peptide28̲3小冊子 p.1 [コンポジット] [100%x100%]2015/3/4 19:50

Biologically Active Peptides
Amyloid β-Proteins
Code

CompoundPrice:Yen

4481-v

New

Amyloid β-Protein (Human, 1-28)
SP-28 (Human)-20

(Trifluoroacetate Form)

Vial

0.5 mg15,000

Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-PheAla-Glu-Asp-Val-Gly-Ser-Asn-Lys(M.W. 3262.5)

C145H209N41O46
Purity ≧99.0% (HPLC)[109770-29-8]

Amyloidogenic Segment of Amyloid β -Protein
Amyloid β-protein (Human, 1-28) is a peptide that was synthesized chemically during the early stages ofamyloid β-proteins research1). Over the years, many research publications using amyloid β-protein (Human,
1-28) have been reported, frequently including: i) formation of amyloid fibrils1-5) and ii) expression ofneurotrophic or neurotoxic activity5-7), some of which are specific to this particular peptide. Amyloid β-protein(Human, 1-28) possesses only one of the fibril forming domains (central domain) and lacks the corresponding
C-terminal one5), so that this peptide reinforces a structural as well as functional interest in the research of
Alzheimer's disease.
1) D.A. Kirschner, H. Inouye, L.K. Duffy, A. Sinclair, M. Lind, and D.J. Selkoe, Proc. Natl. Acad. Sci. U.S.A., 84, 6953
(1987). (Original; Amyloid-Like Fibril Formation)2) B. Klajnert, M. Cortijo-Arellano, J. Cladera, and M. Bryszewska, Biochem. Biophys. Res. Commun., 345, 21 (2006).
(Amyloid Fibril Formation)3) A. Perálvarez-Marin, A. Barth, and A. Graslund, J. Mol. Biol., 379, 589 (2008). (Amyloid Fibril Formation)4) N.G.N. Milton and J.R. Harris, Micron, 40, 800 (2009). (Amyloid Fibril Formation)5) T. Wasiak, M. Ionov, K. Nieznanski, H. Nieznanska, O. Klementieva, M. Granell, J. Cladera, J.-P. Majoral,
A.M. Caminade, and B. Klajnert, Mol. Pharm., 9, 458 (2012). (Amyloid Fibril Formation & Neurotoxicity)
6) J.S. Whitson, D.J. Selkoe, and C.W. Cotman, Science, 243, 1488 (1989). (Pharmacol.)7) B.A. Yankner, L.K. Duffy, and D.A. Kirschner, Science, 250, 279 (1990). (Pharmacol.)4484-vNew-20

Amyloid β-Protein (Human, 1-38)

Vial

0.5 mg17,000(Trifluoroacetate Form)

Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-PheAla-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly(M.W. 4131.5)

C184H277N51O56S
Purity ≧95.0% (HPLC)[131438-74-9]

