2001). (Pharmacol.;Mechanism of Receptor Binding)– 98 –

Na+, K+-ATPase Inhibitor-1 See Code 4216 SPAI-1 (Porcine) on page 140

Compound4441-s

Neuroendocrine Regulatory Peptide-1 (Human)
NERP-1 (Human)
Arg-Pro-Glu-Ser-Ala-Leu-Leu-Gly-Gly-SerGlu-Ala-Gly-Glu-Arg-Leu-Leu-Gln-Gln-GlyLeu-Ala-Gln-Val-Glu-Ala-NH2-20

(M.W. 2679.0)

Price:Yen

C113H192N36O39

Vial

0.1 mg10,000Vial

0.1 mg10,000Vial

0.1 mg13,000[954420-50-9]

Endogenous Suppressor of Vasopressin Release4442-s-20

Neuroendocrine Regulatory Peptide-1 (Rat)
NERP-1 (Rat)
Leu-Glu-Gly-Ser-Phe-Leu-Gly-Gly-Ser-GluAla-Gly-Glu-Arg-Leu-Leu-Gln-Gln-Gly-LeuAla-Gln-Val-Glu-Ala-NH2(M.W. 2558.8)

C110H180N32O38[954420-51-0]

Endogenous Suppressor of Vasopressin Release4443-s-20

Neuroendocrine Regulatory Peptide-2 (Human)
NERP-2 (Human)
Pyr-Ala-Glu-Ala-Thr-Arg-Gln-Ala-Ala-AlaGln-Glu-Glu-Arg-Leu-Ala-Asp-Leu-Ala-SerAsp-Leu-Leu-Leu-Gln-Tyr-Leu-Leu-Gln-GlyGly-Ala-Arg-Gln-Arg-Gly-Leu-Gly-NH2(M.W. 4064.5)

C173H288N56O57

Endogenous Suppressor of Vasopressin Release– 99 –and Proteins

Code

Biologically Active Peptides

Neuroendocrine Regulatory Peptides

Neuroendocrine Regulatory Peptides (continued)
Code

Compound4444-s

Neuroendocrine Regulatory Peptide-2 (Rat)
NERP-2 (Rat)
Pyr-Ala-Glu-Ala-Thr-Arg-Gln-Ala-Ala-AlaGln-Glu-Glu-Arg-Leu-Ala-Asp-Leu-Ala-SerAsp-Leu-Leu-Leu-Gln-Tyr-Leu-Leu-Gln-GlyGly-Ala-Arg-Gln-Arg-Asp-Leu-Gly-NH2-20

(M.W. 4122.5)

Price:Yen
Vial

0.1 mg13,000C175H290N56O59

Endogenous Suppressor of Vasopressin Release"Peptidome", one of the principle research fields in the post-genome era, is a powerful method to discovernovel peptides [http://www.peptidome.jp]. One such study has been reported recently from the collaborationof several groups including National Cardiovascular Center Research Institute and University of Miyazaki. The
peptides disclosed are neuroendocrine regulatory peptide-1 and -2 (abbreviated as NERP-1 and NERP-2,
respectively).
Both peptides were isolated either from medullary thyroid carcinoma TT cells or rat brain applying modern
techniques of peptide chemistry / biochemistry. Human and rat NERP-1 are composed of 26 and 25 amino acidresidues, respectively, and NERP-2 of both species are composed of 38 amino acid residues, all contain the
carboxyl-terminal amide functionality. Interestingly, these peptides were the segments of the neurosecretory
protein VGF, suggesting a unique processing signal for NERP-2.
NERP-1 (Human): RPESALLGGSEAGERLLQQGLAQVEA-NH2
LEGSFLGGSEAGERLLQQGLAQVEA-NH2
NERP-1 (Rat):
NERP-2 (Human): <EAEATRQAAAQEERLADLASDLLLQYLLQGGARQRGLG-NH2<EAEATRQAAAQEERLADLASDLLLQYLLQGGARQRDLG-NH2
NERP-2 (Rat):
Biological activity reported is: i) suppression of vasopressin release induced by intracerebroventricularadministration of angiotensin II in rat and ii) suppression of basal and angiotensin II-induced vasopressin
secretion from the paraventricular and supraoptic nuclei of rat hypothalamus in vitro. Considering the fact that
NERPs coexist with vasopressin in the hypothalamus, these newly identified peptides may be "potent
endogenous suppressor of vasopressin release", thus implying an essential role in body fluid homeostasis.
1) H. Yamaguchi, K. Sasaki, Y. Satomi, T. Shimbara, H. Kageyama, M.S. Mondal, K. Toshinai, Y. Date,
L.J. González, S. Shioda, T. Takao, M. Nakazato, and N. Minamino, J. Biol., Chem., 282, 26354 (2007). (Original)
2) E. Mishiro-Sato, K. Sasaki, T. Matsuo, H. Kageyama, H. Yamaguchi, Y. Date, M. Matsubara, T. Ishizu,
K. Yoshizawa-Kumagaye, Y. Satomi, T. Takao, S. Shioda, M. Nakazato, and N. Minamino, J. Neurochem., 114, 1097
(2010). (Processing & Histochem.)

Neo-Endorphins
4090-v-20

α-Neo-Endorphin (Porcine)
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro-Lys(M.W. 1228.4)

Vial

0.5 mg6,600

C60H89N15O131) K. Kangawa, N. Minamino, N. Chino, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun.,99, 871 (1981). (Original)

4091-v-20

β-Neo-Endorphin (Porcine)
Tyr-Gly-Gly-Phe-Leu-Arg-Lys-Tyr-Pro(M.W. 1100.3)

C54H77N13O12

Vial

0.5 mg6,600[77739-21-0]

1) N. Minamino, K. Kangawa, N. Chino, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun.,99, 864 (1981). (Original)– 100 –

Neurokinins
4154-v

Neurokinin A*
Neuromedin L, Substance K(Human, Porcine, Rat, Mouse)
His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2

-20

Vial

0.5 mg3,900

Neurokinin A*
Bulk
Neuromedin L, Substance K(Human, Porcine, Rat, Mouse)
His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2 • 2AcOH • 5H2O

25 mg

59,000(M.W. 1133.3)

4154
-20

Price:Yen

C50H80N14O14S(M.W. 1133.3 • 120.10 • 90.08)[86933-74-6]

C50H80N14O14S • 2CH3COOH • 5H2O

NK2 Receptor Selective Agonist
1) S. Kimura, M. Okada, Y. Sugita, I. Kanazawa, and E. Munekata, Proc. Jpn. Acad., 59 (B), 101 (1983).
(Original; Porcine Neurokinin A)
2) K. Kangawa, N. Minamino, A. Fukuda, and H. Matsuo, Peptide Chemistry 1983, 309 (1984).
(Original; Porcine Neuromedin L)
3) H. Nawa, T. Hirose, H. Takashima, S. Inayama, and S. Nakanishi, Nature, 306, 32 (1983).
(Original; Porcine Substance K)
4) A.J. Harmar, A. Armstrong, J.C. Pascall, K. Chapman, R. Rosie, A. Curtis, J. Going, C.R.W. Edwards, and G. Fink,
FEBS Lett., 208, 67 (1986). (cDNA Seq.; Human)4317-v-20

Vial

0.5 mg3,900

Neurokinin B
Bulk
Neuromedin K(Human, Porcine, Bovine, Rat, Mouse)
Asp-Met-His-Asp-Phe-Phe-Val-Gly-Leu-Met-NH2 • 1/ 2 AcOH• 4H2O

25 mg

59,000

Neurokinin B
Neuromedin K(Human, Porcine, Bovine, Rat, Mouse)
Asp-Met-His-Asp-Phe-Phe-Val-Gly-Leu-Met-NH2(M.W. 1210.4)

4317
-20

C55H79N13O14S2(M.W. 1210.4 •30.03• 72.06)[86933-75-7]

C55H79N13O14S2 • 1/2 CH3COOH• 4H2O

NK3 Receptor Selective Agonist
1) S. Kimura, M. Okada, Y. Sugita, I. Kanazawa, and E. Munekata, Proc. Jpn. Acad., 59 (B), 101 (1983).
(Original; Porcine Neurokinin B)
2) K. Kangawa, N. Minamino, A. Fukuda, and H. Matsuo, Biochem. Biophys. Res. Commun., 114, 533 (1983).
(Original; Porcine Neuromedin K)
3) M.K. Chawla, G.M. Gutierrez, W.S. Young III, N.T. McMullen, and N.E. Rance, J. Comp. Neurol., 384, 429 (1997).
(Neurokinin B Nucleotide Seq.; Human)4) T.I. Bonner., H.-U. Affolter, A.C. Young, and W.S. Young III, Mol. Brain Res., 2, 243 (1987). (cDNA Seq.; Rat)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 101 –and Proteins

CompoundBiologically Active Peptides

CodeNeuromedins
List of Neuromedins
CodeCompoundQuantity

Price: Yen

Page
102

4152-v

Neuromedin B

0.5 mg vial

3,900

4153-v

Neuromedin C [GRP (18-27)]

0.5 mg vial

3,900

102

4426-s

Neuromedin S (Human)

0.1 mg vial

11,000103

4427-s

Neuromedin S (Rat)

0.1 mg vial

12,0001034377-v

Neuromedin U (Rat)

0.5 mg vial

20,000104

CodeCompound4152-v

Neuromedin B*(Human, Porcine, Rat)
Gly-Asn-Leu-Trp-Ala-Thr-Gly-His-Phe-Met-NH2

-20

Vial

0.5 mg3,900

Neuromedin B*
Bulk(Human, Porcine, Rat)
Gly-Asn-Leu-Trp-Ala-Thr-Gly-His-Phe-Met-NH2 •AcOH • 5H2O

25 mg

59,000(M.W. 1132.3)

4152
-20

Price:Yen

C52H73N15O12S(M.W. 1132.3 • 60.05 • 90.08)[87096-84-2]

C52H73N15O12S • CH3COOH • 5H2O

1) N. Minamino, K. Kangawa, and H. Matsuo, Biochem. Biophys. Res. Commun., 114, 541 (1983). (Original; Porcine)2) I.M. Krane, S.L. Naylor, D. Helin-Davis, W.W. Chin, E.R. Spindel, J. Biol. Chem., 263, 13317 (1988).
(cDNA Seq.; Human)
3) E. Wada, J. Way, A.M. Lebacq-Verheyden, J.F. Battey, J. Neurosci., 10, 2917 (1990). (cDNA Seq.; Rat)

4153-v-20

Vial

0.5 mg3,900

Neuromedin C*
Bulk
Gastrin Releasing Peptide (Human, 18-27)
GRP (18-27)(Human, Porcine, Canine)
Gly-Asn-His-Trp-Ala-Val-Gly-His-Leu-Met-NH2 • 2AcOH • 5H2O

25 mg

59,000

Neuromedin C*
Gastrin Releasing Peptide (Human, 18-27)
GRP (18-27)(Human, Porcine, Canine)
Gly-Asn-His-Trp-Ala-Val-Gly-His-Leu-Met-NH2(M.W. 1120.3)

4153
-20

C50H73N17O11S(M.W. 1120.3 • 120.10 • 90.08)[81608-30-2]

C50H73N17O11S • 2CH3COOH • 5H2O

1) K.A. Roth, C.J. Evans, R.G. Lorenz, E. Weber, J.D. Barchas, and J.K. Chang, Biochem. Biophys. Res. Commun.,
112, 528 (1983). (Original; GRP (18-27))
2) N. Minamino, K. Kangawa, and H. Matsuo, Biochem. Biophys. Res. Commun., 119, 14 (1984).
(Original; Porcine Neuromedin C)
3) M.S. Orloff, J.R. Reeve, Jr., C.M. Ben-Avram, J.E. Shively, and J.H. Walsh, Peptides, 5, 865 (1984). (Seq.; Human)4) J.R. Reeve, Jr., H. Walsh, P. Chew, B. Clark, D. Hawke, and J.E. Shively, J. Biol. Chem., 258, 5582 (1983).
(Isolation & Seq.; Canine Bombesin-like Peptide)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 102 –

Neuromedins (continued)
4426-s

Neuromedin S (Human)
NMS (Human)
Ile-Leu-Gln-Arg-Gly-Ser-Gly-Thr-Ala-AlaVal-Asp-Phe-Thr-Lys-Lys-Asp-His-Thr-AlaThr-Trp-Gly-Arg-Pro-Phe-Phe-Leu-Phe-ArgPro-Arg-Asn-NH2-20

(M.W. 3791.3)

Price:Yen
Vial

0.1 mg11,000C173H265N53O44

Food Intake Suppressor / Regulator of Circadian Rhythm• This compound is distributed through Peptide Institute, Inc. under the license of National Cardiovascular Center andTakeda Pharmaceutical Company Limited.

4427-s-20

Neuromedin S (Rat)
NMS (Rat)
Leu-Pro-Arg-Leu-Leu-His-Thr-Asp-Ser-ArgMet-Ala-Thr-Ile-Asp-Phe-Pro-Lys-Lys-AspPro-Thr-Thr-Ser-Leu-Gly-Arg-Pro-Phe-PheLeu-Phe-Arg-Pro-Arg-Asn-NH2(M.W. 4241.9)

Vial

0.1 mg12,000C193H307N57O49S

Food Intake Suppressor / Regulator of Circadian Rhythm• This compound is distributed through Peptide Institute, Inc. under the license of National Cardiovascular Center andTakeda Pharmaceutical Company Limited.

Neuromedin S (NMS) was discovered from rat brain extracts applying a reverse-pharmacological techniqueusing FM-4/TGR-1 as the target orphan receptor. Based on the partial amino acid sequence of the isolated
peptide, the cDNA sequences of rat, mouse, and human NMS was deduced, showing that the former two
peptides are composed of 36 amino acid residues, and the latter of 33 amino acid residues, respectively. All ofthese peptides have the carboxyl-terminal amide structure. Very interestingly, the carboxyl-terminal 7 residuesof these NMSs are identical to that of neuromedin U (NMU, code 4377-v for the rat peptide), which is also
known to be the ligand of FM-3/GPR66 (NMU receptor type-1) and FM-4/TGR-1 (NMU receptor type-2).
Intracerebroventricular administration of NMS (1 nmol) affects the circadian rhythm of locomotor activity in
rats1). NMS is also found to be an anorexic hormone having the following characteristics2): i) food intake
suppression of NMS in rats (1 nmol) is more potent than that of NMU, ii) NMS counteracts the neuropeptide Y(NPY), ghrelin, and agouti-related protein (AGRP)-evoked food intake stimulation, and iii) NMS augments thelevel of proopiomelanocortin mRNA and corticotropin-releasing factor mRNA, suggesting the involvement ofthese peptides in its anorexigenic effects of NMS.
1) K. Mori, M. Miyazato, T. Ida, N. Murakami, R. Serino, Y. Ueta, M. Kojima, and K. Kangawa, EMBO J., 24, 325 (2005).
(Original)
2) T. Ida, K. Mori, M. Miyazato, Y. Egi, S. Abe, K. Nakahara, M. Nishihara, K. Kangawa, and N. Murakami,
Endocrinology, 146, 4217 (2005). (Pharmacol.; Anorexic Hormone)3) E. Vigo, J. Roa, M. López, J.M. Castellano, R. Fernandez-Fernandez, V.M. Navarro, R. Pineda, E. Aguilar, C.
Diéguez, L. Pinilla, and M. Tena-Sempere, Endocrinology, 148, 813 (2007). (Pharmacol.; Effect on LH Secretion)4) T. Sakamoto, K. Mori, K. Nakahara, M. Miyazato, K. Kangawa, H. Sameshima, and N. Murakami, Biochem. Biophys.
Res. Commun., 361, 457 (2007). (Pharmacol.; Antidiuretic Effect)5) M. Jászberényi, Z. Bagasi, B. Thurzó, I. Foldesi, and G. Telegdy, Horm. Behav., 52, 631 (2007).
(Pharmacol.; Endocrine & Behavioral Effect)6) A. Peier, J. Kosinski, K. Cox-York, Y. Qian, K. Desai, Y. Feng, P. Trivedi, N. Hastings, and D.J. Marsh, Endocrinology,
150, 3101 (2009). (Pharmacol.)7) M. Miyazato, K. Mori, T. Ida, M. Kojima, N. Murakami, and K. Kangawa, Regul. Pept., 145, 37 (2008). (Review)– 103 –and Proteins

CompoundBiologically Active Peptides

CodeNeuromedins (continued)
Code

Compound4377-v

Neuromedin U (Rat)
NMU-23 (Rat)
Tyr-Lys-Val-Asn-Glu-Tyr-Gln-Gly-Pro-ValAla-Pro-Ser-Gly-Gly-Phe-Phe-Leu-Phe-ArgPro-Arg-Asn-NH2-20

(M.W. 2643.0)

Price:Yen

C124H180N34O31

Vial

0.5 mg20,000[117505-80-3]

Food Intake Suppressor
Neuromedin U (NMU), possessing uterus contractile activity, was first isolated from porcine spinal cord as
NMU-8 and NMU-251,2). Later, rat NMU was identified as a single entity, consisting of 23 amino acid residues(NMU-23) because of lack of the double basic site (Gly-Gly substitution for Arg-Arg). In addition to its role insmooth muscle contraction, NMU exerts some other biological activities such as increase of blood pressure,induction of ACTH release, etc. However, the specific receptor for NMU has long been unidentified. NMU
itself is present in the brain as well as in the gut.
Applying the recently developed technique of using the so-called orphan G-protein coupled receptors,
NMU has been reported to be a ligand of two structurally related receptors by several groups [reference 3 and
J. Biol. Chem., 275 , 20247 (2000), ibid., 21068, ibid., 29528]. One is expressed predominantly inperipheral tissue, while another is expressed in the CNS. It is especially interesting to note that in the rat brain,
the second form is expressed in the paraventricular nucleus of the hypothalamus, suggesting NMU to be
involved in the regulation of food intake. Actually, NMU mRNA is located abundantly in the ventromedial
hypothalamic regions and its level is reduced in rats fasted for 48 h. When NMU is injected at a dose of 3 or 10µg in rats, overnight food intake is significantly decreased and accordingly body weight is reduced3,4). Water
intake was also found to be suppressed3).
Taken together, NMU may be one of the physiological mediators of food intake and may be useful inclarifying the intricate mechanism of obesity and leanness.
1) J.M. Conlon, J. Domin, L. Thim, V. DiMarzo, H.R. Morris, and S.R. Bloom, J. Neurochem., 51, 988 (1988).
(Original; Primary Structure)2) N. Minamino, K. Kangawa, M. Honzawa, and H. Matsuo, Biochem. Biophys. Res. Commun., 156, 355 (1988).
(Original; Primary Structure)3) A.D. Howard, R. Wang, S.-S. Pong, T.N. Mellin, A. Strack, X.-M. Guan, Z. Zeng, D.L. Williams, Jr., S.D. Feighner,
C.N. Nunes, B. Murphy, J.N. Stair, H. Yu, Q. Jiang, M.K. Clements, C.P. Tan, K.K. McKee, D.L. Hreniuk, T.P.
McDonald, K.R. Lynch, J.F. Evans, C.P. Austin, C.T. Caskey, L.H.T. Van der Ploeg, and Q. Liu, Nature,406, 70 (2000). (Pharmacol.)4) M. Nakazato, R. Hanada, N. Murakami, Y. Date, M.S. Mondal, M. Kojima, H. Yoshimatsu, K. Kangawa, and
S. Matsukura, Biochem. Biophys. Res. Commun., 277, 191 (2000). (Pharmacol.)5) P.J. Brighton, P.G. Szekeres, and G.B. Willars, Pharmacol. Rev., 56, 231 (2004). (Review)6) A. Peier, J. Kosinski, K. Cox-York, Y. Qian, K. Desai, Y. Feng, P. Trivedi, N. Hastings, and D.J. Marsh, Endocrinology,
150, 3101 (2009). (Pharmacol.)Neuromedin K See Code 4317 Neurokinin B on page 101
Neuromedin L See Code 4154 Neurokinin A on page 101
NMU-23 (Rat) See Code 4377 Neuromedin U (Rat) 102– 104 –

Neuronostatin4452-v

Neuronostatin-13 (Human)(Chimpanzee, Porcine, Canine, Ovine, Bovine, Chicken)
Leu-Arg-Gln-Phe-Leu-Gln-Lys-Ser-Leu-AlaAla-Ala-Ala-NH2

New

-20

(M.W. 1415.7)

Price:Yen
Vial

0.5 mg8,000

C64H110N20O16

Brain/Gut Hormone in Pro-Somatostatin with Neuronal/Neuroendocrine/Cardiovascular Activity
In the post-genome era, a novel peptide called neuronostatin-13 has been predicted in pro-somatostatin
gene sequence based on bioinformatics method. Neuronostatin-13 was purified from porcine tissue by
immuno-affinity procedure and then confirmed to be an endogenous peptide. Actually, neuronostatin-13 is a
13 amino acid residue peptide with carboxyl-terminal amidation, the primary structure of which is conserved inhuman, chimpanzee and some other mammals.
The biological functions of neuronostatin-13 reported so far include: i) intracerebroventricularadministration of neuronostatin-13 in rats increased blood pressure but suppressed food intake and water
drinking (0.3 nmol per rat)1), ii) in both brain and gastric cells, neuronostatin-13 stimulates c-Fos expression
and cell proliferation/migration1), and iii) this peptide depresses cardiac contractile function2). Thus,
neuronostatin-13 might be a new member of brain/gut hormones. In addition, the function of neuronostatin-13
is not mediated by somatostatin receptors. Neuronostatin-13 with "diverse neuronal, neuroendocrine, andcardiovascular actions" could be of interest in the research field of hormonal regulation of the body.
1) W.K. Samson, J.V. Zhang, O. Avsian-Kretchmer, K. Cui, G.L.C. Yosten, C. Klein, R.-M. Lyu, Y.X. Wang, X.Q. Chen,
J. Yang, C.J. Price, T.D. Hoyda, A.V. Ferguson, X.-bin Yuan, J.K. Chang, and A.J.W. Hsueh, J. Biol. Chem., 283,
31949 (2008). (Original; Structure & Pharmacol.)2) Y. Hua, H. Ma, W.K. Samson, and J. Ren, Am. J. Physiol. Regul. Integr. Comp. Physiol., 297, 682 (2009).
(Pharmacol.)– 105 –and Proteins

CompoundBiologically Active Peptides

CodeNeuropeptide B
CodeCompound4459-v

Neuropeptide B-29 (Rat) (Non-Brominated Form)
NPB-29 (Rat) (Non-brominated)
Trp-Tyr-Lys-Pro-Ala-Ala-Gly-Ser-His-HisTyr-Ser-Val-Gly-Arg-Ala-Ala-Gly-Leu-LeuSer-Ser-Phe-His-Arg-Phe-Pro-Ser-Thr

New

-20

(M.W. 3188.5)

Price:Yen
Vial

0.5 mg33,000C147H211N43O38

Ligand of NPBWR1 (GPR7)
cDNA sequences encoding neuropeptide B (NPB) of several species were reported in 2002 1),2) .
Simultaneously, endogenous bovine NPB was identified to be a 29-residue peptide with a uniqueC-6-brominated Trp residue at its position 11),2). However, as far as we know, it has not been reported whether
Trp at position 1 in rat NPB is brominated or not. In the mean time, there have been some papers evaluating thebiological activity of rat non-brominated NPB in food intake [Neuropeptide B-29 (Rat) (Non-BrominatedForm)] in which modulation of food intake in rat seems to be greatly modified by corticotropin-releasing factor
3). Very recently, a novel activity of Neuropeptide B-29 (Rat) (Non-Brominated Form) has been reported, thatis, induction of slow wave sleep in mice when administered during the dark period (1 and 10 nmol / mice, i.c.v.)
4). This effect was abolished by either deletion of Trp at position 1 of NPB or knockout of neuropeptide B/W
receptor-1 (NPBWR1, previously named GPR7) in mice.
Synthetic Neuropeptide B-29 (Rat) (Non-Brominated Form) might be a useful tool for elucidating thebiological function of NPB regardless of the endogenous NPB being brominated or not.
1) R. Fujii, H. Yoshida, S. Fukusumi, Y. Habata, M. Hosoya, Y. Kawamata, T. Yano, S. Hinuma, C. Kitada, T. Asami,
M. Mori, Y. Fujisawa, and M. Fujino, J. Biol. Chem., 277, 34010 (2002). (Original; cDNA Sequence)2) H. Tanaka, T. Yoshida, N. Miyamoto, T. Motoike, H. Kurosu, K. Shibata, A. Yamanaka, S.C. Williams,
J.A. Richardson, N. Tsujino, M.G. Garry, M.R. Lerner, D.S. King, B.F. O'Dowd, T. Sakurai, and M. Yanagisawa,
Proc. Natl. Acad. Sci. U.S.A., 100, 6251 (2003). (Pharmacol.)3) S. Aikawa, M. Ishii, M. Yanagisawa, Y. Sakakibara, and T. Sakurai, Regul. Pept., 151, 147 (2008).
(Pharmacol.; Food Intake Regulatory Activity)
4) N. Hirashima, T. Tsunematsu, K. Ichiki, H. Tanaka, T.S. Kilduff, and A. Yamanaka, Sleep, in press.
(Pharmacol.; Slow Wave Sleep Induction Activity)– 106 –

Neuropeptide S
4425-v

Neuropeptide S (Human)
NPS (Human)
Ser-Phe-Arg-Asn-Gly-Val-Gly-Thr-Gly-MetLys-Lys-Thr-Ser-Phe-Gln-Arg-Ala-Lys-Ser-20

(M.W. 2187.5)

Price:Yen

C93H155N31O28S

Vial

0.5 mg21,000[412938-67-1]

Novel Modulator of Arousal and Anxiety / Food Intake Suppressor
Arousal and anxiety-like behavior are regulated by several modulators in the central nervous system,
including classical neurotransmitters (i.e. noradrenaline) and peptides (i.e. orexin). In a recent paper, a new
peptide named neuropeptide S (NPS), has been identified as a novel modulator of wakefulness and anxiety1).
Human NPS is a 20-amino acid peptide1). Four other mammalian NPSs and chicken NPS were deducedwith high sequence similarity to human NPS.
Human:
Chimpanzee:
Dog:
Rat:
Mouse:
Chicken:SFRNGVGTGM KKTSFQRAKSSFRNGVGTGM KKTSFRRAKSSFRNGVGTGM KKTSFRRAKSSFRNGVGSGV KKTSFRRAKQSFRNGVGSGA KKTSFRRAKQSFRNGVGSGI KKTSFRRAKSNPS-expressing neurons are uniquely localized in an unidentified cluster of cells between locus coeruleus
and Barrington's nucleus in the rat brain. Human NPS induces mobilization of intracellular Ca2+ ions throughthe expressed human NPS receptor (ED50 = 9.4 nM). Synthetic NPS exerts the following functions upon i.c.v.
administration: i) increased locomotor activity in mice (＞0.1 nmol), ii) increased wakefulness in rats by
reducing all sleep stages [REM, slow wave sleep stage 1 (SWS1), and SWS2] (＞0.1 nmol), and iii)
dose-dependent attenuation of anxiety-like behavior in mice. The exact mechanism is not yet understood andthese functions might be mutually related through an arousal-promoting effect. Since NPS is produced bypreviously unidentified neurons in a brain stem region known for regulating anxiety and arousal, it is expected
this novel peptide will help unravel the mechanism of sleep disorders and anxiety.
1) Y.-L. Xu, R.K. Reinscheid, S. Huitron-Resendiz, S.D. Clark, Z. Wang, S.H. Lin, F.A. Brucher, J. Zeng,
N.K. Ly, S.J. Henriksen, L. de Lecea, and O. Civelli, Neuron, 43, 487 (2004). (Original)
2) R.K. Reinscheid and Y.-L. Xu, FEBS J., 272, 5689 (2005). (Minireview)3) B. Beck, B. Fernette, and A. Stricker-Krongrad, Biochem. Biophys. Res. Commun., 332, 859 (2005). (Pharmacol.)4) K.L. Smith, M. Patterson, W.S. Dhillo, S.R. Patel, N.M. Semjonous, J.V. Gardiner, M.A. Ghatei, and S.R. Bloom,
Endocrinology, 147, 3510 (2006). (Pharmacol.)5) A. Fedeli, S. Braconi, D. Economidou, N. Cannella, M. Kallupi, R. Guerrini, G. Calo, C. Cifani, M. Massi,
and R. Ciccocioppo, Eur. J. Neurosci., 30, 1594 (2009). (Pharmacol.)– 107 –and Proteins

CompoundBiologically Active Peptides

CodeNeuropeptide Y (NPY) and Related Peptides
1) Y. Dumont, J.-C. Martel, A. Fournier, S. St-Pierre, and R. Quirion, Progr. Neurobiol., 38, 125 (1992). (Review)2) C. Wahlestedt and D.J. Reis, Annu. Rev. Pharmacol. Toxicol., 33, 309 (1993). (Review)

Code

Compound4158-sNPY (Human, Rat)*
Neuropeptide Y (Human, Rat)
Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-GluAsp-Ala-Pro-Ala-Glu-Asp-Met-Ala-Arg-TyrTyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-LeuIle-Thr-Arg-Gln-Arg-Tyr-NH2-20

(M.W. 4271.7)

4158-v-20

Price:Yen

C189H285N55O57S

Vial

0.1 mg12,000Vial

0.5 mg41,000[90880-35-6]

NPY (Human, Rat)*
Neuropeptide Y (Human, Rat)
Purity Information : Q P See page IV (XVI)

1) C.D. Minth, S.R. Bloom, J.M. Polka, and J.E. Dixon, Proc. Natl. Acad. Sci. U.S.A., 81, 4577 (1984).
(Original; Human cDNA)2) D. Larhammer, A. Ericsson, and H. Persson, Proc. Natl. Acad. Sci. U.S.A., 84, 2068 (1987).
(Original; Rat Nucleotide Seq.)

4162-s-20

NPY (Porcine, Bovine)*
Neuropeptide Y (Porcine, Bovine)
Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-GluAsp-Ala-Pro-Ala-Glu-Asp-Leu-Ala-Arg-TyrTyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-LeuIle-Thr-Arg-Gln-Arg-Tyr-NH2(M.W. 4253.6)

4162-v-20

C190H287N55O57

Vial

0.1 mg12,000Vial

0.5 mg41,000Vial

0.1 mg12,000[83589-17-7]

NPY (Porcine, Bovine)*
Neuropeptide Y (Porcine, Bovine)
Purity Information : Q P See page IV (XVI)
1) K. Tatemoto, Proc. Natl. Acad. Sci. U.S.A., 79, 5485 (1982). (Original)

4314-s-20

[Leu31, Pro34]-NPY (Porcine)[Leu31, Pro34]-Neuropeptide Y (Porcine)(Bovine)Tyr-Pro-Ser-Lys-Pro-Asp-Asn-Pro-Gly-GluAsp-Ala-Pro-Ala-Glu-Asp-Leu-Ala-Arg-TyrTyr-Ser-Ala-Leu-Arg-His-Tyr-Ile-Asn-LeuLeu-Thr-Arg-Pro-Arg-Tyr-NH2(M.W. 4222.6)

C190H286N54O56[125580-28-1]

Purity Information : QP See page IV (XVI)NPY Y1-Receptor Selective Agonist
1) J. Fuhlendorff, U. Gether, L. Aakerlund, N. Langeland-Johansen, H. Thgersen, S.G. Melberg, U.B. Olsen,
O. Thastrup, and T.W. Schwartz, Proc. Natl. Acad. Sci. U.S.A., 87, 182 (1990). (Original)
2) S.P. Sheikh, Am. J. Physiol., 261, G701 (1991). (Pharmacol.)*The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 108 –

Neuropeptide Y (NPY) and Related Peptides (continued)
4315-sNPY (Porcine, 13-36)
Neuropeptide Y (Porcine, 13-36)(Bovine)
Pro-Ala-Glu-Asp-Leu-Ala-Arg-Tyr-Tyr-SerAla-Leu-Arg-His-Tyr-Ile-Asn-Leu-Ile-ThrArg-Gln-Arg-Tyr-NH2-20

(M.W. 2982.4)

Price:Yen

C135H209N41O36

Vial

0.1 mg

6,000[113662-54-7]

NPY Y2-Receptor Selective Agonist
1) M.W. Walker and R.J. Miller, Mol. Pharmacol., 34, 779 (1988). (Pharmacol.)2) J. Fuhlendorff, U. Gether, L. Aakerlund, N. Langeland-Johansen, H. Thgersen, S.G. Melberg, U.B. Olsen,
O. Thastrup, and T.W. Schwartz, Proc. Natl. Acad. Sci. U.S.A., 87, 182 (1990). (Pharmacol.)3) S.P. Sheikh, Am. J. Physiol., 261, G701 (1991). (Pharmacol.)Neuropeptide W
4403-v-20

Neuropeptide W-30 (Human)
NPW30 (Human), hL8C
Trp-Tyr-Lys-His-Val-Ala-Ser-Pro-Arg-TyrHis-Thr-Val-Gly-Arg-Ala-Ala-Gly-Leu-LeuMet-Gly-Leu-Arg-Arg-Ser-Pro-Tyr-Leu-Trp(M.W. 3543.1)

C165H249N49O37S

Vial

0.5 mg33,000Vial

0.5 mg33,000[383415-80-3]

Food Intake-Regulating Peptide / GPR7/GPR8 Ligand
4404-v-20

Neuropeptide W-30 (Rat)
NPW30 (Rat), rL8C
Trp-Tyr-Lys-His-Val-Ala-Ser-Pro-Arg-TyrHis-Thr-Val-Gly-Arg-Ala-Ser-Gly-Leu-LeuMet-Gly-Leu-Arg-Arg-Ser-Pro-Tyr-Leu-Trp(M.W. 3559.1)

C165H249N49O38S[383415-90-5]

Food Intake-Regulating Peptide / GPR7/GPR8 Ligand
A method based on "reverse pharmacology" has been successfully applied to identification of novel ligands
for the orphan receptors. Three groups discovered identical ligands to GPR7 and GPR8, which were designatedeither "neuropeptide W (NPW)" or "L8C" 1,2,3) (in this brief introduction, "NPW" is used as the abbreviation of the
discovered peptide).
Based on the isolated peptide from porcine hypothalamus, cDNA sequence of human and rat NPW werepredicted. Human and rat NPW were deduced to be a 30- or 23-residue peptide [NPW30 or NPW23(corresponding to the amino-terminal 23 residues of NPW30)] because of the existence of the potential double
basic cleaving sites in the precursor. Chemically synthesized NPW30 (and also NPW23) showed: i) binding
activity to both GPR7 and GPR8 at nM or even lower concentrations; ii) inhibitory activity of cAMP
accumulation induced by forskolin; iii) stimulatory activity of prolactin release; and iv) stimulation of
aggregation of melanosomes in melanophres. In addition to these, some roles in food intake regulation4) aresuggested to be in line with the predominant localization of its mRNA in the brain. Later, the implications forthe control of stress hormone secretion by NPW was reported5). NPW should serve as an essential tool forunderstanding biological events originating from CNS activation or inhibition. In addition, the presence of
NPW in gastric antral G cell, was reported6). This finding provides an interesting view for the regulation ofgastric function by this novel brain/gut peptide.

– 109 –and Proteins

CompoundBiologically Active Peptides

CodeNeuropeptide W (continued)
1) Y. Shimomura, M. Harada, M. Goto, T. Sugo, Y. Matsumoto, M. Abe, T. Watanabe, T. Asami, C. Kitada, M. Mori,
H. Onda, and M. Fujino, J. Biol. Chem., 277, 35826 (2002). (Original; NPW)
2) S. Brezillon, V. Lannoy, J.-D. Franssen, E. Le Poul, V. Dupriez, J. Lucchetti, M. Detheux, and M. Parmentier,J. Biol. Chem., 278, 776 (2003). (Original; L8C)
3) H. Tanaka, T. Yoshida, N. Miyamoto, T. Motoike, H. Kurosu, K. Shibata, A. Yamanaka, S.C. Williams,
J.A. Richardson, N. Tsujino, M.G. Garry, M.R. Lerner, D.S. King, B.F. O'Dowd, T. Sakurai, and M. Yanagisawa,
Proc. Natl. Acad. Sci. U.S.A., 100, 6251 (2003). (cDNA )4) M.S. Mondal, H. Yamaguchi, Y. Date, T. Shimbara, K. Toshinai, Y. Shimomura, M. Mori, and M. Nakazato,
Endocrinology, Endocrinology, 144, 4729 (2003). (Pharmacol.)5) M.M. Taylor, E.A. Yuill, J.R. Baker, C.C. Ferri, A.V. Ferguson, and W.K. Samson, Am. J. Physiol. Regul. Integr. Comp.
Physiol., 288, R270 (2005). (Pharmacol.)6) M.S. Mondal, H. Yamaguchi, Y. Date, K. Toshinai, T. Kawagoe, T. Tsuruta, H. Kageyama, Y. Kawamura, S. Shioda, Y.
Shimomura, M. Mori, and M. Nakazato, J. Endocrinol., 188, 49 (2006). (Pharmacol. & Immunohistochem.)
7) F. Takenoya, S. Kitamura,, H. Kageyama, N. Nonaka, M. Seki, K. Itabashi, Y. Date, M. Nakazato, and S. Shioda,
Regul. Pept., 145, 159 (2008). (Pharmacol.)• This compound is distributed through Peptide Institute, Inc. under the license of Takeda Pharmaceutical Company
Limited.

Neurotensin
CodeCompound4029-v

Neurotensin(Human, Bovine, Canine, Mouse)
Pyr-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-ProTyr-Ile-Leu-20

(M.W. 1672.9)

4029
-20

Price:Yen

C78H121N21O20

0.5 mg

3,300

Bulk

25 mg

50,000[55508-42-4]

Neurotensin(Human, Bovine, Canine, Mouse)
Pyr-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-ProTyr-Ile-Leu • 2AcOH • 6H2O
(M.W. 1672.9 • 120.10 • 108.09)

Vial

C78H121N21O20 • 2CH3COOH • 6H2O

1) R. Carraway and S.E. Leeman, J. Biol. Chem., 248, 6854 (1973). (Original; Bovine)
2) R.A. Hammer, S.E. Leeman, R. Carraway, and R.H. Williams, J. Biol. Chem., 255, 2476 (1980). (Original; Human)
3) P.R. Dobner, D.L. Barber, L. Villa-Komaroff, and C. McKiernan, Proc. Natl. Acad. Sci. U.S.A., 84, 3516 (1987).
(cDNA Seq.; Canine)
4) P.R. Dobner, J. Fadel, N. Deitemeyer, R.E. Carraway, and A.Y. Deutch, Proc. Natl. Acad. Sci. U.S.A., 98, 8048
(2001). (cDNA Seq.; Mouse)

Neurotoxin NSTX-3
4195-s-20

Neurotoxin NSTX-3(Papua New Guinean Spider, Nephila maculata)

Vial

0.1 mg

9,000

2,4-Dihydroxyphenylacetyl-L-asparaginylN'-(L-arginylputreanyl)-cadaverine(M.W. 664.80)

C30H52N10O7

1) Y. Aramaki, T. Yasuhara, T. Higashijima, M. Yoshioka, A. Miwa, N. Kawai, and T. Nakajima, Proc. Jpn. Acad.,
62 (B), 359 (1986). (Original)
2) T. Teshima, T. Wakamiya, Y. Aramaki, T. Nakajima, N. Kawai, and T. Shiba, Tetrahedron Lett., 28, 3509 (1987).
(Chem. Synthesis; Preliminary)3) T. Teshima, T. Matsumoto, T. Wakamiya, T. Shiba, Y. Aramaki, T. Nakajima, and N. Kawai, Tetrahedron,47, 3305 (1991). (Chem. Synthesis; Total Synthesis)

Nitric Oxide Synthase Inhibitor See Code 2005 Arg(NO2) on page 301– 110 –

Nociceptin
4318-v

Nociceptin (Human)
Orphanin FQ (Human)(Rat, Mouse, Bovine, Porcine)
Phe-Gly-Gly-Phe-Thr-Gly-Ala-Arg-Lys-SerAla-Arg-Lys-Leu-Ala-Asn-Gln-20

Price:Yen(M.W. 1809.0)

C79H129N27O22

Vial

0.5 mg15,000[170713-75-4]

Agonist of Opioid Receptor-Like-1 (ORL1) Receptor
1) J.-C. Meunier, C. Mollereau, L. Toll, C. Suaudeau, C. Moisand, P. Alvinerie, J.-L. Butour, J.-C. Guillemot, P. Ferrara,
B. Monsarrat, H. Mazarguil, G. Vassart, M. Parmentier, and J. Costentin, Nature, 377, 532 (1995).
(Original; Nociceptin-ORL1 Receptor Agonist)
2) R.K. Reinscheid, H.-P. Nothacker, A. Bourson, A. Ardati, R.A. Henningsen, J.R. Bunzow, D.K. Grandy, H. Langen,
F.J. Monsma, Jr., and O. Civelli, Science, 270, 792 (1995). (Original; Orphanin FQ)
3) C. Mollereau, M.-J. Simons, P. Soularue, F. Liners, G. Vassart, J.-C. Meunier, and M. Parmentier, Proc. Natl. Acad.
Sci. U.S.A., 93, 8666 (1996). (Original; Human, Rat, & Mouse Nociceptin-Nucleotide Seq.)
4) J.C. Meunier, Eur. J. Pharmacol., 340, 1 (1997). (Review)5) G. Csaba and K. Tekes, Brain Dev., 27, 465 (2005). (Review)6) Z.S. Zadori, N. Shujaa, L. Koeles, K.P. Kiraly, K. Tekes, and K. Gyires, Peptides, 29, 2257 (2008). (Pharmacol.)Primary structures of human, bovine, mouse, and rat Nociceptin and Nocistatin precursor
Human

MKVLLCDLLL LSLFSSVFSS CQRDCLTCQE KLHPALDSFD LEVCILECEE KVFPSPLWTP

60

BovineMKILFCDLLL LSLFSSVSSS CQKDCLVCRE KLRPTLDSFS LEMCILECEE KAFTSPLWTP

60

Mouse

MKILFCDVLL LSLLSSVFSS CPRDCLTCQE KLHPAPDSFN LKTCILQCEE KVFPRPLWTV

60

Rat

MKILFCDVLL LSLLSSVFSS CPEDCLTCQE RLHPAPGSFN LKLCILQCEE KVFPRPLWTL

60

Human

CTKVMARSSW QLSPAAPEHV AAALYQPRAS EMQHLRRMPR VRSLFQEQ-- ---------E

109

Bovine

CTKVMARGSW QLSPADPDHV AAALDQPRAS EMQHLKRMPR VRSLFQRQ-- ---------K

109

Mouse

CTKVMASGSG QLSPADPELV SAALYQPKAS EMQHLKRMPR VRSLVQVRDA EPGADAEPGA

120

Rat

CTKAMASDSE QLSPADPELT SAALYQSKAS EMQHLKRMPR VRSVVQARDA EPEA------

114

Human

EPEPGMEEAG EMEQKQLQKR FGGFTGARKS ARKLANQKRF SEFMRQYLVL SMQSSQRRRTBovineRTEPGLEEVG EIEQKQLQKR FGGFTGARKS ARKLANQKRF SEFMRQYLVL SMQSSQRRRT

169

Mouse

DAEPGADDAE EVEQKQLQKR FGGFTGARKS ARKLANQKRF SEFMRQYLVL SMQSSQRRRT

180

Rat

DAEPVADEAD EVEQKQLQKR FGGFTGARKS ARKLANQKRF SEFMRQYLVL SMQSSQRRRT

174

Human

LHQNGNV

176

BovineLHQNGNA

176

Mouse

LHQNGNV

187

Rat

LHQNGNV

181

Nocistatin

Nociceptin
169

Nocistatin– 111 –and Proteins

CompoundBiologically Active Peptides

CodeNocistatins
1) G. Csaba and K. Tekes, Brain Dev., 27, 465 (2005). (Review)

Code

Compound4355-v

Nocistatin (Human)
Met-Pro-Arg-Val-Arg-Ser-Leu-Phe-Gln-GluGln-Glu-Glu-Pro-Glu-Pro-Gly-Met-Glu-GluAla-Gly-Glu-Met-Glu-Gln-Lys-Gln-Leu-Gln-20

(M.W. 3561.9)

Price:Yen
Vial

0.5 mg30,000

C149H238N42O53S3

Endogenous Allodynia / Hyperalgesia-Blocking Peptide
Nociceptin Action Blocking Peptide
1) T. Minami, E. Okuda-Ashitaka, Y. Nishiuchi, T. Kimura, S. Tachibana, H. Mori, and S. Ito, Br. J. Pharmacol.,124, 1016 (1998). (Original; Pharmacol.)2) C. Mollereau, M.-J. Simons, P. Soularue, F. Liners, G. Vassart, J.-C. Meunier, and M. Parmentier, Proc. Natl. Acad.
Sci. U.S.A., 93, 8666 (1996). (Original; Prepronociceptin Nucleotide Seq.)
3) T.-L. Lee, F.M.Y. Fung, F.-G. Chen, N. Chou, E. Okuda-Ashitaka, S. Ito, Y. Nishiuchi, T. Kimura, and S. Tachibana,
NeuroReport, 10,1537 (1999). (Original; Identification in Human)
4) Z.S. Zadori, N. Shujaa, L. Koeles, K.P. Kiraly, K. Tekes, and K. Gyires, Peptides, 29, 2257 (2008). (Pharmacol.)4336-v

Nocistatin (Bovine)-20

(Ammonium Form)

Vial

0.5 mg20,000Thr-Glu-Pro-Gly-Leu-Glu-Glu-Val-Gly-GluIle-Glu-Gln-Lys-Gln-Leu-Gln(M.W. 1927.1)

C82H135N21O32

Endogenous Allodynia / Hyperalgesia-Blocking Peptide
Nociceptin Action Blocking Peptide
1) E. Okuda-Ashitaka, T. Minami, S. Tachibana, Y. Yoshihara, Y. Nishiuchi, T. Kimura, and S. Ito, Nature,392, 286 (1998). (Original)
2) B. Nicol, D.J. Lambert, D.J. Rowbothan, E. Okuda-Ashitaka, S. Ito, D. Smart, and A.T. McKnight, Eur. J. Pharmacol.,356, R1 (1998). (Pharmacol.)3) T. Nakagawa, M. Kaneko, S. Inamura, and M. Satoh, Neurosci. Lett., 265, 64 (1999). (Pharmacol.)4) H. Nakano, T. Minami, K. Abe, T. Arai, M. Tokumura, N. Ibii, E. Okuda-Ashitaka, H. Mori , and S. Ito,J. Pharmacol. Exp. Ther., 292, 331 (2000). (Pharmacol.)5) M. Fantin, C. Fischetti, C. Trapella, and M. Morari, Br. J. Pharmacol., 152, 549 (2007). (Pharmacol.)

NPW30 (Human) See Code 4403 Neuropeptide W-30 (Human) on page 109
NPW30 (Rat) See Code 4404 Neuropeptide W-30 (Rat) on page 109– 112 –

Obestatins4429-sObestatin (Human)
Phe-Asn-Ala-Pro-Phe-Asp-Val-Gly-Ile-LysLeu-Ser-Gly-Val-Gln-Tyr-Gln-Gln-His-SerGln-Ala-Leu-NH2-20

(M.W. 2546.8)

Price:Yen
Vial

0.1 mg

8,000

Vial

0.1 mg

8,000

C116H176N32O33

Food Intake Suppressor
4430-s-20

Obestatin (Rat, Mouse)
Phe-Asn-Ala-Pro-Phe-Asp-Val-Gly-Ile-LysLeu-Ser-Gly-Ala-Gln-Tyr-Gln-Gln-His-GlyArg-Ala-Leu-NH2(M.W. 2516.8)

C114H174N34O31

Food Intake Suppressor

Multifunctional peptide, ghrelin (code 4372-s and 4373-s), was discovered by Kojima et al. in 1999, and its
precursor sequence was also clarified in the same report1). A group at Stanford University School of Medicine
found a novel peptide named "obestatin" in the preproghrelin sequence by using a bioinformatic prediction
method they developed to analyze preproghrelin2). This group also identified peptides such as stresscopin /stresscopin-related peptide (Code 4387-s and 4388-s) and intermedin (also called adrenomedullin 2, Code4421-s and 4422-s) by using the same method.