Endogenous Form of Amyloid β -Protein in Cerebrospinal Fluid
Human amyloid β-proteins are produced by enzymatic cleavages of amyloid precursor protein (APP);
enzymes involved are β- and γ-secretases. Successive scissions of APP by these enzymes yield primarily thelonger forms of amyloid β-protein, such as amyloid β-protein (1-49). Recently, it has been clarified that these
longer forms are not the final products, but the substrates of γ-secretase, providing amyloid β-protein (Human,
1-38) through numerous intermediates such as amyloid β-protein (Human, 1-42) (Code 4349-v), and amyloid
β-protein (Human, 1-43) (Code 4370-v)1,2).
Amyloid β-protein (Human, 1-38) has been discovered to exist in human plasma and cerebrospinal fluid3,4),
among other locations. Functionally, amyloid β-protein (Human, 1-38) is reported to enhance glutamate
neurotoxicity in cortical cultures at doses between 20 and 80 μM5). Amyloid β-protein (Human, 1-38) is now
available from Peptide Institute, Inc.
1) M. Okochi, S. Tagami, K. Yanagida, M. Takami, T.S. Kodama, K. Mori, T. Nakayama, Y. Ihara, and M. Takeda,
Cell Rep., 3, 42 (2013). (γ -Secretase-Mediated Generation)2) N. Matsumura, M. Takami, M. Okochi, S. Wada-Kakuda, H. Fujiwara, S. Tagami, S. Funamoto, Y. Ihara,
and M. Morishima-Kawashima, J. Biol. Chem., 289, 5109 (2014). (γ -Secretase-Mediated Generation)
3) J.M. Maler, H.-W. Klafki, S. Paul, P. Spitzer, T.W. Groemer, A.W. Henkel, H. Esselmann, P. Lewczuk, J. Kornhuber,
and J. Wiltfang, Proteomics, 7, 3815 (2007). (Quantitation in Human Plasma)4) M.E. Lame, E.E. Chambers, and M. Blatnik, Anal. Biochem., 419, 133 (2011).
(Quantitation in Human Cerebrospinal Fluid)5) M.P. Mattson, B. Cheng, D. Davis, K. Bryant, I. Lieberburg, and R.E. Rydel, J. Neurosci., 12, 376 (1992).
(Pharmacol.; Enhancement of Glutamate Neurotoxicity)–1 –Orexins
Code

Compound4482-sOrexin-A (Human, 17-33)
OXA (17-33)
Tyr-Glu-Leu-Leu-His-Gly-Ala-Gly-Asn-HisAla-Ala-Gly-Ile-Leu-Thr-Leu-NH2

New

-20

Price:Yen(M.W.1749.0)

C79H125N23O22
Purity ≧99.0% (HPLC)

Vial

0.1 mg

8,000

Vial

0.1 mg10,000[343268-91-7]

Orexin-1 Receptor Selective Agonist
4483-sNew-20

[Ala11, D-Leu15]-Orexin B (Human)
Arg-Ser-Gly-Pro-Pro-Gly-Leu-Gln-Gly-ArgAla-Gln-Arg-Leu-D-Leu-Gln-Ala-Ser-Gly-AsnHis-Ala-Ala-Gly-Ile-Leu-Thr-Met-NH2(M.W. 2857.3)

C120H206N44O35S[532932-99-3]

Orexin-2 Receptor Selective Agonist
Orexin A (Code 4346-s) and orexin B (Code 4348-s: Human, Code 4347-s: Rat & Mouse) elicit numerous
biological functions including feeding regulation and wake/sleep regulation. These peptides bind to two G
protein-coupled receptors, orexin 1 receptor (OX1) and orexin 2 receptor (OX2) to express their biologicalactivities; orexin A interacts with both OX1 and OX2 non-selectively, whereas orexin B shows preferential OX2binding ability. To learn the contributions of these peptides to exerting an individual function of orexins, aselective ligand to each receptor subtype is required.
After an extensive structure-activity relationship study of orexin A, orexin A (Human, 17-33) was
discovered to be 23-fold more selective to OX1 than OX21). In the case of OX2, [Ala11, D-Leu15]-orexin B(Human) is reported to show a 400-fold selectivity over OX12), although one report described that such potency
in receptor selectivity could not be reproduced3). These two orexin analogs may be useful tools for orexin A andorexin B distinguishing research.
1) N.A. German, A.M. Decker, B.P. Gilmour, B.F. Thomas, and Y. Zhang, ACS Med. Chem. Lett., 4, 1224 (2013).
(Original; Structure-Activity Relationship & Pharmacol.)2) S. Asahi, S.-I. Egashira, M. Matsuda, H. Iwaasa, A. Kanatani, M. Ohkubo, M. Ihara, and H. Morishima,
Bioorg. Med. Chem. Lett., 13, 111 (2003). (Original; Structure-Activity Relationship & Pharmacol.)3) J. Putura, P.M. Turunen, M.H. Ja
ntti, M.E. Ekholm, and J.P. Kukkonen, Neurosci. Lett., 494, 57 (2011). (Pharmacol.)