Ghrelin Precursor (Human)

Ghrelin
MPSPGTVCSL LLLGMLWLDL AMAGSSFLSP EHQRVQQRKE SKKPPAKLQP RALAGWLRPE
DGGQAEGAED ELEVRFNAPF DVGIKLSGVQ YQQHSQALGK FLQDILWEEA KEAPADKObestatin (precursor)
Obestatin was predicted to be a 23-residue peptide with carboxyl-terminal amide functionality, which isflanked by mono basic residues in the preproghrelin sequence in the form of a Gly-extended structure.
Endogenous obestatin was then isolated from rat stomach extracts, by which their prediction was confirmed tobe correct. Obestatin is conserved in the preproghrelin sequences of 11 different mammalian species,
including human.
Synthetic obestatin is reported to suppress food intake in mice which is very interesting because this effect is
opposed to that of ghrelin. It is also reported that obestatin exerts the opposite effects to the role of ghrelin in thegastric emptying activity as well as the contractile activity in the jejunum. Thus, in contrast to ghrelin, obestatin
may be an anorexic peptide leading to body weight loss.
1) M. Kojima, H. Hosoda, Y. Date, M. Nakazato, H. Matsuo, and K. Kangawa, Nature, 402, 656 (1999). (Original;
Preproghrelin)
2) J.V. Zhang, P.-G. Ren, O. Avsian-Kretchmer, C.-W. Luo, R. Rauch, C. Klein, and A.J.W. Hsueh, Science, 310, 996(2005). (Original; Structure & Pharmacol.)3) S.-Q. Tang, Q.-Y. Jiang, Y.-L. Zhang, X.-T. Zhu, G. Shu, P. Gao, D.-Y. Feng, X.-Q. Wang, and X.-Y. Dong,
Peptides, 29, 639 (2008). (Review)4) J.-B. Soares and A.F. Leite-Moreira, Peptides, 29, 1255 (2008). (Review)5) A.-J. Ren, Z.-F. Guo, Y.-K. Wang, L. Lin, X. Zheng, and W.-J. Yuan, Peptides, 30, 439 (2009). (Review)– 113 –and Proteins

CompoundBiologically Active Peptides

CodeOpioid Peptides
List of Opioid Peptides
Code
CompoundMethionine-Enkephalin Containing Peptides
4042-v
Methionine-Enkephalin★
4116-v[D-Ala2,Met5]-Enkephalin★
[D-Ala2,Met5]-Enkephalinamide
4117-v
4119-v
BAM-12P
4055-vα-Endorphin
β-Endorphin (Human)
4060-v
4089-vγ-Endorphin
Leucine-Enkephalin Containing Peptides
4043-v
Leucine-Enkephalin★
Leucine-Enkephalin (Sulfated Form)
4118-v
4115-v[D-Ala2,D-Leu5]-Enkephalin★
4090-v
α-Neo-Endorphin (Porcine)
β-Neo-Endorphin (Porcine)4091-v
4080-v
Dynorphin A (Human, 1-13)
4108-v
Dynorphin A (Human)
Others4079-vβ-Casomorphin-5 (Bovine)★
4078-vβ-Casomorphin-7 (Bovine)
4333-v
Endomorphin-1★
Endomorphin-2★
4334-v
4318-v
Nociceptin (Human)★

Quantity

Price: Yen

Page

0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial

2,100
2,400
2,400
6,600
9,500
17,00011,500

63
64
64
24
58
58
58

0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial

2,100
4,600
2,400
6,600
6,600
6,600
12,500

63
63
64
100
100
56
56

0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial

2,100
2,700
2,100
2,100
15,000

33
34
57
58
111

Other bulk packaging is available.

Orexins
1) T. Sakurai, Regul. Pept., 85, 25 (1999). (Review)2) J.M. Siegel, Cell, 98, 409 (1999). (Review)3) L. De Lecea and J.G. Sutcliffe, Cell. Mol. Life Sci., 56, 473 (1999). (Review)4) R.J. Rodgers, Y. Ishii, J.C.G. Halford, and J.E. Blundell, Neuropeptides, 36, 303 (2002). (Review)5) N. Tsujino and T. Sakurai, Pharmacol. Rev., 61, 162 (2009). (Review)6) M. Mieda and T. Sakurai, CNS Neurol. Disord. Drug Targets, 8, 281 (2009). (Review)7) B.C. Baccari, Curr. Protein Pept. Sci., 11, 148 (2010). (Review)

Code

Compound4346-sOrexin-A (Human)(Rat, Mouse, Bovine)
Pyr-Pro-Leu-Pro-Asp-Cys-Cys-Arg-Gln-LysThr-Cys-Ser-Cys-Arg-Leu-Tyr-Glu-Leu-LeuHis-Gly-Ala-Gly-Asn-His-Ala-Ala-Gly-IleLeu-Thr-Leu-NH2-20

Price:Yen
Vial

0.1 mg20,000(Disulfide bonds between Cys6-Cys12 and Cys7-Cys14)(M.W. 3561.1)

C152H243N47O44S4[205640-90-0]

Appetite-Boosting Peptide / Sleep-Wakefulness State Regulator
1) T. Sakurai, A. Amemiya, M. Ishii, I. Matsuzaki, R.M. Chemelli, H. Tanaka, S.C. Williams, J.A. Richardson,
G.P. Kozlowski, S. Wilson, J.R.S. Arch, R.E. Buckingham, A.C. Haynes, S.A. Carr, R.S. Annan, D.E. McNulty, W.-S.
Liu, J.A. Terrett, N.A. Elshourbagy, D.J. Bergsma, and M. Yanagisawa, Cell, 92, 573 (1998). (Original)
2) L. de Lecea, T.S. Kilduff, C. Peyron, X.-B. Gao, P.E. Foye, P.E. Danielson, C. Fukuhara, E.L.F. Battenberg,
V.T. Gautvik, F.S. Bartlett II, W.N. Frankel, A.N. van den Pol, F.E. Bloom, K.M. Gautvik, and J.G. Sutcliffe,
Proc. Natl. Acad. Sci. U.S.A., 95, 322 (1998). (cDNA; Same Sequence [Hypocretin])3) N. Takahashi, T. Okumura, H. Yamada, and Y. Kohgo, Biochem. Biophys. Res. Commun., 254, 623 (1999).
(Pharmacol.)4) T. Ida, K. Nakahara, T. Murakami, R. Hanada, M. Nakazato, and N. Murakami, Biochem. Biophys. Res. Commun.,
270, 318 (2000). (Pharmacol.)– 114 –

Orexins (continued)
4348-sOrexin-B (Human)
Arg-Ser-Gly-Pro-Pro-Gly-Leu-Gln-Gly-ArgLeu-Gln-Arg-Leu-Leu-Gln-Ala-Ser-Gly-AsnHis-Ala-Ala-Gly-Ile-Leu-Thr-Met-NH2-20

(M.W. 2899.3)

Price:Yen

C123H212N44O35S

Vial

0.1 mg10,000[205640-91-1]

Appetite-Boosting Peptide / Sleep-Wakefulness State Regulator
1) T. Sakurai, A. Amemiya, M. Ishii, I. Matsuzaki, R.M. Chemelli, H. Tanaka, S.C. Williams, J.A. Richardson,
G.P. Kozlowski, S. Wilson, J.R.S. Arch, R.E. Buckingham, A.C. Haynes, S.A. Carr, R.S. Annan, D.E. McNulty,
W.-S. Liu, J.A. Terrett, N.A. Elshourbagy, D.J. Bergsma, and M. Yanagisawa, Cell, 92, 573 (1998). (Original)
2) L. de Lecea, T.S. Kilduff, C. Peyron, X.-B. Gao, P.E. Foye, P.E. Danielson, C. Fukuhara, E.L.F. Battenberg,
V.T. Gautvik, F.S. Bartlett II, W.N. Frankel, A.N. van den Pol, F.E. Bloom, K.M. Gautvik, and J.G. Sutcliffe,
Proc. Natl. Acad. Sci. U.S.A., 95, 322 (1998). (cDNA; Same Sequence [Hypocretin])3) N. Takahashi, T. Okumura, H. Yamada, and Y. Kohgo, Biochem. Biophys. Res. Commun., 254, 623 (1999).
(Pharmacol.)4347-s-20

Vial

Orexin-B (Rat, Mouse)
Hypocretin 2 (Rat, Mouse)
Arg-Pro-Gly-Pro-Pro-Gly-Leu-Gln-Gly-ArgLeu-Gln-Arg-Leu-Leu-Gln-Ala-Asn-Gly-AsnHis-Ala-Ala-Gly-Ile-Leu-Thr-Met-NH2

0.1 mg10,000(M.W. 2936.4) C126H215N45O34S [202801-92-1]
Purity Information: Q P See page IV (XVI)

Appetite-Boosting Peptide / Sleep-Wakefulness State Regulator
1) T. Sakurai, A. Amemiya, M. Ishii, I. Matsuzaki, R.M. Chemelli, H. Tanaka, S.C. Williams, J.A. Richardson,
G.P. Kozlowski, S. Wilson, J.R.S. Arch, R.E. Buckingham, A.C. Haynes, S.A. Carr, R.S. Annan, D.E. McNulty,
W.-S. Liu, J.A. Terrett, N.A. Elshourbagy, D.J. Bergsma, and M. Yanagisawa, Cell, 92, 573 (1998). (Original)
2) L. de Lecea, T.S. Kilduff, C. Peyron, X.-B. Gao, P.E. Foye, P.E. Danielson, C. Fukuhara, E.L.F. Battenberg,
V.T. Gautvik, F.S. Bartlett II, W.N. Frankel, A.N. van den Pol, F.E. Bloom, K.M. Gautvik, and J.G. Sutcliffe,
Proc. Natl. Acad. Sci. U.S.A., 95, 322 (1998). (cDNA; Same Sequence [Hypocretin])3) N. Takahashi, T. Okumura, H. Yamada, and Y. Kohgo, Biochem. Biophys. Res. Commun., 254, 623 (1999).
(Pharmacol.)4) M.S. Mondal, M. Nakazato, Y. Date, N. Murakami, M. Yanagisawa, and S. Matsukura, Biochem. Biophys. Res.
Commun., 256, 495 (1999). (Distribution)

Primary structures of human, rat and mouse Orexin-A and -B precursor
Orexin-A
Human

MNLPSTKVSW AAVTLLLLLL LLPPALLSSG AAAQPLPDCC RQKTCSCRLY ELLHGAGNHA60

Rat

MNLPSTKVPW AAVTLLLLLL L-PPALLSLG VDAQPLPDCC RQKTCSCRLY ELLHGAGNHA59

Mouse

MNFPSTKVPW AAVTLLLLLL L-PPALLSLG VDAQPLPDCC RQKTCSCRLY ELLHGAGNHA59

Human

AGILTLGKRR SGPPGLQGRL QRLLQASGNH AAGILTMGRR AGAEPAPRPC LGRRCSAPAA120

Rat

AGILTLGKRR PGPPGLQGRL QRLLQANGNH AAGILTMGRR AGAELEPYPC PGRRCPTATA119

Mouse

AGILTLGKRR PGPPGLQGRL QRLLQANGNH AAGILTMGRR AGAELEPHPC SGRGCPTVTT119Human

ASVAPGGQSG I131

Rat

TALAPRGGSR V130

Mouse

TALAPRGGSG V130

Orexin-B

Orphanin FQ (Human) See Code 4318 Nociceptin (Human) on page 111– 115 –and Proteins

CompoundBiologically Active Peptides

CodeOsteocalcins
Code

Compound4262-s17,21,24-20

Price:Yen
Vial

Gla-Osteocalcin (Human)
Osteocalcin (Human, Gla17,21,24)

0.1 mginquiry(Ammonium Form)

Tyr-Leu-Tyr-Gln-Trp-Leu-Gly-Ala-Pro-ValPro-Tyr-Pro-Asp-Pro-Leu-Gla-Pro-Arg-ArgGla-Val-Cys-Gla-Leu-Asn-Pro-Asp-Cys-AspGlu-Leu-Ala-Asp-His-Ile-Gly-Phe-Gln-GluAla-Tyr-Arg-Arg-Phe-Tyr-Gly-Pro-Val(Gla: L-γ-Carboxyglutamic acid)(Disulfide bond between Cys23-Cys29)(M.W. 5929.4) C269H381N67O82S2 [136461-80-8]
Purity Information : QX See page IV (XVI)

Bone Gla Protein
1) J.W. Poser, F.S. Esch, N.C. Ling, and P.A. Price, J. Biol. Chem., 255, 8685 (1980). (Original)
2) M. Nakao, Y. Nishiuchi, M. Nakata, T. Kimura, and S. Sakakibara, Pept. Res., 7, 171 (1994). (Chem. Synthesis)
3) P.V. Hauschka, J.B. Lian, D.E.C. Cole, and C.M. Gundberg, Physiol. Rev., 69, 990 (1989). (Review)

4261-s-20

Glu17,Gla21,24-Osteocalcin (Human)
Osteocalcin (Human, Glu17, Gla21,24)

Vial

0.1 mginquiry(Ammonium Form)

Tyr-Leu-Tyr-Gln-Trp-Leu-Gly-Ala-Pro-ValPro-Tyr-Pro-Asp-Pro-Leu-Glu-Pro-Arg-ArgGla-Val-Cys-Gla-Leu-Asn-Pro-Asp-Cys-AspGlu-Leu-Ala-Asp-His-Ile-Gly-Phe-Gln-GluAla-Tyr-Arg-Arg-Phe-Tyr-Gly-Pro-Val(Gla: L-γ-Carboxyglutamic acid)(Disulfide bond between Cys23-Cys29)(M.W. 5885.4)

C268H381N67O80S2
Purity Information : QX See page IV (XVI)

Bone Gla Protein
1) J.W. Poser, F.S. Esch, N.C. Ling, and P.A. Price, J. Biol. Chem., 255, 8685 (1980). (Original)
2) M. Nakao, Y. Nishiuchi, M. Nakata, T. Kimura, and S. Sakakibara, Pept. Res., 7, 171 (1994). (Chem. Synthesis)
3) P.V. Hauschka, J.B. Lian, D.E.C. Cole, and C.M. Gundberg, Physiol. Rev., 69, 990 (1989). (Review)– 116 –

Oxytocins
Springer-Verlag, Berlin, 1968. (Review)

Compound4084-v

Oxytocin*(Human, Porcine, Bovine, Rat, Ovine)
Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2-20

Price:Yen
Vial

0.5 mg3,800(Disulfide bond between Cys1-Cys6)(M.W. 1007.2)

C43H66N12O12S2[50-56-6]

1) V. Du Vigneaud, C. Ressler, and S. Trippett, J. Biol. Chem., 205, 949 (1953). (Original)
2) R.A. Boissonnas, St. Guttmann, P.-A. Jaquenoud, and J.-P. Waller, Helv. Chim. Acta, 38, 1491 (1955).
(Chem. Synthesis)3) M. Zaoral and J. Rudinger, Collection Czech. Chem. Commun., 20, 1183 (1955). (Chem. Synthesis)4) A. Light and V. Du Vigneaud, Proc. Soc. Exp. Biol. Med., 98, 692 (1958). (Original; Human)4025-v-20

[Asu1,6]-Oxytocin*
Deamino-Dicarba-Oxytocin

Vial

0.5 mg4,800

cyclo(Tyr-Ile-Gln-Asn-Asu)-Pro-Leu-Gly-NH2(Asu: L-α-Aminosuberic acid)(Cyclic form between Asu ω-carboxyl group and Tyr α-amino group)(M.W. 956.10)

C45H69N11O12[14317-68-1]

1) T. Yamanaka, S. Hase, S. Sakakibara, I.L. Schwartz, B.M. Dubois, and R. Walter, Mol. Pharmacol., 6, 474 (1970).
(Original)

PACAP See Pituitary Adenylate Cyclase Activating Polypeptides on page 125
PAMP (Human) See Code 4291 Proadrenomedullin N-terminal 20 Peptide (Human) on page 5
PAMP (Rat) See Code 4292 Proadrenomedullin N-terminal 20 Peptide (Rat) on page 5
PAMP-12 (Human) See Code 4339 Proadrenomedullin N-terminal 20 Peptide (Human, 9-20) on page 5

Pancreastatins
4214-v

Chromogranin A (Human, 286-301 Amide)-20

(Hydrochloride Form)

Vial

0.5 mg11,500Glu-Glu-Glu-Glu-Glu-Met-Ala-Val-Val-ProGln-Gly-Leu-Phe-Arg-Gly-NH2(M.W. 1819.0) C78H123N21O27S [133605-57-9]
Purity Information : QE See page IV (XVI)
1) D.S. Konecki, U.M. Benedum, H.H. Gerdes, and W.B. Huttner, J. Biol. Chem., 262, 17026 (1987). (Original; cDNA)

4186-v-20

[Pyr33]-Pancreastatin (Porcine, 33-49)
Pyr-Glu-Glu-Glu-Glu-Glu-Thr-Ala-Gly-AlaPro-Gln-Gly-Leu-Phe-Arg-Gly-NH2(M.W. 1829.9)

Vial

0.5 mg11,500

C77H116N22O30

1) K. Tatemoto, S. Efendic, V. Mutt, G. Makk, G.J. Feistner, and J.D. Barchas, Nature, 324, 476 (1986). (Original)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 117 –and Proteins

Code

Biologically Active Peptides

1) B. Berde (ed.), Neurohypophysial Hormones and Similar Polypeptides, Handbook of Experimental Pharmacology, Vol. 23,

Parathyroid Hormone (PTH) and Related Peptides
List of Parathyroid Hormone (PTH) and Related Peptides
Species
Human

Code

CompoundQuantity

Price: Yen

Page4134-v
4068-s4068-v
4324-v
4094-v
4106-v
4124-v
4169-v
4170-v
4129-v
4180-v
4181-v

PTH (1-84)
PTH (1-34)
PTH (1-34)
PTH (1-31 Amide)
PTH (1-44)
PTH (13-34)
PTH (39-68)
PTH (39-84)
PTH (69-84)[Nle8,18, Tyr34]-PTH (1-34)[Nle8,18, Tyr34]-PTH (1-34 Amide)[Nle8,18, Tyr34]-PTH (3-34 Amide)

20 µg vial
0.1 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial

20,0008,000
27,00030,00041,00022,00036,00041,00012,50037,00036,00036,000

below
below
below
119
119
119
119
120
120
120
120
121

4179-v
4185-v[Tyr34]-PTH (1-34 Amide)[Tyr34]-PTH (7-34 Amide)

0.5 mg vial
0.5 mg vial

36,00036,000121
121

BovineCode

Compound4134-vParathyroid Hormone (Human, 1-84)
PTH (Human, 1-84)
Ser-Val-Ser-Glu-Ile-Gln-Leu-Met-His-AsnLeu-Gly-Lys-His-Leu-Asn-Ser-Met-Glu-ArgVal-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-AspVal-His-Asn-Phe-Val-Ala-Leu-Gly-Ala-ProLeu-Ala-Pro-Arg-Asp-Ala-Gly-Ser-Gln-ArgPro-Arg-Lys-Lys-Glu-Asp-Asn-Val-Leu-ValGlu-Ser-His-Glu-Lys-Ser-Leu-Gly-Glu-AlaAsp-Lys-Ala-Asp-Val-Asn-Val-Leu-Thr-LysAla-Lys-Ser-Gln-20

(M.W. 9424.6)

Price:Yen

C408H674N126O126S2

Vial

20 µg

20,000[68893-82-3]

1) G.N. Hendy, H.M. Kronenberg, J.T. Potts, Jr., and A. Rich, Proc. Natl. Acad. Sci. U.S.A., 78, 7365 (1981).
(Original; cDNA Seq.)
2) T. Kimura, M. Takai, K. Yoshizawa, and S. Sakakibara, Biochem. Biophys. Res. Commun., 114, 493 (1983).
(Chem. Synthesis)
3) H. Takasu, H. Baba, N. Inomata, Y. Uchiyama, N. Kubota, K. Kumaki, A. Matsumoto, K. Nakajima, T. Kimura,
S. Sakakibara, T. Fujita, K. Chihara, and I. Nagai, Endocrinology, 137, 5537 (1996). (Pharmacol.)4068-s-20

Parathyroid Hormone (Human, 1-34)
PTH (Human, 1-34)
Ser-Val-Ser-Glu-Ile-Gln-Leu-Met-His-AsnLeu-Gly-Lys-His-Leu-Asn-Ser-Met-Glu-ArgVal-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-AspVal-His-Asn-Phe(M.W. 4117.7)

4068-v-20

C181H291N55O51S2

Vial

0.1 mg

8,000

Vial

0.5 mg27,000[52232-67-4]

Parathyroid Hormone (Human, 1-34)
PTH (Human, 1-34)

1) M. Takai, Y. Kurano, T. Kimura, and S. Sakakibara, Peptide Chemistry 1979, 187 (1980). (Chem. Synthesis)– 118 –

Parathyroid Hormone (PTH) and Related Peptides (continued)
4324-vParathyroid Hormone (Human, 1-31 Amide)
PTH (Human, 1-31 Amide)
Ser-Val-Ser-Glu-Ile-Gln-Leu-Met-His-AsnLeu-Gly-Lys-His-Leu-Asn-Ser-Met-Glu-ArgVal-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-AspVal-NH2-20

(M.W. 3718.3)

Price:Yen
Vial

0.5 mg30,000C162H270N50O46S2

Adenylate Cyclase- / Bone Growth-Stimulating Peptide
1) R.H. Rixon, J.F. Whitfield, L. Gagnon, R.J. Isaacs, S. Maclean, B. Chakravarthy, J.P. Durkin, W. Neugebauer, V. Ross,
W. Sung, and G.E. Willick, J. Bone Miner. Res., 9, 1179 (1994). (Original)
2) W. Neugebauer, J.-R. Barbier, W.L. Sung, J.F. Whitfield, and G.E. Willick, Biochemistry, 34 , 8835 (1995).
(Biochem.)
3) J.F. Whitfield and P. Morley, Trends Pharmacol. Sci., 16, 382 (1995). (Review)4) J.F. Whitfield, P. Morley, G.E. Willick, V. Ross, J.R. Barbier, R.J. Isaacs, and L. Ohannessian-Barry, Calcif. Tissue Int.,58, 81 (1996). (Pharmacol.)4094-v-20

Parathyroid Hormone (Human, 1-44)
PTH (Human, 1-44)
Ser-Val-Ser-Glu-Ile-Gln-Leu-Met-His-AsnLeu-Gly-Lys-His-Leu-Asn-Ser-Met-Glu-ArgVal-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-AspVal-His-Asn-Phe-Val-Ala-Leu-Gly-Ala-ProLeu-Ala-Pro-Arg

Vial

0.5 mg41,000(M.W. 5063.9) C225H366N68O61S2 [85568-24-7]
Purity Information : QX See page IV (XVI)
1) T. Kimura, M. Takai, Y. Masui, T. Morikawa, and S. Sakakibara, Biopolymers, 20, 1823 (1981). (Chem. Synthesis)

4106-v-20

Parathyroid Hormone (Human, 13-34)
PTH (Human, 13-34)
Lys-His-Leu-Asn-Ser-Met-Glu-Arg-Val-GluTrp-Leu-Arg-Lys-Lys-Leu-Gln-Asp-Val-HisAsn-Phe(M.W. 2808.2)

C125H199N39O33S

Vial

0.5 mg22,000[81306-64-1]

1) R. Nakamura, H. Sokabe, T. Kimura, and S. Sakakibara, Endocrinol. Jpn., 28, 547 (1981). (Pharmacol.; Hypotension)
2) K. Sakaguchi, M. Fukase, I. Kobayashi, T. Kimura, S. Sakakibara, S. Katsuragi, K. Morita, T. Noda, and T. Fujita,
J. Bone Miner. Res., 2, 83 (1987). (Pharmacol.)4124-v-20

Parathyroid Hormone (Human, 39-68)
PTH (Human, 39-68)

Vial

0.5 mg36,000(Hydrochloride Form)

Ala-Pro-Leu-Ala-Pro-Arg-Asp-Ala-Gly-SerGln-Arg-Pro-Arg-Lys-Lys-Glu-Asp-Asn-ValLeu-Val-Glu-Ser-His-Glu-Lys-Ser-Leu-Gly(M.W. 3285.6)