–2 –

CEP1
Code

Compound4487-sCEP1C-Terminally Encoded Peptide 1(Plant, Arabidopsis)
Asp-Phe-Arg-Hyp-Thr-Asn-Pro-Gly-Asn-SerHyp-Gly-Val-Gly-His

New

-20

(M.W. 1583.6)

Price:Yen
Vial

0.1 mg

7,000

C66H98N22O24

Mediator of Systemic N-Demand Signaling in Plant
In plants the peptide ligand-receptor systems are involved in developmental processes with some diversities1).
Peptide ligands in these systems are categorized into groups; the major constituents are the secreted small
peptides with posttranslational modification(s) which function extracellularly2). This particular group of
peptides is encoded by paralogous genes, in which the mature peptides are located at the C-terminal conserved
domains. One such peptide is phytosulfokine (Code 4477-s), which contains two sulfated-Tyr residues.
Another member of this family is CEP1 (C-terminally encoded peptide 1), isolated from Arabidopsis by insilico gene screening3). Very recently, a signaling systems triggered by CEP1 has been clarified4): 1) secretion of
CEP1 from root upon starvation of N-neutrient, 2) translocation of CEP1 to shoot and perception by Leu-richrepeat receptor kinases (LRR-RKs) which are receptors of CEP1, and 3) stimulation of nitrate uptake in roots in
N–rich region. This "root-to-shoot-back-to-root" signaling is considered to be effective in escaping from theretardation of root growth under the nutrient-depleted conditions. CEP1 may help in understanding theadaptation mechanism of plants in environmentally disadvantageous situations.
1) S. Endo, S. Betsuyaku, and H. Fukuda, Curr. Opin. Plant Biol., 21, 140 (2014). (Review)2) Y. Matsubayashi, Annu. Rev. Plant Biol., 65, 385 (2014). (Review)3) K. Ohyama, M. Ogawa, and Y. Matsubayashi, Plant J., 55, 152 (2008). (Original)
4) R. Tabata, K. Sumida, T.Yoshii, K.Ohyama, H. Shinohara, and Y. Matsubayashi, Science, 346, 343 (2014).
(Pharmacol.)–3 –Enzyme Substrates
Code

Compound3234-sLISA-101

New

-20

Price:Yen
Vial

0.1 mg10,000(Trifluoroacetate Form)

γ-L-Glutamyl-(2S)-Nγ-ethyl-Nγ-[(3-oxo-3H-phenoxazin-7-yl)oxy]
carbonyl-2,4-diaminobutyric acid
(M.W. 514.48) C24H26N4O9
Purity ≧98.0% (HPLC)[1638785-74-6]

Fluorogenic Substrate for γ -Glutamyl Cyclotransferase (GGCT)
N
O
N

O

O

O

O
H2N
O

N
H
OH

OH
O

γ-Glutamyl cyclotransferase1) (GGCT, γ-GCT, C7orf24, EC 2.3.2.4) attracts interest as a member ofglutathione cycle-related enzymes. GGCT has been found to be over-expressed in a range of cancers2). In
particular, presence of GGCT is thought to be relevant to the malignancy of the cancer cells3). Additionally, it isinteresting that systemic administration of siRNA of GGCT could retard the tumor growth and induce necrosis oftumor tissue while showing no obvious toxicity to normal tissues4). Specifically, GGCT converts γ-glutamyl
amino acids (γ-Glu-Xaa, Xaa: any amino acid) into 5-oxoproline (pyroglutamate) and the corresponding aminoacids (Xaa). This singular substrate preference hampered its chemical probe development for some time.
Against this background, a novel fluorogenic GGCT probe " LISA*-101" was successfully developed
at Peptide Institute, Inc. in collaboration with Professor Yoshiki of Kyoto Pharmaceutical University and Shiga
University of Medical Science5). GGCT treatment liberates an intact fluorophore "resorufin" from LISA-101
which is not a fluorescence compound. This makes it possible to quantify GGCT activity with the guidance offluorescence (e.g. Ex 571 nm/ Em 585 nm). This probe, LISA-101, can expand the repertoire of strategies usedin cancer studies related to GGCT.
*LISA: Ligand Inspired by Substrate Acidity
1) a) M. Orlowsli, P.G. Richman, and A. Meister, Biochemistry, 8, 1048 (1969); b) A.J. Oakley, T. Yamada, D. Liu,
M. Coggan, A.G. Clark, and P.G. Board, J. Biol. Chem., 283, 22031 (2008). (Isolation and Identification of GGCT)2) P. Gromov, I. Gromova, E. Friis, V. Timmermans-Wielenga, F. Rank, R. Simon, G. Sauter, and J.M.A. Moreira,J. Proteome Res., 9, 3941 (2010). (Proteomic Profiling of Mammary Carcinomas)
3) K. Takemura, H. Kawachi, Y. Eishi, K. Kitagaki, M. Negi, M. Kobayashi, K. Uchida, J. Inoue, J. Inazawa, T. Kawano,and P.G. Board, Human Pathol., 45, 331 (2014). (GGCT as a Diagnostic Marker in Esophageal Tumors)
4) R. Ran, Y. Liu, H. Gao, Q. Kuang, Q. Zhang, J. Tang, H. Fu, Z. Zhang, and Q. He, J. Pharm. Sci., 104, 476 (2015).
(siRNA for Treatment of Drug-Resistant Breast Cancer)5) a) H. Ii, Y. Nishiuchi, T. Yoshiki, and T. Yoshiya, Japan Patent JP 2014-218494 Ab) T.Yoshiya, H. Ii, S.Tsuda, S.Kageyama, T.Yoshiki and Y.Nishiuchi, Org. Biomol. Chem., 13, 3182 (2015).
(Development of LISA-101)• This compound is distributed under the license of Dr. Tatsuhiro Yoshiki and Peptide Institute, Inc.

–4 –

Code

Compound3235-v

Leu-Asp-MCA

New

-20

Price:Yen
Vial

5 mg

5,000

L-Leucyl-L-aspartic acid α-(4-methylcoumaryl-7-amide)(M.W. 403.43) C20H25N3O6 [929621-97-6]
Purity ≧99.0% (HPLC), AMC ≦0.1%, TLC single spot

Substrate for Porphyromonas Gingivalis Dipeptidyl-Peptidase 11
1) Y. Ohara-Nemoto, Y. Shimoyama, S. Kimura, A. Kon, H. Haraga, T. Ono, and T.K. Nemoto, J. Biol. Chem., 286,
38115 (2011).
2) S.M. Rouf, Y. Ohara-Nemoto, T. Hoshino, T. Fujiwara, T. Ono, and T.K. Nemoto, Biochimie, 95, 824 (2013).
3) S.M. Rouf, Y. Ohara-Nemoto, T. Ono, Y. Shimoyama, S. Kimura, and T.K. Nemoto, FEBS Open Bio, 3, 177 (2013).

3236-v

New

-20

Vial

Met-Leu-MCA

5 mg

5,000

(Trifluoroacetate Form)
L-Methionyl- L-Leucine 4-methylcoumaryl-7-amide(M.W. 419.54)

C21H29N3O4S [1009549-31-8]
Purity ≧99.0% (HPLC), AMC ≦0.1%, TLC single spot

Substrate for Porphyromonas Gingivalis Dipeptidyl-Peptidase 71) A. Banbula, J. Yen, A. Oleksy, P. Mak, M. Bugno, J. Travis, and J. Potempa, J. Biol. Chem., 276, 6299 (2001).
2) S.M. Rouf, Y. Ohara-Nemoto, T. Hoshino, T. Fujiwara, T. Ono, and T.K. Nemoto, Biochimie, 95, 824 (2013).
3) S.M. Rouf, Y. Ohara-Nemoto, T. Ono, Y. Shimoyama, S. Kimura, and T.K. Nemoto, FEBS Open Bio, 3, 177 (2013).