C139H234N46O46
Purity Information : QX See page IV (XVI)
1) P. D'Amour, F. Labelle, R. Wolde-Giorghis, and L. Hamel, J. Immunoass., 10, 191 (1989). (Radioimmunoassay)
2) T. Yamaguchi, M. Arao, and M. Fukase, Acta Endocrinol., 127, 267 (1992). (Biochem.; PTH Degradation)3) T. Yamaguchi, M. Fukase, H. Kido, T. Sugimoto, N. Katunuma, and K. Chihara, Life Sci., 54, 381 (1994).
(Biochem.; PTH Degradation)– 119 –and Proteins

CompoundBiologically Active Peptides

CodeParathyroid Hormone (PTH) and Related Peptides (continued)
Code

Compound4169-vParathyroid Hormone (Human, 39-84)
PTH (Human, 39-84)
Ala-Pro-Leu-Ala-Pro-Arg-Asp-Ala-Gly-SerGln-Arg-Pro-Arg-Lys-Lys-Glu-Asp-Asn-ValLeu-Val-Glu-Ser-His-Glu-Lys-Ser-Leu-GlyGlu-Ala-Asp-Lys-Ala-Asp-Val-Asn-Val-LeuThr-Lys-Ala-Lys-Ser-Gln-20

(M.W. 4984.5)

Price:Yen

C211H357N67O72

Vial

0.5 mg41,000[90880-43-6]

1) P. D'Amour, F. Labelle, R. Wolde-Giorghis, and L. Hamel, J. Immunoass., 10, 191 (1989).
(Biochem.; Presence in Circuration)2) T. Yamaguchi, M. Arao, and M. Fukase, Acta Endocrinol., 127, 267 (1992). (Biochem.; PTH Degradation)3) T. Yamaguchi, M. Fukase, H. Kido, T. Sugimoto, N. Katunuma, and K. Chihara, Life Sci., 54, 381 (1994).
(Biochem.; PTH Degradation)

4170-v-20

Parathyroid Hormone (Human, 69-84)
PTH (Human, 69-84)

Vial

0.5 mg12,500(Hydrochloride Form)

Glu-Ala-Asp-Lys-Ala-Asp-Val-Asn-Val-LeuThr-Lys-Ala-Lys-Ser-Gln(M.W. 1716.9)

C72H125N21O27
Purity Information : QE See page IV (XVI)
1) P. D'Amour, F. Labelle, R. Wolde-Giorghis, and L. Hamel, J. Immunoass., 10, 191 (1989). (Radioimmunoassay)2) H. Takasu, H. Baba, N. Inomata, Y. Uchiyama, N. Kubota, K. Kumaki, A. Matsumoto, K. Nakajima, T. Kimura,
S. Sakakibara, T. Fujita, K. Chihara, and I. Nagai, Endocrinology, 137, 5537 (1996). (Pharmacol.)4129-v-20

[Nle8,18, Tyr34]-Parathyroid Hormone (Human, 1-34)[Nle8,18, Tyr34]-PTH (Human, 1-34)
Ser-Val-Ser-Glu-Ile-Gln-Leu-Nle-His-AsnLeu-Gly-Lys-His-Leu-Asn-Ser-Nle-Glu-ArgVal-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-AspVal-His-Asn-Tyr

Vial

0.5 mg37,000(Nle: L-Norleucine)(M.W. 4097.6)

C183H295N55O52

1) T. Noda, S. Katsuragi, and S. Watanabe, The 41st Annual Meeting of Chemical Society of Japan, Osaka, April 1980,
Abstr. No.4S12. (Original)

4180-v-20

[Nle8,18, Tyr34]-Parathyroid Hormone (Human, 1-34 Amide)[Nle8,18, Tyr34]-PTH (Human, 1-34 Amide)
Ser-Val-Ser-Glu-Ile-Gln-Leu-Nle-His-AsnLeu-Gly-Lys-His-Leu-Asn-Ser-Nle-Glu-ArgVal-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-AspVal-His-Asn-Tyr-NH2

Vial

0.5 mg36,000(Nle: L-Norleucine)(M.W. 4096.7)

C183H296N56O51

1) M. Rosenblatt, D. Goltzman, H.T. Keutmann, G.W. Tregear, and J.T. Potts, Jr., J. Biol. Chem., 251, 159 (1976).
(Chem. Synthesis & Biological Activity)2) M.L. Thomas and L.R. Forte, Comp. Biochem. Physiol., 73A, 691 (1982). (Biological Activity)
3) I. Yamamoto, C. Shigeno, J.T. Potts, Jr., and G.V. Segre, Endocrinology, 122, 1208 (1988). (Radioimmunoassay)– 120 –

Parathyroid Hormone (PTH) and Related Peptides (continued)
4181-v[Nle8,18,Tyr34]-Parathyroid Hormone (Human, 3-34 Amide)[Nle8,18,Tyr34]-PTH (Human, 3-34 Amide)
Ser-Glu-Ile-Gln-Leu-Nle-His-Asn-Leu-GlyLys-His-Leu-Asn-Ser-Nle-Glu-Arg-Val-GluTrp-Leu-Arg-Lys-Lys-Leu-Gln-Asp-Val-HisAsn-Tyr-NH2-20

Price:Yen
Vial

0.5 mg36,000(Nle: L-Norleucine)(M.W. 3910.4)

C175H282N54O48

1) S.R. Goldring, J.E. Mahaffey, M. Rosenblatt, J.-M. Dayer, J.T. Potts, Jr., and S.M. Krane, J. Endocrinol. Metab.,48, 655 (1979). (Pharmacol.)2) T.C. Chen, M. Rosenblatt, and J.B. Puschett, Biochem. Biophys. Res. Commun., 94, 1227 (1980). (Pharmacol.)3) D.A. Gray, J.A. Parsons, J.T. Potts, Jr., M. Rosenblatt, and R.W. Stevenson, Br. J. Pharmacol., 76, 259 (1982).
(Pharmacol.)4179-v-20

[Tyr34]-Parathyroid Hormone (Bovine, 1-34 Amide)[Tyr34]-PTH (Bovine, 1-34 Amide)
Ala-Val-Ser-Glu-Ile-Gln-Phe-Met-His-AsnLeu-Gly-Lys-His-Leu-Ser-Ser-Met-Glu-ArgVal-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-AspVal-His-Asn-Tyr-NH2(M.W. 4123.7)

Vial

0.5 mg36,000Vial

0.5 mg36,000C183H289N55O50S21) M. Rosenblatt, Pathobiol. Annu., 11, 53 (1981). (Review)

4185-v-20

[Tyr34]-Parathyroid Hormone (Bovine, 7-34 Amide)[Tyr34]-PTH (Bovine, 7-34 Amide)
Phe-Met-His-Asn-Leu-Gly-Lys-His-Leu-SerSer-Met-Glu-Arg-Val-Glu-Trp-Leu-Arg-LysLys-Leu-Gln-Asp-Val-His-Asn-Tyr-NH2(M.W. 3496.0)

C156H244N48O40S2[86292-93-5]

PTH Antagonist
1) N. Horiuchi, M.F. Holick, J.T. Potts, Jr., and M. Rosenblatt, Science, 220, 1053 (1983). (Original)

Parathyroid Hormone Related Proteins (PTH-rP)
4205-v-20

PTH-rP (Human, 1-34 Amide)
Parathyroid Hormone Related Protein (Human, 1-34 Amide)(Rat, Mouse)
Ala-Val-Ser-Glu-His-Gln-Leu-Leu-His-AspLys-Gly-Lys-Ser-Ile-Gln-Asp-Leu-Arg-ArgArg-Phe-Phe-Leu-His-His-Leu-Ile-Ala-GluIle-His-Thr-Ala-NH2(M.W. 4016.6)

C180H288N58O47

Vial

0.5 mg31,000[112955-31-4]

1) L.J. Suva, G.A. Winslow, R.E.H. Wettenhall, R.G. Hammonds, J.M. Moseley, H. Diefenbach-Jagger, C.P. Rodda,
B.E. Kemp, H. Rodriguez, E.Y. Chen, P.J. Hudson, T.J. Martin, and W.I. Wood, Science, 237, 893 (1987).
(Original; cDNA)
2) N. Horiuchi, M.P. Caulfield, J.E. Fisher, M.E. Goldman, R.L. McKee, J.E. Reagan, J.J. Levy, R.F. Nutt, S.B. Rodan,
T.L. Schofield, T.L. Clemens, and M. Rosenblatt, Science, 238, 1566 (1987). (Pharmacol.; Synthetic PTH-rP Amide)
3) B.E. Kemp, J.M. Moseley, C.P. Rodda, P.R. Ebeling, R.E.H. Wettenhall, D. Stapleton, H. Diefenbach-Jagger, F. Ure,
V.P. Michelangeli, H.A. Simmons, L.G. Raisz, and T.J. Martin, Science, 238, 1568 (1987).
(Pharmacol.; Synthetic PTH-rP Amide)– 121 –and Proteins

CompoundBiologically Active Peptides

CodeParathyroid Hormone Related Proteins (PTH-rP) (continued)
Code

Compound4215-v

PTH-rP (Human, 7-34 Amide)
Parathyroid Hormone Related Protein (Human, 7-34 Amide)
Leu-Leu-His-Asp-Lys-Gly-Lys-Ser-Ile-GlnAsp-Leu-Arg-Arg-Arg-Phe-Phe-Leu-His-HisLeu-Ile-Ala-Glu-Ile-His-Thr-Ala-NH2-20

(M.W. 3364.9)

Price:Yen

C153H247N49O37

Vial

0.5 mg31,000[115695-30-2]

PTH-rP Antagonist
1) K. Nagasaki, K. Yamaguchi, Y. Miyake, C. Hayashi, S. Honda, K. Urakami, K. Miki, S. Kimura, T. Watanabe, and
K. Abe, Biochem. Biophys. Res. Commun., 158, 1036 (1989). (Original)
2) L.J. Suva, G.A. Winslow, R.E.H. Wettenhall, R.G. Hammonds, J.M. Moseley, H. Diefenbach-Jagger, C.P. Rodda,
B.E. Kemp, H. Rodriguez, E.Y. Chen, P.J. Hudson, T.J. Martin, and W.I. Wood, Science, 237, 893 (1987).
(Original; cDNA)

Peptide 234
4460-v

New

Peptide 234
Ac-D-Ala-Asn-Trp-Asn-Gly-Phe-Gly-D-Trp-Arg-Phe-NH2-20

(M.W. 1295.4)

Vial

0.5 mg7,200

C63H78N18O13

Synthetic Kisspeptin Antagonist
Reproduction is one of the major fields of research using GPR-54 agonist, kisspeptin/metastin (Code 4446-s
and 4447-s), and its shorter active fragment (Code 4389-v and 4453-v). Peptide 234, an antagonist of
kisspeptin/metastin in reproduction, was discovered from rigorous structure-activity relationship studies ofhuman Kisspeptin-10 (Human) / Metastin (Human, 45-52) (Code 4389-v), which is an amino acid substituted
analog of the parental peptide at positions 1, 5 and 81). Peptide 234 is a potent agonist in vitro and in vivo: i)inhibition of kisspeptin-10-stimulated inositol phosphate (IC50 = 7 nM)1), ii) blocking the kisspeptin-10 induced
gonadotropin-releasing hormone (GnRH) neuron firing1), iii) inhibition of kisspeptin-10 stimulated LH in intact
male rats1), iv) suppression of GnRH pulse and mean GnRH level (10 nM)1), and v) suppression of LH in
castrated male mice and ovariectomized 17β-estradiol-replaced rats as well as LH pulse in ovariectomized
ewes1),2). Central infusion of peptide 234 to pubertal females delayed vaginal opening and decreased uterine
and ovarian weights at the expected time of puberty, without affecting body weight. Likewise, chronic
intracerebroventricular administration of peptide 234 for 4 days prevented the preovulatory surges of LH andFSH3).
Peptide 234 should be a requisite tool to clarify the GPR-54-kisspeptin signaling in reproduction.
1) A.K. Roseweir, A.S. Kauffman, J.T. Smith, K.A. Guerriero, K. Morgan, J. Pielecka-Fortuna, R. Pineda, M.L. Gottsch, M.
Tena-Sempere, S.M. Moenter, E. Terasawa, I.J. Clarke, R.A. Steiner, and R.P. Millar, J. Neurosci., 29, 3920 (2009).
(Pharmacol.)2) X.-F. Li, J.S. Kinsey-Jones, Y. Cheng, A.M.I. Knox, Y. Lin, N.A. Petrou, A. Roseweir, S.L. Lightman, S.R. Milligan, R.P.
Millar, and K.T. O'Byrne, PLoS One., 4, e8334 (2009). (Pharmacol.)3) R. Pineda, D. Garcia-Galiano, A. Roseweir, M. Romero, M.A. Sanchez-Garrido, F. Ruiz-Pino, K. Morgan, L. Pinilla,
R.P. Millar, and M. Tena-Sempere, Endocrinology, 151, 722 (2010). (Pharmacol.)– 122 –

Peptide Histidine-Methionine (PHM)
4177-v

PHM-27 (Human)
Peptide Histidine-Methionine
His-Ala-Asp-Gly-Val-Phe-Thr-Ser-Asp-PheSer-Lys-Leu-Leu-Gly-Gln-Leu-Ser-Ala-LysLys-Tyr-Leu-Glu-Ser-Leu-Met-NH2-20

(M.W. 2985.4)

Price:Yen

C135H214N34O40S

Vial

0.5 mg33,000[87403-73-4]

1) N. Itoh, K. Obata, N. Yanaihara, and H. Okamoto, Nature, 304, 547 (1983). (Original)

Peptide T
4188-v-20

Peptide T
Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr(M.W. 857.86)

4188
-20

Vial

0.5 mg

3,000

Bulk

25 mg

53,000C35H55N9O16

Peptide T
Ala-Ser-Thr-Thr-Thr-Asn-Tyr-Thr • 4H2O
(M.W. 857.86 • 72.06)

C35H55N9O16 • 4H2O

1) C.B. Pert, J.M. Hill, M.R. Ruff, R.M. Berman, W.G. Robey, L.O. Arthur, F.W. Ruscetti, and W.L. Farrar,
Proc. Natl. Acad. Sci. U.S.A., 83, 9254 (1986). (Original)
2) M.R. Ruff, B.M. Martin, E.I. Ginns, W.L. Farrar, and C.B. Pert, FEBS Lett., 211, 17 (1987). (Pharmacol.)Peptide with Reversed Sequence of Amyloid β-Protein (Human, 1-40)
See Code 4413 Amyloid β-Protein (40-1) on page 14
Peptide with Reversed Sequence of Amyloid β-Protein (Human, 1-42)
See Code 4420 Amyloid β-Protein (42-1) on page 14– 123 –and Proteins

CompoundBiologically Active Peptides

CodePeptide YY
1) H. Ueno, H. Yamaguchi, M. Mizuta, and M. Nakazato, Regul. Pept., 145, 12 (2008). (Review)2) M.T. Neary and R.L. Batterham, Physiol. Behav., 97, 616 (2009). (Review)

Code

Compound4400-v

Peptide YY (Human, 3-36)
PYY (Human, 3-36)
Ile-Lys-Pro-Glu-Ala-Pro-Gly-Glu-Asp-AlaSer-Pro-Glu-Glu-Leu-Asn-Arg-Tyr-Tyr-AlaSer-Leu-Arg-His-Tyr-Leu-Asn-Leu-Val-ThrArg-Gln-Arg-Tyr-NH2-20

(M.W. 4049.5)

Price:Yen
Vial

0.5 mg39,000C180H279N53O54

Physiological Inhibitor for Food Intake / NPY Y2-Receptor Agonist
Food intake is regulated by many peptides and proteins, and the majority of orexigenic and anorectic effects
elicited by these factors are mediated through their action within the brain. However, the origin of these
peptidic factors is not necessarily in the brain. For example, the major producing organ of ghrelin [Code 4372-s(human) and Code 4373-s (rat)] is the stomach. Later, peptide YY (3-36) [PYY (3-36)] was designated as a newmember of this family of satiety peptides1).
PYY (3-36) is a gut-derived endogenous peptide2), which is secreted postprandially. When PYY (3-36) was
injected peripherally in rats in a dose of 0.3 µg per 100 g (body weight), its plasma concentration increased to
the normal postprandial range and food intake was significantly suppressed1). Direct central administration ofthis peptide into the arcuate nucleus also inhibited food consumption. PYY (3-36) is a well-known agonist for
NPY Y2 receptor (Y2R)3, 4). Although the Y2R was not thought to be significantly involved in NPY-induced foodintake, a report in 2002 clarified its importance in body weight regulation5). Interestingly, no feeding inhibition
by PYY (3-36) was detected in a Y2R-deficient mouse. Furthermore, the anorectic effect of PYY (3-36) was seen
in humans upon infusion (0.8 pmol per kg per min) for 90 min: food intake suppression by 33% was observedin the 24 h period★. The role of the vagal nerve in peripheral PYY (3-36) induced feeding reduction has beenreported6). The functions of PYY (3-36), especially through a Y2R-dependent mechanism, should shed light on
the ongoing question of body weight control.
★

Please note: All the peptides in this catalog including PYY (3-36) are not for human consumption.
1) R.L. Batterham, M.A. Cowley, C.J. Small, H. Herzog, M.A. Cohen, C.L. Dakin, A.M. Wren, A.E. Brynes, M.J. Low,
M.A. Ghatei, R.D. Cone, and S.R. Bloom, Nature, 418, 650 (2002). (Original; Inhibition of Food Intake)2) G.A. Eberlein, V.E. Eysselein, M. Schaeffer, P. Layer, D. Grandt, H. Goebell, W. Niebel, M. Davis, T.D. Lee, J.E.
Shively, and J.R. Reeve, Jr., Peptides, 10, 797 (1989). (Original; Endogenous Form)
3) D.A. Keire, P. Mannon, M. Kobayashi, J.H. Walsh, T.E. Solomon, and J.R. Reeve, Jr., Am. J. Physiol. Gastrointest.
Liver Physiol., 279, G126 (2000). (Original; Y2R Selectivity)
4) S. Chamorro, O. Della-Zuana, J.-L. Fauche｀re, M. Félétou, J.-P. Galizzi, and N. Levens, Int. J. Obes., 26, 281 (2002).
(Review; Y2R Selectivity)
5) A. Sainsbury, C. Schwarzer, M. Couzens, S. Fetissov, S. Furtinger, A. Jenkins, H.M. Cox, G. Sperk, T Ho
kfelt, and
H. Herzog, Proc. Natl. Acad. Sci. U.S.A., 99, 8938 (2002). (Pharmacol.; Food intake Regulation through Y2R)
6) S. Koda, Y. Date, N. Murakami, T. Shimbara, T. Hanada, K. Toshinai, A. Niijima, M. Furuya, N. Inomata, K. Osuye,
and M. Nakazato, Endocrinology, 146, 2369 (2005). (Physiol.; Role of Vagal Nerve)7) E.E. Ladenheim, Am. J. Physiol. Rgul. Integr. Comp. Physiol., 293, R37 (2007). (Review)8) D. Boey, A. Sainsbury, and H. Herzog, Peptides, 28, 390 (2007). (Review)– 124 –

Physalaemin
4030-v

Physalaemin*(Frog, Physalaemus fuscumaculatus)
Pyr-Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly-LeuMet-NH2-20

(M.W. 1265.4)

4030
-20

Price:Yen

C58H84N14O16S

0.5 mg

3,300

Bulk

25 mg

49,000[2507-24-6]

Physalaemin*(Frog, Physalaemus fuscumaculatus)
Pyr-Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly-LeuMet-NH2 • AcOH • 3H2O
(M.W. 1265.4 • 60.05 • 54.06)

Vial

C58H84N14O16S • CH3COOH • 3H2O

1) V. Erspamer, A. Anastasi, G. Bertaccini, and J.M. Cei, Experientia, 20, 489 (1964). (Original)
2) L. Bernardi, G. Bosisio, O. Goffredo, and R. de Castiglione, Experientia, 20, 490 (1964). (Chem. Synthesis)

Pituitary Adenylate Cyclase Activating Polypeptides (PACAP)
1) A. Arimura, Peptides, 28, 1617 (2007). (Review)2) J. Watanabe, T. Nakamachi, R. Matsuno, D. Hayashi, M. Nakamura, S. Kikuyama, S. Nakajo, and S. Shioda,
Peptides, 28, 1713 (2007). (Review)3) M. Nakata and T. Yada, Curr. Pharm. Des., 13, 1105 (2007). (Review)4) D. Vaudry, A. Falluel-Morel, S. Bourgault, M. Basille, D. Burel, O. Wurtz, A. Fournier, B.K. Chow, H. Hashimoto,
L. Galas, and H. Vaudry, Pharmacol. Rev., 61, 283 (2009). (Review)

4221-v-20

PACAP38 (Human)*
Vial
Pituitary Adenylate Cyclase Activating Polypeptide 38 (Human)(Ovine, Rat, Mouse)
His-Ser-Asp-Gly-Ile-Phe-Thr-Asp-Ser-TyrSer-Arg-Tyr-Arg-Lys-Gln-Met-Ala-Val-LysLys-Tyr-Leu-Ala-Ala-Val-Leu-Gly-Lys-ArgTyr-Lys-Gln-Arg-Val-Lys-Asn-Lys-NH2(M.W. 4534.3)

0.5 mg32,000C203H331N63O53S

1) A. Miyata, A. Arimura, R.R. Dahl, N. Minamino, A. Uehara, L. Jiang, M.D. Culler, and D.H. Coy, Biochem. Biophys.
Res. Commun., 164, 567 (1989). (Original)• This compound is distributed through Peptide Institute, Inc. under the license of Tulane University.

4231-v-20

PACAP27 (Human, 1-27 Amide)*Vial
0.5 mgPituitary Adenylate Cyclase Activating Polypeptide 27 (Human, 1-27 Amide)(Ovine, Rat, Mouse)
His-Ser-Asp-Gly-Ile-Phe-Thr-Asp-Ser-TyrSer-Arg-Tyr-Arg-Lys-Gln-Met-Ala-Val-LysLys-Tyr-Leu-Ala-Ala-Val-Leu-NH2(M.W. 3147.6)

C142H224N40O39S

22,000[127317-03-7]

1) A. Miyata, L. Jiang, R.R. Dahl, C. Kitada, K. Kubo, M. Fujino, N. Minamino, and A. Arimura, Biochem. Biophys.
Res. Commun., 170, 643 (1990). (Original)
2) C. Kimura, S. Ohkubo, K. Ogi, M. Hosoya, Y. Itoh, H. Onda, A. Miyata, L. Jiang, R.R. Dahl, H.H. Stibbs, A. Arimura,and M. Fujino, Biochem. Biophys. Res. Commun., 166, 81 (1990). (Original; Human & Ovine cDNA)3) K. Ogi, C. Kimura, H. Onda, A. Arimura, and M. Fujino, Biochem. Biophys. Res. Commun., 173, 1271 (1990).
(Original; Rat cDNA)4) K. Okazaki, Y. Itoh, K. Ogi, S. Ohkubo, and H. Onda, Peptides, 16, 1295 (1995). (Original; Mouse cDNA)• This compound is distributed through Peptide Institute, Inc. under the license of Tulane University.

*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 125 –and Proteins

CompoundBiologically Active Peptides

CodePituitary Adenylate Cyclase Activating Polypeptides (PACAP) (continued)
Code

Compound

4286-v

PACAP (Human, 6-38)
Vial
Pituitary Adenylate Cyclase Activating Polypeptide (Human, 6-38)(Ovine, Rat)
Phe-Thr-Asp-Ser-Tyr-Ser-Arg-Tyr-Arg-LysGln-Met-Ala-Val-Lys-Lys-Tyr-Leu-Ala-AlaVal-Leu-Gly-Lys-Arg-Tyr-Lys-Gln-Arg-ValLys-Asn-Lys-NH2-20

(M.W. 4024.7)

Price:Yen

C182H300N56O45S

0.5 mg32,000[143748-18-9]

PACAP Selective Antagonist
1) P. Robberecht, P. Gourlet, P. De Neef, M.C. Woussen-Colle, M.C. Vandermeers-Piret, A. Vandermeers, and
J. Christophe, Eur. J. Biochem., 207, 239 (1992). (Original)
2) A. Vandermeers, S. Vandenborre, X. Hou, P. De Neef, P. Robberecht, M-C. Vandermeers-Piret, and J. Christophe,
Eur. J. Biochem., 208, 815 (1992). (Pharmacol.)Platelet Factor-4 Related Peptide
4305-v-20

Platelet Factor-4 (Human, 58-70)
Pro-Leu-Tyr-Lys-Lys-Ile-Ile-Lys-Lys-LeuLeu-Glu-Ser(M.W. 1573.0)

C76H133N17O18

Vial

0.5 mg4,000[82989-21-7]

Angiogenesis Inhibitor
1) T.E. Maione, G.S. Gray, J. Petro, A.J. Hunt, A.L. Donner, S.I. Bauer, H.F. Carson, and R.J. Sharpe, Science,
247, 77 (1990). (Original)– 126 –Plectasin
4432-sPlectasin(Fungus, Pseudoplectania nigrella)
Gly-Phe-Gly-Cys-Asn-Gly-Pro-Trp-Asp-GluAsp-Asp-Met-Gln-Cys-His-Asn-His-Cys-LysSer-Ile-Lys-Gly-Tyr-Lys-Gly-Gly-Tyr-CysAla-Lys-Gly-Gly-Phe-Val-Cys-Lys-Cys-Tyr-20

Price:Yen
Vial

0.1 mg23,000(Disulfide bonds between Cys4-Cys30, Cys15-Cys37, and Cys19-Cys39)(M.W. 4401.9)

C189H267N53O56S7

Antimicrobial Peptide
Defensin peptides are essential members of host-defense antimicrobial peptides found in both vertebrates
and invertebrates. Many defensins of invertebrate, as well as higher plants, have been discovered as the Cysrich peptide having the disulfide arrangement of the cystine–stabilized α-β tertiary structures, which is adifferent characteristic structure from that of vertebrate peptides such as α- and β-defensins. A new member of
the CSH motif family of peptides, termed plectasin, was isolated from a fungus Pseudoplectania nigrella for the
first time1).
Plectasin kills several species of Gram-positive bacteria including clinical isolates of Stereptococcus
pneumoniae, whereas Gram-negative bacteria are resistant to it. The bactericidal activity of plectasin shows
slower kinetics, suggesting that an alternative mechanism should be considered to explain its activity. In two
mouse models in vivo, plectasin (10 mg/kg) exerts anti-infective activity against S. pneumoniae as effective as
vancomycin in the peritoneal infection model and as effective as penicillin in the pneumonia model.
Considering plectasin has neither cytotoxicity nor hemolytic activity to mammalian cells, this peptide may be anovel antimicrobial peptide useful for studying the host-defense mechanism against invaders. Recently, an
inoffensive antibiotic effect of plectasin has reported. Plectasin showed no cytotoxicity to A549 cells, normal
epithelial cells, or lung fibroblasts, and it did not induce IL-8 production2).
1) P.H. Mygind, R.L. Fischer, K.M. Schnorr, M.T. Hansen, C.P. So
nksen, S. Ludvigsen, D. Raventós, S. Buskov, B.
Christensen, L. De Maria, O. Taboureau, D. Yaver, S.G. Elvig-Jrgensen, M.V. Srensen, B.E. Christensen, S.
Kjaerulff, N. Frimodt-Moller, R.I. Lehrer, M. Zasloff, and H.-H. Kristensen, Nature, 437, 975 (2005).
(Original; Structure & Antimicrobial Activity)
2) S. Hara, H. Mukae, N. Sakamoto, H. Ishimoto, M. Amenomori, H. Fujita, Y. Ishimatsu, K. Yanagihara, S. Kohno,
Biochem. Biophys. Res. Commun., 374, 709 (2008). (Pharmacol.)3) K. Mandal, B.L. Pentelute, V. Tereshko, V. Thammavongsa, O. Schneewind, A.A. Kossiakoff, and S.B.H. Kent,
Protein Sci., 18, 1146 (2009). (X-ray Structure)4) T. Schneider, T. Kruse, R. Wimmer, I. Wiedemann, V. Sass, U. Pag, A. Jansen, A.K. Nielsen, P.H. Mygind,
D.S. Raventos, S. Neve, B. Ravn, A.M. Bonvin, L. De Maria, A.S. Andersen, L.K. Gammelgaard, H.G. Sahl,
and H.H. Kristensen, Science, 328, 1168 (2010). (Pharmacol.)– 127 –and Proteins

CompoundBiologically Active Peptides

CodePleiotrophin
Code

Compound4335-v

Pleiotrophin (Human)
PTN (Human)
Gly-Lys-Lys-Glu-Lys-Pro-Glu-Lys-Lys-ValLys-Lys-Ser-Asp-Cys-Gly-Glu-Trp-Gln-TrpSer-Val-Cys-Val-Pro-Thr-Ser-Gly-Asp-CysGly-Leu-Gly-Thr-Arg-Glu-Gly-Thr-Arg-ThrGly-Ala-Glu-Cys-Lys-Gln-Thr-Met-Lys-ThrGln-Arg-Cys-Lys-Ile-Pro-Cys-Asn-Trp-LysLys-Gln-Phe-Gly-Ala-Glu-Cys-Lys-Tyr-GlnPhe-Gln-Ala-Trp-Gly-Glu-Cys-Asp-Leu-AsnThr-Ala-Leu-Lys-Thr-Arg-Thr-Gly-Ser-LeuLys-Arg-Ala-Leu-His-Asn-Ala-Glu-Cys-GlnLys-Thr-Val-Thr-Ile-Ser-Lys-Pro-Cys-GlyLys-Leu-Thr-Lys-Pro-Lys-Pro-Gln-Ala-GluSer-Lys-Lys-Lys-Lys-Lys-Glu-Gly-Lys-LysGln-Glu-Lys-Met-Leu-Asp-20

Price:Yen
Vial

50 µg

30,000(Disulfide bonds between Cys15-Cys44, Cys23-Cys53, Cys30-Cys57, Cys67-Cys99, and Cys77-Cys109)(M.W. 15302.6)

C658H1079N197O198S12

Heparin-Binding Growth Factor (Neurite Outgrowth-Promoting Factor)
1) Y.-S. Li, P.G. Milner, A.K. Chauhan, M.A. Watson, R.M. Hoffman, C.M. Kodner, J. Milbrandt, and T.F. Deuel,
Science, 250, 1690 (1990). (Primary Structure)2) P.G. Milner, D. Shah, R. Veile, H. Donis-Keller, and B.V. Kumar, Biochemistry, 31, 12023 (1992).
(Nucleotide Seq.; Human)
3) F. Czubayko, A.M. Schulte, G.J. Berchem, and A. Wellstein, Proc. Natl. Acad. Sci. U.S.A., 93, 14753 (1996).
(Pharmacol.)4) T. Inui, M. Nakao, H. Nishio, Y. Nishiuchi, S. Kojima, T. Muramatsu, T. Kimura, and S. Sakakibara, J. Pept. Res.,55, 384 (2000). (Chem. Synthesis & S-S Bond)

PLTX-II
4300-s-20

PLTX-II(Spider, Plectreurys tristes)
Ala-Asp-Cys-Ser-Ala-Thr-Gly-Asp-Thr-CysAsp-His-Thr-Lys-Lys-Cys-Cys-Asp-Asp-CysTyr-Thr-Cys-Arg-Cys-Gly-Thr-Pro-Trp-GlyAla-Asn-Cys-Arg-Cys-Asp-Tyr-Tyr-Lys-AlaArg-Cys-Asp-Thr(Palmitoyl)-NH2

Vial

0.1 mg30,000(Disulfide bonds undetermined)(M.W. 5108.7)

C208H313N61O70S10

Presynaptic Ca2+ Channel Blocker
1) W.D. Branton, L. Kolton, Y.N. Jan, and L.Y. Jan, J. Neurosci., 7, 4195 (1987). (Original)
2) H.-T. Leung, W.D. Branton, H.S. Phillips, L. Jan, and L. Byerly, Neuron, 3, 767 (1989). (Pharmacol.)3) W.D. Branton, M.S. Rudnick, Y. Zhou, E.D. Eccleston, G.B. Fields, and L.D. Bowers, Nature, 365, 496 (1993).
(Thr (Palmitoyl) Amide Structure)4) J. Bódi, H. Nishio, Y. Zhou, W.D. Branton, T. Kimura, and S. Sakakibara, Pept. Res., 8, 228 (1995).
(Chem. Synthesis & Biological Activity)5) G.F. King, Toxicon, 49, 513 (2007). (Review)

Prepro-hBD-4 (Human, 25-61) See Code 4406 β-Defensin-4 (Human) on page 53
Prepro-LEAP-2 (Human, 38-77) See Code 4405 LEAP-2 (Human) on page 90
Proadrenomedullin N-terminal 20 Peptide See Code 4291 PAMP (Human), Code 4292 PAMP (Rat), andCode 4339 PAMP-12 (Human) on page 5
Proangiotensin-12 (Rat) See Code 4439 on page 18– 128 –

Prolactin-Releasing Peptides

Compound4352-v

Prolactin-Releasing Peptide (Human)
PrRP31 (Human)
Ser-Arg-Thr-His-Arg-His-Ser-Met-Glu-IleArg-Thr-Pro-Asp-Ile-Asn-Pro-Ala-Trp-TyrAla-Ser-Arg-Gly-Ile-Arg-Pro-Val-Gly-ArgPhe-NH2-20

(M.W. 3664.1)

Price:Yen
Vial

0.5 mg25,000C160H252N56O42S

Multifunctional Peptide in Neuroendocrinology
1) S. Hinuma, Y. Habata, R. Fujii, Y. Kawamata, M. Hosoya, S. Fukusumi, C. Kitada, Y. Masuo, T. Asano,
H. Matsumoto, M. Sekiguchi, T. Kurokawa, O. Nishimura, H. Onda, and M. Fujino, Nature, 393, 272 (1998).
(Original; cDNA)2) F. Satoh, D.M. Smith, J.V. Gardiner, M. Mahmoodi, K.G. Murphy, M.A. Ghatei, and S.R. Bloom, Br. J. Pharmacol.,129, 1787 (2000). (Pharmacol.)• This compound is distributed through Peptide Institute, Inc. under the license of Takeda Pharmaceutical Company
Limited.

4353-v-20

Prolactin-Releasing Peptide (Rat)
PrRP31 (Rat)
Ser-Arg-Ala-His-Gln-His-Ser-Met-Glu-ThrArg-Thr-Pro-Asp-Ile-Asn-Pro-Ala-Trp-TyrThr-Gly-Arg-Gly-Ile-Arg-Pro-Val-Gly-ArgPhe-NH2(M.W. 3594.0)Vial

0.5 mg25,000C156H242N54O43S

Multifunctional Peptide in Neuroendocrinology
1) S. Hinuma, Y. Habata, R. Fujii, Y. Kawamata, M. Hosoya, S. Fukusumi, C. Kitada, Y. Masuo, T. Asano,
H. Matsumoto, M. Sekiguchi, T. Kurokawa, O. Nishimura, H. Onda, and M. Fujino, Nature, 393, 272 (1998).
(Original; cDNA)2) M. Maruyama, H. Matsumoto, K. Fujiwara, J. Noguchi, C. Kitada, S. Hinuma, H. Onda, O. Nishimura, M. Fujino,
T. Higuchi, and K. Inoue, Neurosci. Lett., 276, 193 (1999). (Pharmacol.)3) F. Satoh, D.M. Smith, J.V. Gardiner, M. Mahmoodi, K.G. Murphy, M.A. Ghatei, and S.R. Bloom, Br. J. Pharmacol.,129, 1787 (2000). (Pharmacol.)4) H. Matsumoto, M. Maruyama, J. Noguchi, Y. Horikoshi, K. Fujiwara, C. Kitada, S. Hinuma, H. Onda, O. Nishimura,
K. Inoue, and M. Fujino, Neurosci. Lett., 285, 234 (2000). (Pharmacol.)• This compound is distributed through Peptide Institute, Inc. under the license of Takeda Pharmaceutical Company
Limited.

PTN (Human) See Code 4335 Pleiotrophin (Human) on page 128 and 153– 129 –and Proteins

Code

Biologically Active Peptides

1) B. Sun, K. Fujiwara, S. Adachi, and K. Inoue, Regul. Pept., 126, 27 (2005). (Review)2) S. Fukusumi, R. Fujii, and S. Hinuma, Peptides, 27, 1073 (2006). (Review)3) D.A. Bechtold and S.M. Luckman, J. Endocrinol., 192, 3 (2007). (Review)

ProTx-I
Code

Compound4409-s

ProTx-I(Tarantula, Thrixopelma pruriens)
Glu-Cys-Arg-Tyr-Trp-Leu-Gly-Gly-Cys-SerAla-Gly-Gln-Thr-Cys-Cys-Lys-His-Leu-ValCys-Ser-Arg-Arg-His-Gly-Trp-Cys-Val-TrpAsp-Gly-Thr-Phe-Ser-20

Price:Yen
Vial

0.1 mg22,000(Disulfide bonds between Cys2-Cys16, Cys9-Cys21, and Cys15-Cys28)(M.W. 3987.5)

C171H245N53O47S6
Purity Information: QE See page IV (XVI)

T-Type Ca2+ Channel / Na+ Channel / K+ Channel Blocker (Gating Modifier)
ProTx-I was isolated from the venom of the tarantula Thrixopelma pruriens and its primary structure wasdetermined to consist of 35 amino acid residues with three intrachain disulfide bonds1). This peptide belongs toa member of the "inhibitor cystine knot motif" peptide family. We determined three disulfide linkages in thesynthetic peptide as shown above in the sequence (The experimental procedure remains to be published).
Like other venomous toxins, ProTx-I exerts inhibitory activities for each ion channels: i) T-type Ca2+ channel[Cav3.1 (α1G), IC50 = 53 nM], ii) Na+ channel [Nav1.2, Nav1.5, Nav1.7 (IC50 = 51 nM), and Nav1.8 (IC50 = 27nM)], and iii) K+ channel [Kv2.1 (IC50 = 411 nM) and Kv1.3 (40% blocking at 730 nM)]. ProTx-I thus elicits
multiple channel blocking activities with certain selectivity since K+ channel inhibitory activity is relatively
weak. ProTx-I is one of the first high-affinity ligands to be identified that possess tetrodotoxin-resistant Na+ andT-type Ca2+ channel blocking activity. This peptide should prove useful for elucidating the gating mechanism ofvoltage-dependent ion channels.
1) R.E. Middleton, V.A. Warren, R.L. Kraus, J.C. Hwang, C.J. Liu, G. Dai, R.M. Brochu, M.G. Kohler, Y.-D. Gao, V.M.
Garsky, M.J. Bogusky, J.T. Mehl, C.J. Cohen, and M.M. Smith, Biochemistry, 41, 14734 (2002). (Original)
2) T. Ohkubo, J. Yamazaki, and K. Kitamura, J. Pharmacol. Sci., 112, 452 (2010). (Pharmacol.)3) B.T. Priest, K.M. Blumenthal, J.J. Smith, V.A. Warren, and M.M. Smith, Toxicon, 49, 194 (2007). (Review)– 130 –

ProTx-II
4450-s

ProTx-II(Tarantula, Thrixopelma pruriens)
Tyr-Cys-Gln-Lys-Trp-Met-Trp-Thr-Cys-AspSer-Glu-Arg-Lys-Cys-Cys-Glu-Gly-Met-ValCys-Arg-Leu-Trp-Cys-Lys-Lys-Lys-Leu-Trp

New

-20

Price:Yen
Vial

0.1 mg20,000(Disulfide bonds between Cys2-Cys16, Cys9-Cys21, and Cys15-Cys25)(M.W. 3826.6)

C168H250N46O41S8+Na Channel (Especially Nav1.7) / Ca2+ Channel Blocker (Gating Modifier)
ProTx-II, as well as ProTx-I (Code 4409-s), were isolated from the venom of Thrixopelma pruriens1). Bothpeptides contain three disulfide linkages in the inhibitor cystine-knot arrangement, although their primarystructures are variable except for the conserved Cys residues; ProTx-II is composed of 30 amino acid residues,
which is shorter than that of ProTx-I (35 amino acid residues).
Voltage-gated sodium channels play a critical role in modulating the excitability of most neurons, including
nociceptive sensory neurons signaling pain. ProTx-II was first reported to block Na + (including
tetrodotoxin-resistant Nav1.8) and Ca2+ channels in the similar specificity as ProTx-I; however, in contrast to
ProTx-I, ProTx-II does not block K+ channels (Kv1.2 / Kv1.3 / Kv1.5 / Kv2.1) at dose of 460 nM1). Later the
research using ProTx-II was mainly devoted to elucidating the Nav channel subtype-specificity: i) with the
mutagenesis in both ProTx-II and Nav1.5, it is clarified that ProTx-II interacting site of Nav1.5 is not theneurotoxin site 42), and ii) ProTx-II is a selective blocker of Nav1.7 (IC50 = 0.3 nM) because other Nav1channels (Nav1.2 - Nav1.6 and Nav1.8) were 100-fold less potent3). In the latter special case, phenylalanine
813 in Nav1.7 channel is identified as the interacting site with ProTx-II, thus indicating the novel mechanism of
ProTx-II for the Nav1 channel blocking activity. Binding of 125I-ProTx-II is insensitive to the presence of otherwell characterized Nav1 channel modulators, suggesting that ProTx-II binds to a novel site, which may be more
conducive to conferring subtype selectivity than the site occupied by traditional local anesthetics andanticonvulsants. Gain-of-function mutations in the Nav1.7 channel lead to dorsal root ganglia neuron
hyperexcitability associated with severe pain, whereas loss of the Nav1.7 channel in patients leads to
indifference to pain4).
The specificity of Na+ channel blocking activity of ProTx-II together with ProTx-I are reviewed recently5).
ProTx-II could be an attractive target for pain research due to its reported features of Na+ channel blocking
specificity.
1) R.E. Middleton, V.A. Warren, R.L. Kraus, J.C. Hwang, C.J. Liu, G. Dai, R.M. Brochu, M.G. Kohler, Y.-D. Gao,
V.M. Garsky, M.J. Bogusky, J.T. Mehl, C.J. Cohen, and M.M. Smith, Biochemistry, 41, 14734 (2002). (Original)
2) J.J. Smith, T.R. Cummins, S. Alphy, and K.M. Blumenthal, J. Biol. Chem., 282, 12687 (2007).
(Pharmacol.; Novel Toxin Binding Site Coupled to Nav Activation)3) W.A. Schmalhofer, J. Calhoun, R. Burrows, T. Bailey, M.G. Kohler, A.B. Weinglass, G.J. Kaczorowski, M.L. Garcia,
M. Koltzenburg, and B.T. Priest, Mol. Pharmacol, 74, 1476 (2008). (Pharmacol.; Inhibition of Nav1.7 Channels)4) S.D. Dib-Hajj, T.R. Cummins, J.A. Black, and S.G. Waxman, Trends Neurosci., 30, 555 (2007). (Review)5) B.T. Priest, K.M. Blumenthal, J.J. Smith, V.A. Warren, and M.M. Smith, Toxicon, 49, 194 (2007). (Review)6) S. Sokolov, R.L. Kraus, T. Scheuer, and W.A. Catterall, Mol. Pharmacol., 73, 1020 (2008). (Pharmacol.)– 131 –and Proteins

CompoundBiologically Active Peptides

CodePsalmotoxin
Code

Compound4435-sPsalmotoxin 1
PcTX1(South American Tarantula, Psalmopoeus cambridgei)-20

Price:Yen
Vial

0.1 mg23,000(Trifluoroacetate Form)

Glu-Asp-Cys-Ile-Pro-Lys-Trp-Lys-Gly-CysVal-Asn-Arg-His-Gly-Asp-Cys-Cys-Glu-GlyLeu-Glu-Cys-Trp-Lys-Arg-Arg-Arg-Ser-PheGlu-Val-Cys-Val-Pro-Lys-Thr-Pro-Lys-Thr(Disulfide bonds between Cys3-Cys18, Cys10-Cys23, and Cys17-Cys33)(M.W. 4689.4)

C200H312N62O57S6
Purity Information: QE See page IV (XVI)

Selective Blocker for Acid-Sensitive Ion Channel, ASIC1a
The acid-sensing ion channels (ASICs) are members of the epithelial Na + channel (EnaC)/degenerin
superfamily, which are expressed both in central and peripheral nervous systems. The ASICs are functionallyinvolved in nociception, learning, or mechanosensation. Because ASICs are composed of several subunits inboth homo- and hetero-multimeric assembly, specific blockers for each subtype are required for the precise
analysis of the functional role of each ASIC.
Psalmotoxin 1, isolated from the venom of the tarantula, Psalmopoeus cambridgei, is a 40 amino acidresidue peptide with three intramolecular disulfide bonds1). Three-dimensional solution structure analysis by
NMR revealed that this peptide is a member of inhibitor cystine knot toxins2). Among the ASICs, psalmotoxin 1
blocks the ASIC1a homomultimer selectively (IC50 = 0.9 nM)1), although this peptide binds to ASIC1b in achannel state-dependent manner and promotes its opening3). Psalmotoxin 1 increases the apparent affinity for
H+, by which the ASIC1a channel inhibition may occur4). Following activities of psalmotoxin 1 have beenreported: i) inhibition of Na+ currents (both inward and outward) in malignant glioma cells (IC50 = 36 pM)5) andii) protection of the brain from ischemic injury (100 ng/ml)6).
Psalmotoxin 1 should be useful tool to study the role in the ASIC1a-tiggered responses in the body.
1) P. Escoubas, J.R. De Weille, A. Lecoq, S. Diochot, R. Waldmann, G. Champigny, D. Moinier, A. Ménez, and M.
Lazdunski, J. Biol. Chem., 275, 25116 (2000). (Original; Primary Structure & ASIC Blocking Selectivity)
2) P. Escoubas, C. Bernard, G. Lambeau, M. Lazdunski, and H. Darbon, Protein Sci., 12, 1332 (2003).
(Three-dimensional Solution Structure)3) X. Chen, H. Kalbacher, and S. Gru
nder, J. Gen. Physiol., 127, 267 (2006). (Pharmacol.; State-Dependent Function)4) X. Chen, H. Kalbacher, and S. Gru
nder, J. Gen. Physiol., 126, 71 (2005). (Pharmacol.; Mechanism of Channel
Inhibition)5) J.K. Bubien, H.-L. Ji, G. Yancey Gillespie, C.M. Fuller, J.M. Markert, T.B. Mapstone, and D.J. Benos, Am. J. Physiol.
Cell Physiol., 287, C1282 (2004). (Pharmacol.; Inhibition of Malignant Glioma Na+ Channels)
6) Z.-G. Xiong, X.-M. Zhu, X.-P. Chu, M. Minami, J. Hey, W.-L. Wei, J.F. MacDonald, J.A. Wemmie, M.P. Price, M.J.
Welsh, and R.P. Simon, Cell, 118, 687 (2004). (Pharmacol.; Neuroprotection in Ischemia)7) S. Diochot, M. Salinas, A. Baron, P. Escoubas, and M. Lazdunski, Toxicon, 49, 271 (2007). (Review)8) Y.J. Qadri, B.K. Berdiev, Y. Song, H.L. Lippton, C.M. Fuller, and D.J. Benos, J. Biol. Chem., 284, 17625 (2009).
(Pharmacol.)– 132 –

Purotoxin
4457-sPurotoxin-1(Wolf Spider, Geolycosa sp.)
Gly-Tyr-Cys-Ala-Glu-Lys-Gly-Ile-Arg-CysAsp-Asp-Ile-His-Cys-Cys-Thr-Gly-Leu-LysCys-Lys-Cys-Asn-Ala-Ser-Gly-Tyr-Asn-CysVal-Cys-Arg-Lys-Lys

New

-20

Price:Yen
Vial

0.1 mg22,000(Reported disulfide bonds between Cys3-Cys16, Cys10-Cys21, Cys15-Cys32, and Cys23-Cys30)(M.W. 3836.5)