–5 –Glycopeptides
Big Angiotensin-25
CodeCompoundPrice:Yen

24009-sNew

Big Angiotensin-25 (Human)
Bang-25-20

(Trifluoroacetate Form)

Vial

0.1 mg20,000

Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-[O- β -D -Galactopyranosyl-(1→ 4)-O-2acetamido-2-deoxy-β-D-glucopyranosyl-(1→2)-O-α-D-mannopyranosyl-(1→3)-[O-β-Dgalactopyranosyl-(1→4)-O-2-acetamido-2-deoxy-β-D-glucopyranosyl-(1→2)-O-α-Dmannopyranosyl-(1 → 6)]-O- β -D -mannopyranosyl-(1 → 4)-O-2-acetamido-2-deoxy- β -D glucopyranosyl-(1 → 4)-N-2-acetamido-2-deoxy- β-D -glucopyranosyl-(1 → 4)]-Asn-Glu-Ser-ThrCys(Cys)-Glu-Gln-Leu-Ala-Lys-Ala-Asn(M.W. 4677.9)

C195H307N43O85S2

Synthetic Product

Glycosylated Novel Endogenous Angiotensin Family Peptide
OH OH
O

HO

HO
O
HO
OH

O
AcNH
HO
HO
HO

O
O
O
HO
O

OH OH
O HO
HO
O
OH HO

HO
HO
HO
O

O

OH
O

HO
O
HO

HO
O
HO
AcNH
O

O

NH

AcNH
O

O

AcNH
Asp Arg Val Tyr Ile His Pro Phe His Leu Val Ile His N
H

Cys
Glu Ser Thr Cys Glu Gln Leu Ala Lys Ala Asn
O

Since the discovery of the longer form of angiotensin I (Human) (Code 4007) in rat, named proangiotensin12 (Rat) (Code 4439-v), Professor Kitamura of University of Miyazaki has endeavored to find the longer form ofangiotensin family peptide(s) in humans. As a result, he clarified that such peptides in humans are not a 12amino acid residue peptide corresponding to proangiotensin-12 (Rat), but rather a 25 amino acid residue
peptide called big angiotensin-25 (Human)1).
Big angiotensin-25 (Human) was isolated from urine as a major peptide when surveyed using an antibody
raised against the N-terminal portion of angiotensin II. Structure analysis revealed that the primary structure of
big angiotensin-25 (Human) is comprised of the first 25 amino acid residues of angiotensinogen and there exists
two modifications in the sequence: i) N-glycosylation by 9-mer sugar at Asn14 in the typical N-glycosylation
motif, Asn-Glu-Ser and ii) attachment of Cys on Cys18 through disulfide linkage. In collaboration with Professor
Kitamura, we have succeeded in synthesizing big angiotensin-25 (Human) and confirmed that the native andsynthetic big angiotensin-25 (Human) elute at the identical retention time on reversed phase-HPLC1,2).
Interestingly, big angiotensin-25 (Human) is cleaved rapidly by chymase, directly providing angiotensin II,
whereas it is slowly cleaved by renin (an enzyme generating angiotensin I). Other experimental results showthat big angiotensin-25 (Human) immunoreactivity is located in various tissues in humans such as kidney andheart, among others. Big angiotensin-25 (Human) is suggested to be a precursor of tissue angiotensin II.
Chemically synthesized big angiotensin-25 (Human), available now, will help to unravel the in vivo
functional roles of this particular form of the angiotensin family peptide.
1) S. Nagata, K. Hatakeyama, M. Asami, M. Tokashiki, H. Hibino, Y. Nishiuchi, K. Kuwasako, J. Kato, Y. Asada,and K. Kitamura, Biochem. Biophys. Res. Commun., 441, 757 (2013).
(Original; Structure & Enzymatic Generation of Angiotensin II).
2) H. Hibino, S. Nagata, K. Hatakeyama, M. Asami, M. Tokashiki, K. Kuwasako, J. Kato, Y. Asada, K. Kitamura,and Y. Nishiuchi, Peptide Science 2013, 50, 151 (2014). (Chem. Synthesis)