C155H248N50O48S8

Inhibitor of P2X3 Purinoreceptors
Lots of mechanisms for pain signaling are proposed. Recently, the specific Na+ channels targeted bypeptidic toxins, such as µ-conotoxin SIIIA (Code 4440-v) and ProTx-II (Code 4450-s), are receiving muchattention. P2X3 purinoreceptors are another component participating in pain signaling, which are activated by
ATP and other nucleotides. Very recently, P2X3 inhibitory peptide named purotoxin-1 has been isolated fromthe wolf spider Geolycosa sp.: a 35-residue peptide with 4 disulfide bonds, three of which are connected in theinhibitor cystine knot arrangement1). Inhibitory potency of desensitized P2X3 receptors is reported to be as highas 12 nM and specificity to P2X3 receptors is high because this peptide does not block other voltage- andligand-gated channels including vanilloid TRPV1 receptors. A low dose of 0.5 nM of this peptide reduced
capsaicin-induced nociception in rat.
Purotoxin-1 may contribute to the development of novel antinociceptive drugs.
1) E.V. Grishin, G.A. Savchenko, A.A. Vassilevski, Y.V. Korolkova, Y.A. Boychuk, V.Y. Viatchenko-Karpinski,
K.D. Nadezhdin, A.S. Arseniev, K.A. Pluzhnikov, V.B. Kulyk, N.V. Voitenko, and O.O. Krishtal, Ann. Neurol.,67, 680 (2010). (Original; Structure & Pharmacol.)– 133 –and Proteins

CompoundBiologically Active Peptides

CodePyroglutamylated RFamide Peptide
Code

Compound4419-sPyroglutamylated RFamide Peptide (Human)
QRFP (Human)
Pyr-Asp-Glu-Gly-Ser-Glu-Ala-Thr-Gly-PheLeu-Pro-Ala-Ala-Gly-Glu-Lys-Thr-Ser-GlyPro-Leu-Gly-Asn-Leu-Ala-Glu-Glu-Leu-AsnGly-Tyr-Ser-Arg-Lys-Lys-Gly-Gly-Phe-SerPhe-Arg-Phe-NH2-20

(M.W. 4503.8)

Price:Yen
Vial

0.1 mg13,000C199H301N55O65

Endogenous Ligand for AQ27 / SP9155 / GPR103
The group of Takeda Pharmaceutical Company Limited has long been involved in discovering orphan
receptor ligands and identified a novel peptide in human utilizing the recently established gene database.
Actually, they searched the database to detect peptides with the carboxyl-terminal Arg-Phe-NH2 (RFamide)
moiety in the mature peptide. As a result, the peptide termed pyroglutamylated RFamide peptide (QRFP) was
identified by analyzing the expressed peptide in Chinese hamster ovary cells as a 43 amino acid residue
peptide1). The peptide corresponding to the carboxyl-terminal 26 amino acid residues of QRFP was also
predicted by another group using a similar approach and then termed P5182). Both of these peptides were
found to interact with an orphan receptor (AQ27/SP9155/GPR103; all of these denote the same orphan receptor
of interest). Human 26RFa was proposed by another group based on the primary structure of their determinedfrog peptide in which 26RFa is identical to P5183).
The biological activities of QRFP and 26RFa reported are: i) upon intravenous administration in rats at doses
between 40 and 400 nmol/kg, QRFP induced aldosterone secretion in a dose-dependent manner,ii) intracerebroventricular administration of 26RFa in mice (after partial food deprivation for 18 h) stimulated
food intake at doses of 100 and 1000 ng/mouse, iii) central QRFP (rat QRFP is used in this report)
administration evoked feeding, behavioral arousal, and elevation of blood pressure in mice 4) , andiv) intracerebroventricular infusion of QRFP increased fat mass and decreased rectal temperature in mice5).
QRFP might have variable activities other than those identified, thus, it should serve as an essential memberof the RFamide family peptides in humans.
1) S. Fukusumi, H. Yoshida, R. Fujii, M. Maruyama, H. Komatsu, Y. Habata, Y. Shintani, S. Hinuma, and M. Fujino,
J. Biol. Chem., 278, 46387 (2003). (Original: QRFP)
2) Y. Jiang, L. Luo, E.L. Gustafson, D. Yadav, M. Laverty, N. Murgolo, G. Vassileva, M. Zeng, T.M. Laz, J. Behan, P. Qiu,
L. Wang, S. Wang, M. Bayne, J. Greene, F. Monsma, Jr., and F.L. Zhang, J. Biol. Chem., 278, 27652 (2003). (Orphan
Receptor Ligand / 26-Residue Peptide, P518)
3) N. Chartrel, C. Dujardin, Y. Anouar, J. Leprince, A. Decker, S. Clerens, J.-C. Do-Régo, F. Vandesande,
C. Llorens-Cortes, J. Costentin, J.-C. Beauvillain, and H. Vaudry, Proc. Natl. Acad. Sci. U.S.A., 100, 15247 (2003).
(26-Residue Peptide, 26RFa)
4) S. Takayasu, T. Sakurai, S. Iwasaki, H. Teranishi, A. Yamanaka, S.C. Williams, H. Iguchi, Y.I. Kawasawa, Y. Ikeda, I.
Sakakibara, K. Ohno, R.X. Ioka, S. Murakami, N. Dohmae, J. Xie, T. Suda, T. Motoike, T. Ohuchi, M. Yanagisawa,
and J. Sakai, Proc. Natl. Acad, Sci. U.S.A., 103, 7438 (2006). (Pharmacol.)5) R. Moriya, H. Sano, T. Umeda, M. Ito, Y. Takahashi, M. Matsuda, A. Ishihara, A. Kanatani, and H. Iwaasa,
Endocrinology, 147, 2916 (2006). (Pharmacol.)6) S. Fukusumi, R. Fujii, and S. Hinuma, Peptides, 27, 1073 (2006). (Review)7) D.A. Bechtold and S.M. Luckman, J. Endocrinol., 192, 3 (2007). (Review)

Pyr-Lys-Arg-Pro-Ser-Gln-Arg-Ser-Lys-Tyr-Leu See Code 4237 on page 223
QRFP (Human) See Code 4419 Pyroglutamylated RFamide Peptide (Human) above
Renin Substrate See Code 3229 Nma-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys(Dnp)-D-Arg-D-Arg-NH2
on page 222, Code 3110 Suc-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-MCA on page 226 andCode 4133 Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His on page 209– 134 –

RFamide-Related Peptides
4380-sRFamide-Related Peptide-1 (Human)
RFRP-1 (Human)
Ser-Leu-Asn-Phe-Glu-Glu-Leu-Lys-Asp-TrpGly-Pro-Lys-Asn-Val-Ile-Lys-Met-Ser-ThrPro-Ala-Val-Asn-Lys-Met-Pro-His-Ser-PheAla-Asn-Leu-Pro-Leu-Arg-Phe-NH2-20

(M.W. 4256.9)

Price:Yen
Vial

0.1 mg12,000C195H304N52O51S2

Endogenous Ligand for OT7T022 / FF1Among peptides with the carboxyl (C)-terminal Arg-Phe-NH2 (RFamide family of peptides), FMRF-Amide(Code 4142-v) was first isolated from Mollusks in 19771). Another member of this family, Leu-Pro-Leu-Arg-PheNH2 (Code 4144), was identified in chicken brain in 1983, yet there had not been any reports of corresponding
mammalian peptides with the same five C-terminal residues. A related peptide was deduced from a humangenome database search by elucidating its endogenous form through application of peptide / DNA chemistry.
The name of the target peptide is RFamide-related peptide-1 (RFRP-1).
Human RFRP-1 was first predicted to be a 12 amino acid residue peptide. Subsequent synthesis andbiochemical studies found it to be a ligand for the orphan receptor, OT7T022 (also called FF1)2). Later, theendogenous form of human RFRP-1 was determined to be composed of 37 amino acid residues including theabove 12 residue peptide at its C-terminus3). The same peptide was isolated by another group who named it
NPSF(1-37) 4). Human RFRP-1 inhibits forskolin-stimulated cAMP production in CHO cells expressing
OT7T022 (ED50=21 nM). The potency is slightly less than that of the 12 residue peptide (ED50=4.9 nM),
however, this result suggests that the C-terminal portion of RFRP-1 is responsible for the recognition of
OT7T022. Immunoreactive RFRP-1 was observed in the central nervous system (CNS), with the highest amountdetected in the hypothalamus5). Specific receptors of RFRP-1, OT7T022 or FF1, were found in the CNS. It isinteresting to note that the synthetic peptide composed of 12 amino acid residues described above showed
prolactin-releasing activity at 10 nM2) and that rat NPSF(1-37) had the anti-opioid effect in two models of
nociception at 1.0 nmol/rat4). Thus, RFRP-1 should serve as an important biochemical tool to further research
investigations. Later, it was reported that intrathecal administration of RFRP-1 induced tactile antiallodynia andthermal antinociception in rat6).
1) D.A. Price and M.J. Greenberg, Science, 197, 670 (1977). (Original; FMRF-Amide)2) S. Hinuma, Y. Shintani, S. Fukusumi, N. Iijima, Y. Matsumoto, M. Hosoya, R. Fujii, T. Watanabe, K. Kikuchi,
Y. Terao, T. Yano, T. Yamamoto, Y. Kawamata, Y. Habata, M. Asada, C. Kitada, T. Kurokawa, H. Onda,
O. Nishimura, M. Tanaka, Y. Ibata, and M. Fujino, Nat. Cell Biol., 2, 703 (2000).
(Original; cDNA & Pharmacol.)3) S. Fukusumi, Y. Habata, H. Yoshida, N. Iijima, Y. Kawamata, M. Hosoya, R. Fujii, S. Hinuma, C. Kitada, Y. Shintani,
M. Suenaga, H. Onda, O. Nishimura, M. Tanaka, Y. Ibata, and M. Fujino, Biochim. Biophys. Acta, 1540, 221 (2001).
(Endogenous Form)
4) Q. Liu, X.-M. Guan, W.J. Martin, T.P. McDonald, M.K. Clements, Q. Jiang, Z. Zeng, M. Jacobson, D.L. Williams, Jr.,
H. Yu, D. Bomford, D. Figueroa, J. Mallee, R. Wang, J. Evans, R. Gould, and C.P. Austin, J. Biol. Chem.,
276, 36961 (2001). (Original; NPSF)
5) T. Yano, N. Iijima, K. Kakihara, S. Hinuma, M. Tanaka, and Y. Ibata, Brain Res., 982, 156 (2003). (Histochem.)
6) A. Pertovaara, M. 
Ostergård, M.-L. 
Anko, S. Lehti-Koivunen, A. Brandt,b W. Hong, E.R. Korpi, and P. Panula,
Neuroscience, 134, 1023 (2005). (Pharmacol.)7) S. Fukusumi, R. Fujii, and S. Hinuma, Peptides, 27, 1073 (2006). (Review)8) D.A. Bechtold and S.M. Luckman, J. Endocrinol., 192, 3 (2007). (Review)• This compound is distributed through Peptide Institute, Inc. under the license of Takeda Pharmaceutical Company
Limited.

– 135 –and Proteins

CompoundBiologically Active Peptides

CodeRFamide-Related Peptides (continued)
Code

Compound4461-v

RFamide-Related Peptide-3 (Human)
RFRP-3 (Human)(Ovine)Val-Pro-Asn-Leu-Pro-Gln-Arg-Phe-NH2

New

-20

(M.W. 969.14)

Price:Yen
Vial

0.5 mg

6,000

Vial

0.5 mg8,000

C45H72N14O10

Gonadotropin-Inhibitory Hormone
4462-v

New-20

RFamide-Related Peptide-3 (Rat)
RFRP-3 (Rat)
Ala-Asn-Met-Glu-Ala-Gly-Thr-Met-Ser-HisPhe-Pro-Ser-Leu-Pro-Gln-Arg-Phe-NH2(M.W. 2020.3)

C88H134N26O25S2

Gonadotropin-Inhibitory Hormone
RFamide-Related Peptide-3 (RFRP-3) was discovered from the cDNA sequences, in which two other family
peptides, RFRP-1 (Code 4380-s for one of the endogenous forms) and RFRP-2 are encoded1),2). Endogenous
forms of human and rat RFRP-3 were determined to be an 8- and 18-residue peptide, respectively3),4).
Biological activities of RFRP-3 include: i) function as gonadotropin inhibitory hormone (GnIH), resulting in the
reduction in LH secretion; ii) increase in food intake and growth hormone secretion; and iii) no effect on Kiss-1
mRNA expression5),6). RFRP-3 should be especially valuable research tools in reproduction and puberty
studies.
1) S. Hinuma, Y. Shintani, S. Fukusumi, N. Iijima, Y. Matsumoto, M. Hosoya, R. Fujii, T. Watanabe, K. Kikuchi,
Y. Terao, T. Yano, T. Yamamoto, Y. Kawamata, Y. Habata, M. Asada, C. Kitada, T. Kurokawa, H. Onda,
O. Nishimura, M. Tanaka, Y. Ibata, and M. Fujino, Nat.Cell Biol., 2, 703 (2000). (Original: Human & Rat cDNA)2) I.J. Clarke, I.P. Sari, Y. Qi, J.T. Smith, H.C. Parkington, T. Ubuka, J. Iqbal, Q. Li, A. Tilbrook, k. Morgan, A.J. Pawson,
K. Tsutsui, R.P. Millar, and G.E. Bentley, Endocrinology, 149, 5811 (2008). (Original: Ovine cDNA)
3) T. Ubuka, K. Morgan, A.J. Pawson, T. Osugi, V. S. Chowdhury, H. Minakata, K. Tsutsui, R.P. Millar,
and G.E. Bentley, PLoS One., 4, e8400 (2009). (Endogenous Form: Human RFRP-3)
4) K. Ukena, E. Iwakoshi, H. Minakata, and K. Tsutsui, FEBS Lett., 512, 255 (2002). (Endogenous Form: Rat RFRP-3)5) I.J. Clarke, Y. Qi, I.P. Sari, and J.T. Smith., Front.Neuroendocrinol., 30, 371 (2009). (Review: Pharmacol.)6) M.A. Johnson and G.S. Fraley, Neuroendocrinology, 88, 305 (2008). (Pharmacol.)– 136 –

Salusins
4417-sSalusin-α (Human)
Ser-Gly-Ala-Leu-Pro-Pro-Ala-Pro-Ala-AlaPro-Arg-Pro-Ala-Leu-Arg-Ala-Gln-Arg-AlaGly-Pro-Ala-Gly-Pro-Gly-Ala-Lys-NH2-20

(M.W. 2603.0)

Price:Yen
Vial

0.1 mg12,000Vial

0.1 mg

9,000

C114H192N40O30

Hypotensive / Mitogenic Peptide
4418-s-20

Salusin-β (Human)
Ala-Ile-Phe-Ile-Phe-Ile-Arg-Trp-Leu-LeuLys-Leu-Gly-His-His-Gly-Arg-Ala-Pro-Pro(M.W. 2342.8)

C115H176N32O21

Hypotensive / Mitogenic Peptide
Biologically active peptides have long been isolated from natural sources using the chromatographic
separation and purification methods to identify new endogenous ligands. Advancements in genomic research
led to strategies of discovering novel peptides, notably using bioinformatical DNA sequence analysis
techniques. Late in 2003, two peptides termed salusin-α and salusin-β were discovered using this technique;that is, the selection of putative secretory prepropeptides, which possess the structural features of processing
signals resulting in mature peptides with less than 40 amino acid residues1). Salusin-α was predicted to be a 28residue peptide with an amidated carboxyl-terminus, while salusin-β was predicted to be a 20-residue peptide
with a free carboxyl-terminus. These two peptides were encoded in the order of salusin-β and salusin-α from asingle mRNA transcribed from TOR2A.
Preprosalusin: AWD • • • • • • • • • • • • • RK-[salusin-β]-RR-[salusin-α]G** carboxyl-terminal Gly in the above sequence is the precursor of the amide structure.

salusin-α: SGALPPAPAAPRPALRAQRAGPAGPGAK-NH2
salusin-β: AIFIFIRWLLKLGHHGRAPP

Chemically synthesized salusin-α and salusin-β exerted the following biological activities1): i) mitogenic
effects in rat vascular smooth muscle cells and fibroblasts, probably through mutually distinct receptors,ii) dose-dependent hypotensive activity in rats (1-10 nmol/kg for salusin-α and 0.1-1 nmol/kg for salusin-β ), andiii) [Arg8 ]-vasopressin releasing activity in perfused rat pituitaries (exclusive activity of salusin-β in adose-dependent manner [0.01-100 nM]). Immunohistochemical experiments showed that both of these
peptides are present in numerous tissues, including kidney as the major source. Following interestingobservations were reported further: i) salusin-β induced hypotension and bradycardia were completely blockedby pretreatment with atropine, but not by propranolol2), ii) salusin-α and salusin-β did not directly affectcardiac function in the rat heart, but promote cardiomyocyte growth3), and iii) salusin-β activated the mouse
mas-like G protein-coupled receptor, mMrgA1, with an EC50 of about 300 nM4).
1) M. Shichiri, S. Ishimaru, T. Ota, T. Nishikawa, T. Isogai, and Y. Hirata, Nat. Med., 9, 1166 (2003). (Original)
2) H. Izumiyama, H. Tanaka, K. Egi, M. Sunamori, Y. Hirata, and M. Shichiri, Hypertension, 45, 419 (2005).
(Pharmacol.)3) F. Yu, J. Zhao, J. Yang, B. Gen, S. Wang, X. Feng, C. Tang, and L. Chang, Regul. Pept., 122, 191 (2004). (Pharmacol.)4) Z. Wang, T. Takahashi, Y. Saito, H. Nagasaki, N. K. Ly, H.-P. Nothacker, R.K. Reinscheid, J. Yang, J. K. Chang, M.
Shichiri, and O. Civelli, Eur. J. Pharmacol. 539, 145 (2006). (Pharmacol.)5) K. Sato, T. Koyama, T. Tateno, Y. Hirata, and M. Shichiri, Peptides, 27, 2561 (2006). (Radioimmunoassay)6) T. Watanabe, K. Nishio, T. Kanome, T. Matsuyama, S. Koba, T. Sakai, K. Sato, S. Hongo, K. Nose, H. Ota,
Y. Kobayashi, T. Katagiri, M. Shichiri, and A. Miyazaki, Circulation, 117, 638 (2008). (Pharmacol.)7) J.S. Shi, D. Li, N. Li, L. Lin, Y.J. Yang, Y. Tang, T. Sun, W.J. Yuan, and A.J. Ren, Peptides, 31, (2010) (Pharmacol.)– 137 –and Proteins

CompoundBiologically Active Peptides

CodeSarafotoxins
1) E. Kochva, A. Bdolah, and Z. Wollberg, Toxicon, 31, 541 (1993). (Review)2) F. Ducancel, Toxicon, 40, 1541 (2002). (Review)3) F. Ducancel, Cell. Mol. Life Sci., 62, 2828 (2005). (Review)

Code

Compound4206-sSarafotoxin S6b*
(Snake, Atractaspis engaddensis)
Cys-Ser-Cys-Lys-Asp-Met-Thr-Asp-Lys-GluCys-Leu-Tyr-Phe-Cys-His-Gln-Asp-Val-IleTrp-20

Price:Yen
Vial

0.1 mg15,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 2563.9)

C110H159N27O34S5[120972-53-4]

Endothelin Related Peptide
1) C. Takasaki, N. Tamiya, A. Bdolah, Z. Wollberg, and E. Kochva, Toxicon, 26, 543 (1988).
(Original; Chem. Structure)2) Y. Kloog, I. Ambar, M. Sokolovsky, E. Kochva, Z. Wollberg, and A. Bdolah, Science, 242, 268 (1988).
(Original; Biochem.)
3) K. Nakajima, S. Kumagaye, H. Nishio, H. Kuroda, T.X. Watanabe, Y. Kobayashi, H. Tamaoki, T. Kimura, and
S. Sakakibara, J. Cardiovasc. Pharmacol., 13 (Suppl. 5), S8 (1989). (Chem. Synthesis & Biological Activity)
4) T.X. Watanabe, Y. Itahara, K. Nakajima, S. Kumagaye, T. Kimura, and S. Sakakibara, J. Cardiovasc. Pharmacol.,17 (Suppl. 7), S5 (1991). (Pharmacol.)4246-s-20

Sarafotoxin S6c*
(Snake, Atractaspis engaddensis)
Cys-Thr-Cys-Asn-Asp-Met-Thr-Asp-Glu-GluCys-Leu-Asn-Phe-Cys-His-Gln-Asp-Val-IleTrp

Vial

0.1 mg15,000(Disulfide bonds between Cys1-Cys15 and Cys3-Cys11)(M.W. 2515.8)

C103H147N27O37S5[121695-87-2]

Selective ETB Receptor Agonist
1) C. Takasaki, N. Tamiya, A. Bdolah, Z. Wollberg, and E. Kochva, Toxicon, 26, 543 (1988).
(Original; Chem. Structure)2) W.G. Nayler, X.H. Gu, and D.J. Casley, Biochem. Biophys. Res. Commun., 161, 89 (1989). (Pharmacol.)3) D.L. Williams, Jr., K.L. Jones, D.J. Pettibone, E.V. Lis, and B.V. Clineschmidt, Biochem. Biophys. Res. Commun.,
175, 556 (1991). (Pharmacol.)Schizophrenia Related Peptide
4061
-20

Bulk

Schizophrenia Related Peptide
Thr-Val-Leu(M.W. 331.41)

25 mg
100 mg

C15H29N3O51) C.E. Frohman, Chem. Eng. News, 1977, 35. (Original)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 138 –

8,300
17,000Scyllatoxin
4260-sScyllatoxin
Leiurotoxin I(Scorpion, Leiurus quinquestriatus hebraeus)
Ala-Phe-Cys-Asn-Leu-Arg-Met-Cys-Gln-LeuSer-Cys-Arg-Ser-Leu-Gly-Leu-Leu-Gly-LysCys-Ile-Gly-Asp-Lys-Cys-Glu-Cys-Val-LysHis-NH2-20

Price:Yen
Vial

0.1 mg20,000(Reported disulfide bonds between Cys3-Cys21, Cys8-Cys26, and Cys12-Cys28)(M.W. 3423.1)

C142H237N45O39S7[142948-19-4]

2+

Small Conductance Ca -Activated K + Channel Blocker
1) G.G. Chicchi, G. Gimenez-Gallego, E. Ber, M.L. Garcia, R. Winquist, and M.A. Cascieri, J. Biol. Chem.,
263, 10192 (1988). (Original)
2) P. Auguste, M. Hugues, C. Mourre, D. Moinier, A. Tartar, and M. Lazdunski, Biochemistry, 31, 648 (1992).
(Pharmacol.)3) J.C. Martins, F.J.M. Van de Ven, and F.A.M. Borremans, J. Mol. Biol., 253, 590 (1995). (S-S Bond)

Secretins
1) J.E. Jorpes and V. Mutt (eds.), Secretin, Cholecystokinin, Pancreozymin and Gastrin, Handbook of Experimental
Pharmacology, Vol.34, Springer-Verlag, Berlin, 1973. (Review)

4165-v-20

Secretin (Human)
His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-LeuSer-Arg-Leu-Arg-Glu-Gly-Ala-Arg-Leu-GlnArg-Leu-Leu-Gln-Gly-Leu-Val-NH2(M.W. 3039.4)

C130H220N44O40

Vial

0.5 mg29,000[108153-74-8]

1) M. Carlquist, H. Jo
rnvall, W.G. Forssmann, L. Thulin, C. Johansson, and V. Mutt, IRCS Med. Sci., 13, 217 (1985).
(Original)
2) K. Iguchi, T. Mochizuki, T. Inoue, C. Yanaihara, S. Naruse, K. Nokihara, W.G. Forssmann, V. Mutt, T. Kanno, andN. Yanaihara, Peptide Chemistry 1985, 191 (1986). (Chem. Synthesis & Biological Activity)

4112-v-20

Secretin (Porcine)
His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-LeuSer-Arg-Leu-Arg-Asp-Ser-Ala-Arg-Leu-GlnArg-Leu-Leu-Gln-Gly-Leu-Val-NH2(M.W. 3055.4)

C130H220N44O41

Vial

0.5 mg29,000Vial

0.5 mg

3,600

Bulk

25 mg

51,000[17034-35-4]