–6 –

SGP
Code

Compound

24010

Sialylglycopeptide
Bulk
5 mg
30,000
SGP (α2,6)
Lys-Val-Ala-[O-(5-Acetamido-3,5-dideoxy-D-glycero-α-D-galacto-2nonulopyranosylonic acid)-(2→6)-O-β-D-galactopyranosyl-(1→4)-O-2-acetamido-2-deoxyβ-D-glucopyranosyl-(1→2)-O-α-D-mannopyranosyl-(1→3)-[O-(5-acetamido-3,5dideoxy-D-glycero-α-D-galacto-2-nonulopyranosylonic acid)-(2→6)-O-β-Dgalactopyranosyl-(1→4)-O-2-acetamido-2-deoxy-β-D-glucopyranosyl-(1→2)-O-α-Dmannopyranosyl-(1→6)]-O-β-D-mannopyranosyl-(1→4)-O-2-acetamido-2-deoxy-β-Dglucopyranosyl-(1→4)-N-2-acetamido-2-deoxy-β-D-glucopyranosyl]-(1→4)-Asn-Lys-Thr

New

-20

Price:Yen(M.W. 2865.8) C112H189N15O70
Purity ≧95.0% (HPLC)[189035-43-6]

Natural product isolated from egg yolk

HO OH
HO
AcHN

O
HO

CO2H
O
OH
HO

HO
O
HO
OH

O

O

O

AcNH
HO
HO
HO

O
O
HO
O

HO OH

CO2H
O
HO
O
AcHN
OH
HO
HO

HO
O
HO
OH
O

HO
HO
HO
O
AcNH

O
O

OH HO
O
O
HO

HO
O
HO
AcNH
O

O
AcNH

Lys Val Ala N
H

H
N

O

O

Lys Thr

1) A. Seko, M. Koketsu, M. Nishizono, Y. Enoki, H.R. Ibrahim, L.R. Juneja, M. Kim, and T. Yamamoto,
Biochim. Biophys. Acta, 1335, 23 (1997).

Fmoc-Asn with 11 or 9 saccharide derivatives will be also available by custom service.

–7 –peptide28̲3小冊子 p.9 [コンポジット] [100%x100%]2015/3/4 19:52

受託サービス
受託サービス

詳しくは、弊社 Website をご覧ください

http://www.peptide.co.jp/custom

ペプチド合成受託合成

成功率 ＞99% ！

多くの実績に裏付けされた信頼のペプチド合成受託サービスです。

❶

ご希望のペプチド（Cys 含有ペプチドも含む）
2-200 残基（200 残基を越える場合も可能です。ご相談下さい）

❷
❸
❹
❺
❻
❼
❽

各種酵素基質（MCA, AFC, p NA, その他の蛍光，発色基質など）
消光性蛍光基質（Nma-Dnp，MOCAc-Dnp，Dabcyl-EDANS の組合せなど）
酵素阻害剤（アルデヒド，フルオロメチルケトン，クロロメチルケトン，ボロン酸誘導体など）
ジスルフィド結合含有ペプチド（1 組，2 組，3 組以上，分子内，分子間）
環状ペプチドおよび枝分かれペプチド
鎖状および環状デプシペプチド
糖ペプチド［Asn（GlcNAc）, Ser/Thr（GalNAc）, Ser/Thr（GlcNAc）, Ser/Thr（Gal-GalNAc）,
Ser/Thr（Neu-Gal-GalNAc）, 1-Deoxyfructosyl 含有ペプチドなど］