Ser-Gln-Asn-Tyr-Pro-Ile-Val See Code 4236 on page 224

Serum Thymic Factor
4058-v-20

Serum Thymic Factor
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn(M.W. 858.85)

4058
-20

C33H54N12O15[63958-90-7]

Serum Thymic Factor
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn • AcOH • 2H2O
(M.W. 858.85• 60.05 • 36.03)

C33H54N12O15 • CH3 COOH • 2H2O

1) J.F. Bach, M. Dardenne, J.M. Pleau, and J. Rosa, Nature, 266, 55 (1977). (Original)– 139 –and Proteins

CompoundBiologically Active Peptides

CodeSNX-482
CodeCompound4363-s

SNX-482(Tarantula, Hysterocrates gigas)
Gly-Val-Asp-Lys-Ala-Gly-Cys-Arg-Tyr-MetPhe-Gly-Gly-Cys-Ser-Val-Asn-Asp-Asp-CysCys-Pro-Arg-Leu-Gly-Cys-His-Ser-Leu-PheSer-Tyr-Cys-Ala-Trp-Asp-Leu-Thr-Phe-SerAsp-20

Price:Yen
Vial

0.1 mg30,000(Reported disulfide bonds between Cys7-Cys21, Cys14-Cys26, and Cys20-Cys33)(M.W. 4495.0)

C192H274N52O60S7[203460-30-4]Class E (R-type) Ca2+ Channel Blocker
1) R. Newcomb, B. Szoke, A. Palma, G. Wang, X.-h. Chen, W. Hopkins, R. Cong, J. Miller, L. Urge, K. Tarczy-Hornoch,
J.A. Loo, D.J. Dooley, L. Nadasdi, R. W. Tsien, J. Lemos, and G. Miljanich, Biochemistry, 37, 15353 (1998).
(Original)
2) L. Urge, B. Szoke, D. Silva, P. Tran-Tau, D. Hom, K. Tarczy-Hornoch, and L. Nádasdi, In, Peptides 1998,
Proceedings of 25th European Peptide Symposium (S. Bajusz and F. Hudecz, eds.), Akadémiai Kiadó Butapest, 1999,
pp.748-749. (S-S Bond)
3) A. Tottene, S. Volsen, and D. Pietrobon, J. Neurosci., 20, 171 (2000). (Pharmacol.)4) G. Wang, G. Dayanithi, R. Newcomb, and J. R. Lemos, J. Neurosci., 19, 9235 (1999). (Pharmacol.)5) D. Sochivko, A. Pereverzev, N. Smyth, C. Gissel, T. Schneider, and H. Beck, J. Physiol., 542, 699 (2002).
(Pharmacol.)6) X. Jing, D.-Q. Li, C.S. Olofsson, A. Salehi, V.V. Surve, J. Caballero, R. Ivarsson, I. Lundquist, A. Pereverzev,
T. Schneider, P. Rorsman, and E. Renstroem, J. Clin. Invest., 115, 146 (2005). (Pharmacol.)Sodium Potassium ATPase Inhibitor-1 (SPAI-1)
4216-s-20

SPAI-1 (Porcine)
Sodium Potassium ATPase Inhibitor-1 (Porcine)
Na+, K+-ATPase Inhibitor-1 (Porcine)
Leu-Leu-Ser-Lys-Arg-Gly-His-Cys-Pro-ArgIle-Leu-Phe-Arg-Cys-Pro-Leu-Ser-Asn-ProSer-Asn-Lys-Cys-Trp-Arg-Asp-Tyr-Asp-CysPro-Gly-Val-Lys-Lys-Cys-Cys-Glu-Gly-PheCys-Gly-Lys-Asp-Cys-Leu-Tyr-Pro-Lys

Vial

0.1 mg23,000(Disulfide bonds between Cys8-Cys37, Cys15-Cys41, Cys24-Cys36, and Cys30-Cys45)(M.W. 5628.6)

C245H378N72O65S81) K. Araki, J. Kuroki, O. Ito, M. Kuwada, and S. Tachibana, Biochem. Biophys. Res. Commun., 164, 496 (1989).
(Original)
2) K. Araki, M. Kuwada, O. Ito, J. Kuroki, and S. Tachibana, Biochem. Biophys. Res. Commun., 172, 42 (1990).
(S-S Bond)
3) H. Nishio, S. Kumagaye, H. Kuroda, N. Chino, J. Emura, T. Kimura, and S. Sakakibara, Pept. Res., 5, 227 (1992).
(Chem. Synthesis)– 140 –

Somatostatin (SRIF) and Related Peptides
4023-vSomatostatin
SRIF (Somatotropin Release Inhibiting Factor)
GIF (Growth Hormone Release Inhibiting Factor)(Human, Ovine, Porcine, Rat, Mouse)
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-ThrPhe-Thr-Ser-Cys-20

Price:Yen
Vial

0.5 mg

9,000

Bulk

25 mg

91,000(Disulfide bond between Cys3-Cys14)(M.W. 1637.9)

4023
-20

C76H104N18O19S2[38916-34-6]

Somatostatin
SRIF (Somatotropin Release Inhibiting Factor)
GIF (Growth Hormone Release Inhibiting Factor)(Human, Ovine, Porcine, Rat, Mouse)
Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-ThrPhe-Thr-Ser-Cys • 2AcOH • 6H2O
(Disulfide bond between Cys3-Cys14)(M.W. 1637.9 • 120.10 • 108.09)

C76H104N18O19S2 • 2CH3COOH • 6H2O

1) P. Brazeau, W. Vale, R. Burgus, N. Ling, M. Butcher, J. Rivier, and R. Guillemin, Science, 179, 77 (1973).
(Original; Ovine)
2) D.J. Koerker, W. Ruch, E. Chideckel, J. Palmer, C.J. Goodner, J. Ensinck, and C.C. Gale, Science, 184, 482 (1974).
(Pharmacol.)3) A. Arimura, H. Sato, A. Dupont, N. Nishi, and A.V. Schally, Science, 189, 1007 (1975). (Pharmacol.)4) L.-P. Shen, R.L. Pictet, and W.J. Rutter, Proc. Natl. Acad. Sci. U.S.A., 79, 4575 (1982). (cDNA Seq.; Human)

4101-v-20

[D-Trp8]-Somatostatin
Ala-Gly-Cys-Lys-Asn-Phe-Phe-D-Trp-Lys-ThrPhe-Thr-Ser-Cys

Vial

0.5 mg12,000(Disulfide bond between Cys3-Cys14)(M.W. 1637.9)

C76H104N18O19S2[58976-46-8]

1) J. Rivier, H. Brown, and W. Vale, Biochem. Biophys. Res. Commun., 65, 746 (1975). (Original)

4038-v-20

[Tyr1]-Somatostatin
Tyr-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-ThrPhe-Thr-Ser-Cys

Vial

0.5 mg11,000(Disulfide bond between Cys3-Cys14)(M.W. 1730.0)

C82H108N18O20S2[59481-23-1]

Purity Information : QX See page IV (XVI)For Radioimmunoassay
1) A. Arimura, H. Sato, D.H. Coy, and A.V. Schally, Proc. Soc. Exp. Biol. Med., 148, 784 (1975). (Original)

Spantide See Code 4173 [D-Arg1,D-Trp7,9,Leu11]-Substance P on page 145– 141 –and Proteins

CompoundBiologically Active Peptides

CodeStichodactyla Toxin
Code

Compound4287-sStichodactyla Toxin
ShK(Sea Anemone, Stichodactyla helianthus)
Arg-Ser-Cys-Ile-Asp-Thr-Ile-Pro-Lys-SerArg-Cys-Thr-Ala-Phe-Gln-Cys-Lys-His-SerMet-Lys-Tyr-Arg-Leu-Ser-Phe-Cys-Arg-LysThr-Cys-Gly-Thr-Cys-20

Price:Yen
Vial

0.1 mg22,000(Reported disulfide bonds between Cys3-Cys35, Cys12-Cys28, and Cys17-Cys32)(M.W. 4054.8)

C169H274N54O48S7

Voltage-Dependent K+ Channel (A Channel) Blocker
1) E. Karlsson, A.L. Harvey, A. Aneiros, and O. Castaneda,Toxicon, 31, 504 (1993). (Original; in Abstract)2) J.Pohl, F. Hubalek, M.E. Byrnes, K.R. Nielsen, A. Woods, and M.W. Pennington, Lett. Pept. Sci., 1, 291 (1994).
(S-S Bond)3) O. Castan
eda, V.Sotolongo, A.M. Amor, R. Stocklin, A.J. Anderson, A.L. Harvey, A. Engstro
m, C. Wernstedt, and
E. Karlsson, Toxicon, 33, 603 (1995). (Pharmacol.)Substance K See Code 4154 Neurokinin A on page 101

Stresscopin / Urocortin and Related Peptides
1) C.L. Chang and S.Y.T. Hsu, Peptides, 25, 1681 (2004). (Review)2) E.A. Woodcock, Endocrinology, 145, 21 (2004). (Review)3) Y. Kuperman and A. Chen, Trends Endocrinol. Metab., 19, 122 (2008). (Review)4) W.H. Pan and A.J. Kastin, Prog. Neurobiol., 84, 148 (2008). (Review)5) P. Boonprasert, N. Lailerd, and N. Chattipakorn, Int. J. Cardiol., 127, 307 (2008). (Review)

List of Stresscopin / Urocortin and Related Peptides
Code

CompoundQuantity

Price: Yen

Page

4387-s4388-s4328-s4327-s4383-sStresscopin (Human)
Stresscopin-Related Peptide (Human)
Urocortin (Human)
Urocortin (Rat)
Urocortin II (Mouse)

0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial
0.1 mg vial

16,00018,00014,00014,00014,000

below
143
143
143
144

Sequence Comparison of Human "Stresscopin / Urocortin III" and "Stresscopin-Related Peptide / Urocortin II"
Code

CompoundSequence

4387-s―Stresscopin (Human)
Urocortin III (Human)

TK FTLSLDVPTN IMNLLFNIAK AKNLRAQAAA NAHLMAQI-NH2FTLSLDVPTN IMNLLFNIAK AKNLRAQAAA NAHLMAQI-NH2

4388-sStresscopin-Related
HPGSR IVLSLDVPIG LLQILLEQAR ARAAREQATT NARILARV-NH2
Peptide (Human)
IVLSLDVPIG LLQILLEQAR ARAAREQAAT NARILARV-NH2
Urocortin II (Human)―4387-s-20

Stresscopin (Human)
Thr-Lys-Phe-Thr-Leu-Ser-Leu-Asp-Val-ProThr-Asn-Ile-Met-Asn-Leu-Leu-Phe-Asn-IleAla-Lys-Ala-Lys-Asn-Leu-Arg-Ala-Gln-AlaAla-Ala-Asn-Ala-His-Leu-Met-Ala-Gln-Ile-NH2(M.W. 4367.1)Vial

0.1 mg16,000C195H326N56O53S2

Selective Ligand for Type 2 CRF Receptors
1) S.Y. Hsu and A.J.W. Hsueh, Nat. Med., 7, 605 (2001). (Original)
2) F.M. Dautzenberg and R.L. Hauger, Trends Pharmacol. Sci., 23, 71 (2002). (Review)3) V. Mart́nez, L. Wang, J.E. Rivier, W. Vale, and Y Taché, J. Pharmacol. Exp. Ther., 301, 611 (2002). (Pharmacol.)4) A. Chanalaris, K.M. Lawrence, A. Stephanou, R.D. Knight, S.Y. Hsu, A.J.W. Hsueh, and D.S. Latchman, J. Mol. Cell.
Cardiol., 35, 1295 (2003). (Pharmacol.)– 142 –Stresscopin / Urocortin and Related Peptides (continued)
Price:Yen

4388-sStresscopin-Related Peptide (Human)-20

(Hydrochloride Form)

Vial

0.1 mg18,000

His-Pro-Gly-Ser-Arg-Ile-Val-Leu-Ser-LeuAsp-Val-Pro-Ile-Gly-Leu-Leu-Gln-Ile-LeuLeu-Glu-Gln-Ala-Arg-Ala-Arg-Ala-Ala-ArgGlu-Gln-Ala-Thr-Thr-Asn-Ala-Arg-Ile-LeuAla-Arg-Val-NH2(M.W. 4687.5)

C205H358N68O57

Selective Ligand for Type 2 CRF Receptors
1) S.Y. Hsu and A.J.W. Hsueh, Nat. Med., 7, 605 (2001). (Original)
2) F.M. Dautzenberg and R.L. Hauger, Trends Pharmacol. Sci., 23, 71 (2002). (Review)3) V. Mart́nez, L. Wang, J.E. Rivier, W. Vale, and Y Taché, J. Pharmacol. Exp. Ther., 301, 611 (2002). (Pharmacol.)4) A. Chanalaris, K.M. Lawrence, A. Stephanou, R.D. Knight, S.Y. Hsu, A.J.W. Hsueh, and D.S. Latchman, J. Mol. Cell.
Cardiol., 35, 1295 (2003). (Pharmacol.)4328-s-20

Urocortin (Human)
Asp-Asn-Pro-Ser-Leu-Ser-Ile-Asp-Leu-ThrPhe-His-Leu-Leu-Arg-Thr-Leu-Leu-Glu-LeuAla-Arg-Thr-Gln-Ser-Gln-Arg-Glu-Arg-AlaGlu-Gln-Asn-Arg-Ile-Ile-Phe-Asp-Ser-Val-NH2(M.W. 4696.2)

C204H337N63O64

Vial

0.1 mg14,000[176591-49-4]

Ligand for Type 1 / Type 2 CRF Receptors
1) C.J. Donaldson, S.W. Sutton, M.H. Perrin, A.Z. Corrigan, K.A. Lewis, J.E. Rivier, J.M. Vaughan, and W.W. Vale,
Endocrinology, 137, 2167 (1996). (Original; cDNA & Pharmacol.)2) D.P. Behan, O. Khongsaly, N. Ling, and E.B. De Souza, Brain Res., 725, 263 (1996). (Biochem.)
3) Y. Murakami, T. Mori, K. Koshimura, M. Kurosaki, T. Hori, N. Yanaihara, and Y. Kato, Endocr. J., 44, 627 (1997).
(Pharmacol.)4) K. Takahashi, K. Totsune, M. Sone, O. Murakami, F. Satoh, Z. Arihara, H. Sasano, K. Iino, and T. Mouri, Peptides,
19, 643 (1998). (Immunohistochem.)

4327-s-20

Urocortin (Rat)(Mouse)Asp-Asp-Pro-Pro-Leu-Ser-Ile-Asp-Leu-ThrPhe-His-Leu-Leu-Arg-Thr-Leu-Leu-Glu-LeuAla-Arg-Thr-Gln-Ser-Gln-Arg-Glu-Arg-AlaGlu-Gln-Asn-Arg-Ile-Ile-Phe-Asp-Ser-Val-NH2(M.W. 4707.3)

C206H338N62O64

Vial

0.1 mg14,000[171543-83-2]

Ligand for Type 1 / Type 2 CRF Receptors
1) J. Vaughan, C. Donaldson, J. Bittencourt, M.H. Perrin, K. Lewis, S. Sutton, R. Chan, A.V. Turnbull, D. Lovejoy,
C. Rivier, J. Rivier, P.E. Sawchenko, and W. Vale, Nature, 378, 287 (1995). (Original; cDNA & Pharmacol.)2) A.V. Turnbull, W. Vale, and C. Rivier, Eur. J. Pharmacol., 303, 213 (1996). (Pharmacol.; Inhibition of Edema)3) M. Spina, E. Merlo-Pich, R.K.W. Chan, A.M. Basso, J. Rivier, W. Vale, and G.F. Koob, Science, 273, 1561 (1996).
(Pharmacol.; Suppression of Appetite)4) L.Y. Zhao, C.J. Donaldson, G.W. Smith, and W.W. Vale, Genomics, 50, 23 (1998). (Nucleotide Seq.; Mouse)– 143 –and Proteins

CompoundBiologically Active Peptides

CodeStresscopin / Urocortin and Related Peptides (continued)
Code

Compound4383-s

Urocortin II (Mouse)
Val-Ile-Leu-Ser-Leu-Asp-Val-Pro-Ile-GlyLeu-Leu-Arg-Ile-Leu-Leu-Glu-Gln-Ala-ArgTyr-Lys-Ala-Ala-Arg-Asn-Gln-Ala-Ala-ThrAsn-Ala-Gln-Ile-Leu-Ala-His-Val-NH2-20

(M.W. 4152.9)

Price:Yen
Vial

0.1 mg14,000C187H320N56O50

Selective Ligand for Type 2 CRF Receptors
1) T.M. Reyes, K. Lewis, M.H. Perrin, K.S. Kunitake, J. Vaughan, C.A. Arias, J.B. Hogenesch, J. Gulyas, J. Rivier,
W.W. Vale, and P.E. Sawchenko, Proc. Natl. Acad. Sci. U.S.A., 98, 2843 (2001). (Original; Urocortin II)2) M. Million, C. Maillot, P. Saunders, J. Rivier, W. Vale, and Y. Taché, Am. J. Physiol. Gastrointest. Liver Physiol., 282,
G34 (2002). (Pharmacol.)3) C. Li, J. Vaughan, P.E. Sawchenko, and W.W. Vale, J. Neurosci., 22, 991 (2002). (Histochem.)
4) V. Mart́nez, L. Wang, J.E. Rivier, W. Vale, and Y. Taché, J. Pharmacol. Exp. Ther., 301, 611 (2002). (Pharmacol.)Substance P and Related Peptides
1) D. Regoli, A. Boudon, and J.-L. Fauchere, Pharmacol. Rev., 46, 551 (1994). (Review)

4014-v-20

Substance P*(Human, Bovine, Rat, Mouse)
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-LeuMet-NH2(M.W. 1347.6)

4014
-20

C63H98N18O13S

0.5 mg

3,300

Bulk

25 mg
100 mg50,000136,000[33507-63-0]

Substance P*(Human, Bovine, Rat, Mouse)
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-LeuMet-NH2 • 3AcOH • 5H2O
(M.W. 1347.6 • 180.16 • 90.08)

Vial

C63H98N18O13S • 3CH3COOH • 5H2O

Purity Information : QP See page IV (XVI)
1) U.S. von Euler and J.H. Gaddum, J. Physiol., 72, 74 (1931). (Naming)2) M.M. Chang, S.E. Leeman, and H.D. Niall, Nature New Biol., 232, 86 (1971). (Original; Bovine)
3) A.J. Harmar, A. Armstrong, J.C. Pascall, K. Chapman, R.Rosie, A. Curtis, J. Going, C.R.W. Edwards, and G. Fink,
FEBS Lett., 208, 67 (1986). (cDNA Seq.; Human)4172-v[D-Arg1,D-Pro2,D-Trp7,9,Leu11]-Substance P-20

(Hydrochloride Form)

Vial

0.5 mg

4,600

Bulk

25 mg

130,000

D-Arg-D-Pro-Lys-Pro-Gln-Gln- D-Trp-Phe-D-Trp-LeuLeu-NH2(M.W. 1497.8)

4172
-20

C75H108N20O13[84676-91-5][D-Arg1,D-Pro2,D-Trp7,9,Leu11]-Substance P
D-Arg-D-Pro-Lys-Pro-Gln-Gln- D-Trp-Phe-D-Trp-LeuLeu-NH2 • 3HCl • 8H2O
(M.W. 1497.8 • 109.38 • 144.12)

C75H108N20O13 • 3HCl • 8H2O

Purity Information : QP See page IV (XVI)

Bombesin Receptor Antagonist
1) R.T. Jensen, S.W. Jones, K. Folkers, and J.D. Gardner, Nature, 309, 61 (1984). (Original; Bombesin Antagonist)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 144 –

Substance P and Related Peptides (continued)
4173-v[D-Arg1,D-Trp7,9,Leu11]-Substance P
Spantide-20

Price:Yen
Vial

0.5 mg

4,600

Bulk

25 mg

130,000(Hydrochloride Form)
D-Arg-Pro-Lys-Pro-Gln-Gln-D-Trp-Phe-D-Trp-LeuLeu-NH2(M.W. 1497.8)

4173
-20

C75H108N20O13[91224-37-2][D-Arg1,D-Trp7,9,Leu11]-Substance P
Spantide
D-Arg-Pro-Lys-Pro-Gln-Gln-D-Trp-Phe-D-Trp-LeuLeu-NH2 • 3HCl • 8H2O
(M.W. 1497.8 • 109.38 • 144.12)

C75H108N20O13 • 3HCl • 8H2O

Purity Information : QP See page IV (XVI)

Substance P Antagonist
1) K. Folkers, R. Hákanson, J. Horig, X. Jie-Cheng, and S. Leander, Br. J. Pharmacol., 83, 449 (1984). (Original)

4113-v[D-Pro2,D-Trp7,9]-Substance P-20

(Hydrochloride Form)

Vial

0.5 mg

4,600

Bulk

25 mg

130,000

Arg-D-Pro-Lys-Pro-Gln-Gln-D-Trp-Phe-D-Trp-LeuMet-NH2(M.W. 1515.8)

4113
-20

C74H106N20O13S[80434-86-2][D-Pro2,D-Trp7,9]-Substance P
Arg-D-Pro-Lys-Pro-Gln-Gln-D-Trp-Phe-D-Trp-LeuMet-NH2 • 3HCl • 6H2O
(M.W. 1515.8 • 109.38 • 108.12)

C74H106N20O13S • 3HCl • 6H2O

Purity Information : QP See page IV (XVI)

Substance P Antagonist
1) G. Engberg, T.H. Svensson, S. Rosell, and K. Folkers, Nature, 293, 222 (1981). (Original)

4114-v-20

[D-Pro4,D-Trp7,9]-Substance P (4-11)
D-Pro-Gln-Gln-D-Trp-Phe-D-Trp-Leu-Met-NH2(M.W. 1134.4)

C57H75N13O10S

Vial

0.5 mg4,100[81039-85-2]

Substance P Antagonist
1) S. Caranikas, J. Mizrahi, P.D. Orleans-Juste, and D. Regoli, Eur. J. Phamacol., 77, 205 (1982). (Original)

4059-v-20

[Tyr8]-Substance P*
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Tyr-Gly-LeuMet-NH2

Vial

0.5 mg(M.W. 1363.6) C63H98N18O14S [55614-10-3]
Purity Information : Qx See page IV (XVI)For Radioimmunoassay*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 145 –

4,900

and Proteins

CompoundBiologically Active Peptides

CodeTachykinins
List of Tachykinins
Code

CompoundQuantity

Price: Yen

Page

NK1 Receptor Selective Peptides
Agonist4014-v

Substance P★

0.5 mg vial

3,300

144

4173-v
4113-v
4114-v[D-Arg1 D-Trp7,9 Leu11]-Substance P (Spantide)★
[D-Pro2, D-Trp7,9]-Substance P★
[D-Pro4, D-Trp7,9]-Substance P (4-11)

0.5 mg vial
0.5 mg vial
0.5 mg vial

4,600
4,600
4,100

145
145
145

4059-v[Tyr8]-Substance P

0.5 mg vial

4,900

145 / 242

0.5 mg vial

3,900

101

0.5 mg vial

3,900

101

0.5 mg vial
0.5 mg vial

8,000
8,000

57
57

0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial
0.5 mg vial

3,300
2,600
5,200
3,900
3,900

125
57
24
102
102

Antagonist

for RIANK2 Receptor Selective Agonist
4154-v

Neurokinin A★

NK3 Receptor Selective Agonist
4317-v

Neurokinin B★

Other NK Receptor Ligand
4411-v
4412-vEndokinin C (Human)
Endokinin D (Human)

Non-Mammalian Tachykinins / Bombesin Related Peptides
4030-v
4003-v
4086-v
4152-v
4153-v★

Physalaemin★
Eledoisin Related Peptide★
Bombesin★
Neuromedin B★
Neuromedin C★

Other bulk packaging is available.

Tertiapin
CodeCompound4364-sTertiapin(Honey Bee, Apis mellifera)
Ala-Leu-Cys-Asn-Cys-Asn-Arg-Ile-Ile-IlePro-His-Met-Cys-Trp-Lys-Lys-Cys-Gly-LysLys-NH2-20

Price:Yen
Vial

0.1 mg15,000(Disulfide bonds between Cys3-Cys14 and Cys5-Cys18)(M.W. 2455.1)

C106H176N34O23S5

Inward-Rectifier K+ Channel Blocker
1) W. Jin and Z. Lu, Biochemistry, 37, 13291 (1998). (Original; Pharmacol.)2) X. Xu and J.W. Nelson, Proteins Struct. Funct. Genet., 17, 124 (1993). (Structure; S-S Bond)
3) H. Kitamura, M. Yokoyama, H. Akita, K. Matsushita, Y. Kurachi, and M. Yamada, J. Pharmacol. Exp.Ther.,
293, 196 (2000). (Pharmacol.)4) M.-D. Drici, S. Diochot, C. Terrenoire, G. Romey, and M.L. Lazdunski, Br. J. Pharmacol., 131, 569 (2000).
(Pharmacol.)– 146 –

Tityustoxin
4313-sTityustoxin Kα
TsTX-Kα(Scorpion, Tityus serrulatus)
Val-Phe-Ile-Asn-Ala-Lys-Cys-Arg-Gly-SerPro-Glu-Cys-Leu-Pro-Lys-Cys-Lys-Glu-AlaIle-Gly-Lys-Ala-Ala-Gly-Lys-Cys-Met-AsnGly-Lys-Cys-Lys-Cys-Tyr-Pro-20

Price:Yen
Vial

0.1 mg30,000(Reported disulfide bonds between Cys7-Cys28, Cys13-Cys33, and Cys17-Cys35)(M.W. 3941.7)

C168H275N49O46S7

Voltage-Dependent K+ Channel (A Channel) Blocker
1) T.R. Werkman, T.A. Gustafson, R.S. Rogowski, M.P. Blaustein, and M.A. Rogawski, Mol. Pharmacol., 44, 430 (1993).
(Original)
2) R.S. Rogowski, B.K. Krueger, J.H. Collins, and M.P. Blaustein, Proc. Natl. Acad. Sci. U.S.A., 91, 1475 (1994).
(Pharmacol.)3) W.F. Hopkins, J. Pharmacol. Exp. Ther., 285, 1051 (1998). (Pharmacol.)4) K.C. Ellis, T.C. Tenenholz, H. Jerng, M. Hayhurst, C.S. Dudlak, W.F. Gilly, M.P. Blaustein, and D.J. Weber,
Biochemistry, 40, 5942 (2001). (S-S Bond)

Thyrotropin Releasing Hormone (TRH)4011-v-20

TRH
Thyrotropin Releasing Hormone(Human, Ovine, Porcine, Rat)
Pyr-His-Pro-NH2(M.W. 362.38)

4011
-20

C16H22N6O4

Vial

0.5 mg

1,900

Bulk

25 mg
100 mg

4,500
12,200[24305-27-9]

TRH
Thyrotropin Releasing Hormone(Human, Ovine, Porcine, Rat)
Pyr-His-Pro-NH2 • H2O(M.W. 362.38 • 18.02)

C16H22N6O4 • H2O
1) R. Burgus, T.F. Dunn, D. Desiderio, and R. Guillemin, C.R. Acad. Sci. Paris, 269, 1870 (1969). (Original; Ovine)
2) J. Bler, F. Enzman, K. Folkers, C.Y. Bowers, and A.V. Schally, Biochem. Biophys. Res. Commun., 37, 705 (1969).
(Original; Porcine)3) M. Yamada, S. Radovick, F.E. Wondisford, Y. Nakayama, B.D. Weintraub, and J.F. Wilber, Mol. Endocrinol.,4, 551 (1990). (cDNA Seq.; Human)

T-Kinin See Code 4130 Isoleucyl-Seryl-Bradykinin on page 28
TMRIA-K4 See Code 3401 on page 240

Tuftsin
4020-v-20

TuftsinThr-Lys-Pro-Arg(M.W. 500.59)

4020
-20

C21H40N8O6

0.5 mg

2,700

Bulk

25 mg
100 mg12,00036,000[9063-57-4]

TuftsinThr-Lys-Pro-Arg • 2AcOH(M.W. 500.59 • 120.10)
C21H40N8O6 • 2CH3COOH

Vial[72103-53-8]

Phagocytosis-Stimulating Peptide
1) K. Nishioka, A. Constantpoulos , P.S. Satoh, and V.A. Najjar, Biochem. Biophys. Res. Commun., 47, 172 (1972).
(Original)
2) K. Nishioka, P.S. Satoh, A. Constantpoulos, and V.A. Najjar, Biochim. Biophys. Acta, 310, 230 (1973).
(Chem. Synthesis & Pharmacol.)– 147 –and Proteins

CompoundBiologically Active Peptides

CodeUrocortins
As for the details, see the section of Stresscopin / Urocortin and Related Peptides on pages 142 ～ 144
CodeCompoundQuantity

Price: Yen

Page

4328-s4327-s4383-s

Urocortin (Human)
Urocortin (Rat)
Urocortin II (Mouse)

0.1 mg vial
0.1 mg vial
0.1 mg vial

14,00014,00014,000

143
143
144

Uroguanylin See Code 4295 Uroguanylin Isomer A (Human) , Code 4354 Uroguanylin (Rat)and Code 4463 Uroguanylin Isomer B (Human) on pages 76～78

Urotensin II and Related Peptides
1) A.P. Davenport and J.J. Maguire, Trends Pharmacol. Ther., 21, 80 (2000). (Review)2) K.L. Ong, K.S.L. Lam, and B.M.Y. Cheung, Cardiovasc. Drug. Ther., 19, 65 (2005). (Review)
3) T. Sugo and M. Mori, Peptides, 29, 809 (2008). (Review)4) K.L. Ong, L.Y.F. Wong, and B.M.Y. Cheung, Peptides, 29, 859 (2008). (Review)5) Z. Carmine and F. Mallamaci, Curr. Opin. Nephrol. Hypertens., 17, 199 (2008). (Review)6) D. Guidolin, G. Albertin, and D. Ribatti, Peptides, 31, 1219 (2010). (Review)

List of Urotensin II and Related Peptides
Code

CompoundQuantity

Price: Yen

Page

4365-v
4371-v
4408-vUrotensin II (Human)
Urotensin II (Rat)
Urotensin II-Related Peptide (Human)

0.5 mg vial
0.5 mg vial
0.5 mg vial

20,00020,00012,000

below
149
149

Code

Compound4365-vUrotensin II (Human)
UII(Monkey)-20

Price:Yen
Vial

0.5 mg20,000(Hydrochloride Form)

Glu-Thr-Pro-Asp-Cys-Phe-Trp-Lys-Tyr-CysVal(Disulfide bond between Cys5-Cys10)(M.W. 1388.6)

C64H85N13O18S2 [251293-28-4]
Purity Information : QE See page IV (XVI)

Potent Vasoconstrictor
1) Y. Coulouarn, I. Lihrmann, S. Jegou, Y. Anouar, H. Tostivint, J.C. Beauvillain, J.M. Conlon, H.A. Bern, and H. Vaudry,
Proc. Natl. Acad. Sci. U.S.A., 95, 15803 (1998). (Original)
2) R.S. Ames, H.M. Sarau, J.K. Chambers, R.N. Willette, N.V. Aiyar, A.M. Romanic, C.S. Louden, J.J. Foley,
C.F. Sauermelch, R.W. Coatney, Z. Ao, J. Disa, S.D. Holmes, J.M. Stadel, J.D. Martin, W.-S. Liu, G.I. Glover,
S. Wilson, D.E. McNulty, C.E. Ellis, N.A. Elshourbagy, U. Shabon, J.J. Trill, D.W.P. Hay, E.H. Ohlstein, D.J. Bergsma,
and S.A. Douglas, Nature, 401, 282 (1999). (Pharmacol.)3) M.R. MacLean, D. Alexander, A. Stirrat, M. Gallagher, S.A. Douglas, E.H. Ohlstein, I. Morecroft, and K. Polland,
Br. J. Pharmacol., 130, 201 (2000). (Pharmacol.)4 ) N.A. Elshourbagy, S.A. Douglas, U. Shabon, S. Harrison, G. Duddy, J.L. Sechler, Z. Ao, B.E. Maleeff., D. Naselsky,
J. Disa, and N.V. Aiyar , Br. J. Pharmacol., 136, 9 (2002). (Original; Monkey)– 148 –Urotensin II and Related Peptides (continued)
4371-vUrotensin II (Rat)[Pyr110]-Prepro-Urotensin II (Rat, 110-123)
Pyr-His-Gly-Thr-Ala-Pro-Glu-Cys-Phe-TrpLys-Tyr-Cys-Ile-20

Price:Yen
Vial

0.5 mg20,000(Disulfide bond between Cys8-Cys13)(M.W. 1663.9)

C77H102N18O20S2

Vasoconstrictor
Following the sequence determination of human urotensin II (U-II), the same group reported thecorresponding rat peptide cDNA sequence. When we look at the deduced peptide sequence of rat prepro-U-II,
there are two double basic sites at its C-terminal region, which might be the enzymatic cleavage sites foryielding the mature peptide of Urotensin II (Rat). We chose the shorter peptide of 14 amino acid residues with
pyroglutamic acid modification for Gln110 as the possible candidate for Urotensin II (Rat) and chemicallysynthesized it. Synthetic [Pyr110]-prepro-U-II (110-123) was confirmed to have a vasoconstricting activity as
potent as that of human peptide in the isolated thoracic aorta of rat. Cardiovascular activity of Urotensin II(Rat) and Urotensin II (Human) is also reported2). We, therefore, named this peptide as Urotensin II (Rat) in thiscatalog (putative naming only), although the native form of Urotensin II (Rat) remains to be identified.
1) Y. Coulouarn, S. Jégou, H. Tostivint, H. Vaudry, and I. Lihrmann, FEBS Lett., 457, 28 (1999). (Original)
2) S.M. Gardiner, J.E. March, P.A. Kemp, A.P. Davenport, and T. Bannett, Br. J. Pharmacol., 132, 1625 (2001).
(Pharmacol.)4408-v-20

Urotensin II-Related Peptide (Human)(Rat, Mouse)
Ala-Cys-Phe-Trp-Lys-Tyr-Cys-Val

Vial

0.5 mg12,000(Disulfide bond between Cys2-Cys7)(M.W. 1017.2)

C49H64N10O10S2[342878-90-4]

Endogenous Hypotensive Peptide
1) T. Sugo, Y. Murakami, Y. Shimomura, M. Harada, M. Abe, Y. Ishibashi, C. Kitada, N. Miyajima, N. Suzuki,
M. Mori, and M. Fujino, Biochem. Biophys. Res. Commun., 310, 860 (2003).
(Original; Urotensin II-Related Peptide)2) M. Mori and M. Fujino, Peptides, 25, 1815 (2004). (Review)

Vasoactive Intestinal Contractor See Code 4211 VIC (Mouse) on page 63– 149 –and Proteins

CompoundBiologically Active Peptides

CodeVasoactive Intestinal Peptide (VIP)
CodeCompound4110-sVIP (Human, Porcine)
Vasoactive Intestinal Peptide (Human, Porcine)(Bovine, Rat, Canine)
His-Ser-Asp-Ala-Val-Phe-Thr-Asp-Asn-TyrThr-Arg-Leu-Arg-Lys-Gln-Met-Ala-Val-LysLys-Tyr-Leu-Asn-Ser-Ile-Leu-Asn-NH2-20

(M.W. 3325.8)

4110-v-20

Price:Yen

C147H238N44O42S

Vial

0.1 mg

9,500

Vial

0.5 mg33,000[40077-57-4]

VIP (Human, Porcine)
Vasoactive Intestinal Peptide (Human, Porcine)(Bovine, Rat, Canine)[40077-57-4]

1) V. Mutt and S.I. Said, Eur. J. Biochem., 42, 581 (1974). (Original; Porcine)2) N. Itoh, K. Obata, N. Yanaihara, and H. Okamoto, Nature, 304, 547 (1983). (cDNA Seq.; Human)
3) R. Dimaline, J.R. Reeve, Jr., J.E. Shively, and D. Hawke, Peptides, 5, 183 (1984). (Original; Rat)
4) S.C. Wang, B.H. Du, J. Eng, M. Chang, J.D. Hulmes, Y.-C.E. Pan, and R.S. Yalow, Life Sci., 37, 979 (1985).
(Original; Canine)

Vasopressin, Vasotocin, and Related Peptides
1) B. Berde (ed.), Neurohypophysial Hormones and Similar Polypeptides, Handbook of Experimental Pharmacology, Vol. 23,
Springer-Verlag, Berlin, 1968. (Review)

4085-v-20

[Arg8]-Vasopressin*(Human, Bovine, Ovine, Rat, Mouse)
Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Arg-Gly-NH2

Vial

0.5 mg

4,800(Disulfide bond between Cys1-Cys6)(M.W. 1084.2)

C46H65N15O12S2[113-79-1]

1) E.A. Popenoe and V. Du Vigneaud, J. Biol. Chem., 205, 133 (1953). (Original; Bovine)
2) A. Light and V. Du Vigneaud, Proc. Soc. Exp. Biol. Med., 98, 692 (1958). (Original; Human)
3) H. Schmale, S. Heinsohn and D. Richter, EMBO J., 2, 763 (1983). (Nucleotide Seq.; Rat)

4026-v-20

[Asu1,6,Arg8]-Vasopressin*
Deamino-Dicarba-Arginine-Vasopressin

Vial

0.5 mg5,700

cyclo(Tyr-Phe-Gln-Asn-Asu)-Pro-Arg-Gly-NH2(Asu: L-α-Aminosuberic acid)(Cyclic form between Asu ω-carboxyl group and Tyr α-amino group)(M.W. 1033.1)

C48H68N14O12 [40944-53-4]
Purity Information : QX See page IV (XVI)

1) S. Hase, S. Sakakibara, M. Wahrenburg, M. Kirchberger, I.L. Schwartz, and R. Walter, J. Am. Chem. Soc.,
94, 3590 (1972). (Original)

4203-v-20

[Pmp1,Tyr(Me)2]-Arg8-Vasopressin*
Pmp-Tyr(Me)-Phe-Gln-Asn-Cys-Pro-Arg-Gly-NH2

Vial

0.5 mg10,500(Pmp: β-Mercapto-β,β-cyclopentamethylene propionic acid)(Tyr(Me): O-Methyl-L-tyrosine)(Disulfide bond between Pmp1-Cys6)(M.W. 1151.4)

C52H74N14O12S2[73168-24-8]

Potent Arginine Vasopressin V1 Antagonist
1) M. Kruszynski, B. Lammerk, M. Manning, J. Seto, J. Halder, and W.H. Sawyer, J. Med. Chem., 23, 364 (1980).
(Original)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 150 –

Vasopressin, Vasotocin, and Related Peptides (continued)
4192-v[Arg8]-Vasotocin*(Frog, Chicken)
Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Arg-Gly-NH2-20

Price:Yen
Vial

0.5 mg

4,800(Disulfide bond between Cys1-Cys6)(M.W. 1050.2)

C43H67N15O12S2[74927-14-3]

1) R. Acher, J. Chauvet, M.T. Lenci, F. Morel, and J. Maetz, Biochim. Biophys. Acta, 42, 379 (1960). (Original; Frog)
2) J. Chauvet, M.T. Lenci, and R. Acher, Biochim. Biophys. Acta, 38, 571 (1960). (Original; Chicken)

4027-v-20

[Asu1,6,Arg8]-Vasotocin*
Deamino-Dicarba-Arginine-Vasotocin

Vial

0.5 mg5,700

cyclo(Tyr-Ile-Gln-Asn-Asu)-Pro-Arg-Gly-NH2(Asu: L-α-Aminosuberic acid)(Cyclic form between Asu ω-carboxyl group and Tyr α-amino group)(M.W. 999.12)

C45H70N14O12[35375-13-4]

1) S. Hase, S. Sakakibara, M. Wahrenburg, M. Kirchberger, I.L. Schwartz, and R. Walter, J. Am. Chem. Soc.,
94, 3590 (1972). (Original)

VIC (Mouse) See Code 4211 on page 63

Virus Replication Inhibiting Peptide
4092
-20

Bulk

Virus Replication Inhibiting Peptide
Z-D-Phe-Phe-Gly

25 mg
100 mg

7,800
16,000(Z: Benzyloxycarbonyl)(M.W. 503.55)

C28H29N3O6 [75539-79-6]
1) C.D. Richardson, A. Scheid, and P.W. Choppin, Virology, 105, 205 (1980). (Original)

Xenin
4279-v-20

Xenin 25 (Human)
Met-Leu-Thr-Lys-Phe-Glu-Thr-Lys-Ser-AlaArg-Val-Lys-Gly-Leu-Ser-Phe-His-Pro-LysArg-Pro-Trp-Ile-Leu(M.W. 2971.6)

Vial

0.5 mg29,000C139H224N38O32S

Xenopsin Related Peptide
1) G.E. Feurle, G. Hamscher, R. Kusiek, H.E. Meyer, and J.W. Metzger, J. Biol. Chem., 267, 22305 (1992). (Original)*

The biological activity of these peptides is examined by the Division of Pharmacology, Peptide Institute, Inc.

– 151 –and Proteins

CompoundBiologically Active Peptides

CodeBiologically Active Proteins
Lysenin
Code

Compound4802-v

Lysenin(Earthworm, Eisenia foetida)-20

Price:Yen
Vial

50 µg

20,000Natural product isolated from the coelomic fluid of earthworm
Salt free lyophilized powder(M.W. 33 kDa)

Sphingomyelin-Specific Binding Protein
Lysenin is a sphingomyelin-specific binding protein without any cross reactions with other sphingolipids,
such as sphingosine, ceramide and sphingosyl phosphocholine1). It was isolated from the coelomic fluid of theearthworm Eisenia foetida by Sekizawa et al. in 19962,3) and has a molecular size of 33 kDa as determined bysize-exclusion chromatography2). It has hemolytic and smooth muscle-contracting activity4) and lethal effects
on mouse and Xenopus spermatozoa5). The lethal effects may be brought about by the interaction of lyseninwith sphingomyelin present in the outer leaflets of plasma membranes of spermatozoa. It was shown thatlysenin required cell surface sphingomyelin for its lytic activity on Chinese hamster ovary cells6). In
combination with immunological techniques, it is possible to use lysenin as a tool for histochemical
identification and tissue distribution studies of sphingomyelin1,5). In view of the involvement of ceramide,
sphingosine, and sphingosine 1-phosphate, which are derived from sphingomyelin, in signal transduction,
mitogenesis and apoptosis7), lysenin may serve as a useful tool in elucidating specific reactions leading todefined cellular responses.
1) A. Yamaji, Y. Sekizawa, K. Emoto, H. Sakuraba, K. Inoue, H. Kobayashi, and M. Umeda, J. Biol. Chem.,
273, 5300 (1998).
2) Y. Sekizawa, K. Hagiwara, T. Nakajima, and H. Kobayashi, Biomed. Res., 17, 197 (1996).
3) Y. Sekizawa, T. Kubo, H. Kobayashi, T. Nakajima, and S. Natori, Gene, 191, 97 (1997).
4) H. Kobayashi, Y. Sekizawa, S. Shioda, S. Natori, T. Nakajima, and M. Umeda, In, Neuroendocrinology-Retrospect
and Perspectives (H.-W. Korf and K.H. Usadel eds.), Springer, 1997, p. 255.
5) M. Ito, S. Abe, Y. Sekizawa, and H. Kobayashi, Biomed. Res., 18, 399 (1997).
6) K. Hanada, T. Hara, M. Fukasawa, A. Yamaji, M. Umeda, and M. Nishijima, J. Biol. Chem., 273, 33787 (1998).
7) L.R. Ballou, S.J.F. Laulederkind, E.F. Rosloniec, and R. Raghow, Biochim. Biophys. Acta, 1301, 273 (1996).
• This product is produced by Zenyaku Kogyo Co., Ltd.

– 152 –

Midkines
4298-v

Midkine (Human)-20

Amino Acid Sequence: See Page 94(M.W. 13240.1)

Price:Yen

C570H915N177O167S10

Vial

50 µg

30,000[170138-17-7]

Synthetic ProductHeparin-Binding Growth / Differentiation Factor(Neurotrophic Factor, Neurite Outgrowth-Promoting Factor)
Plasminogen Activator Activity Enhancer
1) J.-i. Tsutsui, K. Uehara, K. Kadomatsu, S. Matsubara, and T. Muramatsu, Biochem. Biophys. Res. Commun.,
176, 792 (1991). (Original)
2) H. Muramatsu, T. Inui, T. Kimura, S. Sakakibara, X.-j. Song, H. Maruta, and T. Muramatsu, Biochem. Biophys. Res.
Commun., 203, 1131 (1994). (Pharmacol.)3) T. Inui, J. Bódi, S. Kubo, H. Nishio, T. Kimura, S. Kojima, H. Maruta, T. Muramatsu, and S. Sakakibara, J. Peptide Sci.,
2, 28 (1996). (Chem. Synthesis)4) G.S.P. Yu, J. Hu, and H. Nakagawa, Neurosci. Lett., 254, 128 (1998). (Pharmacol.; Inhibition of β -amyloid
cytotoxicity)• This product is distributed under the license of Prof. Takashi Muramatsu. Its use for any purpose other than researchis strictly prohibited.

4299-sMidkine (Human, 60-121)-20

See Page 95

Vial

0.1 mg30,000• This product is distributed under the license of Prof. Takashi Muramatsu. Its use for any purpose other than researchis strictly prohibited.

Pleiotrophin
4335-v-20

Vial

Pleiotrophin (Human)
PTN (Human)

50 µg

30,000Amino Acid Sequence: See Page 128(M.W. 15302.6)

C658H1079N197O198S12

Synthetic ProductHeparin-Binding Growth Factor (Neurite Outgrowth-Promoting Factor)
1) Y.-S. Li, P.G. Milner, A.K. Chauhan, M.A. Watson, R.M. Hoffman, C.M. Kodner, J. Milbrandt, and T.F. Deuel,
Science, 250, 1690 (1990). (Primary Structure)2) P.G. Milner, D. Shah, R. Veile, H. Donis-Keller, and B.V. Kumar, Biochemistry, 31, 12023 (1992).
(Nucleotide Seq.; Human)
3) F. Czubayko, A.M. Schulte, G.J. Berchem, and A. Wellstein, Proc. Natl. Acad. Sci. U.S.A., 93, 14753 (1996).
(Pharmacol.)4) T. Inui, M. Nakao, H. Nishio, Y. Nishiuchi, S. Kojima, T. Muramatsu, T. Kimura, and S. Sakakibara, J. Pept. Res.,55, 384 (2000). (Chem. Synthesis & S-S Bond)– 153 –and Proteins

CompoundBiologically Active Peptides

CodeAppendix

Lists in this catalog****** Biologically Active Peptides and Proteins ******
List Name

Page

List of Adrenomedullin and Related Peptides …………………………………………………………

5

List of Angiotensin and Related Peptides ……………………………………………………………… 15
List of ANP and Related Peptides ……………………………………………………………………… 19
List of Bradykinin and Related Peptides ……………………………………………………………… 25
List of Conotoxins ………………………………………………………………………………………… 38
List of Defensins ………………………………………………………………………………………… 45
List of Endothelin and Related Peptides……………………………………………………………… 59

List of Feeding-Regulatory Peptides …………………………………………………………………… 65
List of lon Channel Blockers …………………………………………………………………………… 42
List of Kisspeptin / Metastin and Related Peptide …………………………………………………… 86
List of Muscarinic Toxins……………………………………………………………………………… 96

List of Neuromedins ……………………………………………………………………………………… 102
List of Opioid Peptides………………………………………………………………………………… 114

List of Parathyroid Hormone (PTH) and Related Peptides………………………………………… 118

List of Products for Alzheimer's Disease Research …………………………………………………… 11
List of Stresscopin / Urocortin and Related Peptides ………………………………………………… 142
List of Tachykinins……………………………………………………………………………………… 146

List of Urotensins II and Related Peptides …………………………………………………………… 148****** Enzyme Inhibitors and Substrates ******
List Name

Page

List of Inhibitors and Substrates for Various Proteases ……………………………………………… 156
List of MCA-Substrates………………………………………………………………………………… 164

List of MOCAc / Dnp type Substrates ………………………………………………………………… 166
List of Nma / Dnp type Substrates ……………………………………………………………………… 166
List of pNA-Substrates …………………………………………………………………………………… 174– 154 –