❾
❿
⓫
⓬
⓭
⓮
⓯
⓰
⓱
⓲
⓳
⓴

リン酸化ペプチド［Ser（PO3H2），Thr（PO3H2），Tyr（PO3H2）誘導体］
フォスファターゼ抵抗性リン酸化ペプチドミミック（Ser, Thr, Tyr, His, Asp 対応）
硫酸化ペプチド［Tyr（SO3H）］
蛍光標識ペプチド（FITC, Rhodamine, BODIPY, DY- シリーズなど 380 nm-730 nm に対応）
13

15

2

安定同位体ラベルアミノ酸含有ペプチド（ C， N， H など）
PEG 化（分子量 150 〜 4 万まで , N 末端 , C 末端 , 側鎖）
フォトアフィニティ用ラベル化（N3, Benzophenone, Diazirine など）
細胞膜透過性修飾（Tat, オリゴアルギニン , Penetratin など）
非天然アミノ酸含有ペプチド（ハイプシン , システインスルフィン酸など他多数）
アミノ基修飾（Biotinyl 化 , Myristoyl 化 , Palmitoyl 化 , Methyl 化 , Malonyl 化など種々の修飾）
チオール基修飾（Farnesyl 化，Geranyl 化，Palmitoyl 化など）
水酸基修飾（Octanoyl 化 , Palmitoyl 化 , Palmitoleoyl 化など）
ペプチド結合の修飾（還元型 , スタチン型など）
ペプチドアルコール
アミノ酸誘導体 , 保護ペプチドその他

受 託 合 成 量： 標準 10mg-25mg から g、kg オーダーまで承ります。（お見積り依頼の際に、ご相談下さい）
納期： 配列、修飾、難度、合成量により異なります（最短 1 週間〜）
個別お見積いたしますのでご用命下さい。

保 証 純 度： 通常、トリフルオロ酢酸塩でご提供いたします。
規格（1）HPLC で検定：90% 以上（精製品）（2）HPLC で検定：95% 以上（精製品）（3）HPLC で検定：99% 以上（精製品）など

通常、HPLC チャート、アミノ酸分析結果、質量分析結果を添付いたします。
その他の分析項目につきましてはご相談させていただきます。
価格： 個別にお見積りいたしますので、E-mail、あるいは FAX にてご用命下さい。

8 

peptide28̲3小冊子 p.10 [コンポジット] [100%x100%]2015/3/4 19:52

ペプチド医薬品合成（GMP）
弊社は、医薬品製造業許可を取得しており、医薬品原薬および原薬中間体の製造が可能です。
GMP 対応、治験薬 GMP 対応など個別にご相談させていただきます。
現在、ペプチド医薬品の基礎研究から上市後の受託製造まで、トータルなサービスのご提供に取り組んでいます。高品質なペプチド原薬をあらゆる場面でご提供できますので、お気軽にお問い合わせ下さい。

基礎研究

非臨床試験

臨床研究

治験

薬事申請

上市

糖鎖関連合成糖を母体とした有機化合物から九糖まで実績多数

単糖・オリゴ糖

修飾糖

蛍光標識糖

糖脂質

グリコサミノグリカン
フラグメント

各種糖アナログ

安定同位体
ラベル糖
脂

糖ヌクレオチド質

糖化最終産物抗体 ( ポリクローナル ) 作製
エピトープ選択抗原ペプチドの合成

コンジュゲート作製

抗体作製

抗体の精製

抗体の修飾

株式会社 ペプチド研究所 受託サービス窓口〒 567-0085 大阪府茨木市彩都あさぎ 7-2-9
電話：072-643-4343（直通） FAX：072-643-4422
E-mail：custom@peptide.co.jp http://www.peptide.co.jp/custom

カタログ製品に関して
電話 : 072-643-4480
E-mail: sales@peptide.co.jp
受託サービスに関して
電話 : 072-643-4343
E-mail: custom@peptide.co.jp