Enzyme Substrates and Related Peptides …………… 204
FRETS (Peptide) Library ……………………………… 232
Peptide Tools …………………………………………… 239
Enzymes ………………………………………………… 243
Polypeptides …………………………………………… 244
Oligopeptides ………………………………………… 245– 203 –

Enzyme Substrates

Enzyme Substrates
and Related
PeptidesEnzyme Substrates and Related Peptides
The purity grade of the following products is guaranteed according to our Purity Criteria on page III and IV(XIV and XV).
CodeCompoundGrade

Price:Yen

AAF-CMK See Code 3202 Ala-Ala-Phe-CH2Cl on page 182
AAFP See Code 3197 4-Methoxyphenylazoformyl-Phe on page 219

3078

Ac-Arg-OMe • HCl

2～10

Acetyl-L-arginine methyl ester monohydrochloride(M.W. 230.26 • 36.46)

B
C9H18N4O3 • HCl

1g
5g

3,200
8,800

[1784-05-0]

Substrate for C1r1) R.B. Sim, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, ed.), Academic Press,
New York, 1981, pp. 26-42.

Ac-Asp-Asn-Leu-Asp-H (aldehyde) See Code 3221 on page 178

3220-v-20

A

Ac-Asp-Asn-Leu-Asp-MCA[Ac-DNLD-MCA]

Vial

5 mg

7,000

5 mg

9,000

Acetyl-L-aspartyl-L-asparaginyl-L-leucyl-L-aspartic acidα-(4-methylcoumaryl-7-amide)(M.W. 674.66)

C30H38N6O12

Synthetic ProductSelective Substrate for Caspase-3 Designed by in silico Screening System
1) S. Tanuma, A. Yoshimori, and R. Takasawa, Biol. Pharm. Bull., 27, 968 (2004).

Ac-Asp-Gln-Thr-Asp-H (aldehyde) See Code 3194 on page 178

3193-v-20

A

Ac-Asp-Gln-Thr-Asp-MCA[Ac-DQTD-MCA]

Vial

Acetyl-L-aspartyl-L-gutaminyl-L-threonyl-L-aspartic acidα-(4-methylcoumaryl-7-amide)(M.W. 676.63)

C29H36N6O13

Substrate for Caspase-7/3(Deduced from the Cleavage Site of Focal Adhesion Kinase and Gelsolin)
1) L.-P. Wen, J.A. Fahrni, S. Troie, J.-L. Guan, K. Orth, and G.D. Rosen, J. Biol. Chem., 272, 26056 (1997).
2) S. Kothakota, T. Azuma, C. Reinhard, A. Kippel, J. Tang, K. Chu, T.J. McGarry, M.W. Kirschner, K. Koths,
D.J. Kwiatkowski, and L.T. Williams, Science, 278, 294 (1997).

– 204 –

Enzyme Substrates and Related Peptides (continued)
Code

CompoundGrade

Price:Yen

Ac-Asp-Glu-Val-Asp-H (aldehyde) See Code 3172 on page 178

3171-v-20

A

Ac-Asp-Glu-Val-Asp-MCA[Ac-DEVD-MCA]

Vial

5 mg

7,000

Acetyl-L-aspartyl-L-glutamyl-L-valyl-L-aspartic acidα-(4-methylcoumaryl-7-amide)(M.W. 675.64)

C30H37N5O13[169332-61-0]

Substrate for Caspase-3/7/8

Ac-Asp-Met-Gln-Asp-H (aldehyde) See Code 3192 on page 179

3227-v

New-20

Ac-Glu-Ser-Glu-Asn-MCA
A
Vial
5 mg
[Ac-ESEN-MCA]
Acetyl-L-glutamyl-L-seryl-L-glutamyl-L-asparagine α-(4-methylcoumaryl-7-amide)(M.W. 676.63)

10,000C29H36N6O13

Substrate for Vacuolar Processing Enzyme (VPE)
1) M. Kuroyanagi, M. Nishimura, and I. Hara-Nishimura, Plant Cell Physiol., 43, 143 (2002).
2) N. Hatsugai, M. Kuroyanagi, K. Yamada, T. Meshi, S. Tsuda, M. Kondo, M. Nishimura, and I. Hara-Nishimura,
Science, 305, 855 (2004).
3) M. Kuroyanagi, K. Yamada, N. Hatsugai, M. Kondo, M. Nishimura, and I. Hara-Nishimura, J. Biol. Chem., 280,
32914 (2005).

3058
2～10

Ac-Gly-Lys-OMe • AcOH
[AGLME]

A

0.1 g
1g

2,200
8,300

Acetylglycyl-L-lysine methyl ester(M.W. 259.30• 60.05)

C11H21N3O4 • CH3COOH[14752-92-2]

Substrate for u-PA (Urokinase) and C1s
1) P.L. Walton, Biochim. Biophys. Acta, 132, 104 (1967).
2) N. Miwa, Y. Obata, and A. Suzuki, Biochem. Biophys. Res. Commun., 112, 754 (1983).
3) R.B. Sim, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, ed.), Academic Press,
New York, 1981, pp. 26-42.

Ac-Ile-Glu-Thr-Asp-H (aldehyde) See Code 3196 on page 179

3195-v-20

A

Ac-Ile-Glu-Thr-Asp-MCA[Ac-IETD-MCA]

Vial

5 mg

10,000

Acetyl-L-isoleucyl-L-glutamyl-L-threonyl-L-aspartic acidα-(4-methylcoumaryl-7-amide)(M.W. 675.68)

C31H41N5O12

Substrate for Procaspase-3 Cleaving Enzyme (Caspase-8/6 and Granzyme B)(Deduced from the Cleavage Site of Procaspase-3)
1) N.A. Thornberry, T.A. Rano, E.P. Peterson, D.M. Rasper, T. Timkey, M. Garcia-Calvo, V.M. Houtzager,
P.A. Nordstrom, S. Roy, J.P. Vaillancourt, K.T. Chapman, and D.W. Nicholson, J. Biol. Chem., 272, 17907 (1997).

Ac-Leu-Glu-His-Asp-H (aldehyde) See Code 3199 on page 179– 205 –

Enzyme Substrates

1) D.W. Nicholson, A. Ali, N.A. Thornberry, J.P. Vaillancourt, C.K. Ding, M. Gallant, Y. Gareau, P.R. Griffin,
M. Labelle, Y.A. Lazebnik, N.A. Munday, S.M. Raju, M.E. Smulson, T.-T. Yamin, V.L. Yu, and D.K. Miller,
Nature, 376, 37 (1995).
2) N.A. Thornberry, T.A. Rano, E.P. Peterson, D.M. Rasper, T. Timkey, M. Garcia-Calvo, V.M. Houtzager,
P.A. Nordstrom, S. Roy, J.P. Vaillancourt, K.T. Chapman, and D.W. Nicholson, J. Biol. Chem., 272, 17907 (1997).

Enzyme Substrates and Related Peptides (continued)
Code

Compound3198-v

Ac-Leu-Glu-His-Asp-MCA[Ac-LEHD-MCA]

-20

Grade
A

Price:Yen
Vial

5 mg

10,000

Acetyl-L-leucyl-L-glutamyl-L-histidyl-L-aspartic acidα-(4-methylcoumaryl-7-amide)(M.W. 711.72)

C33H41N7O11[292633-16-0]

Substrate for Caspase-91) N.A. Thornberry, T.A. Rano, E.P. Peterson, D.M. Rasper, T. Timkey, M. Garcia-Calvo, V.M. Houtzager,
P.A. Nordstrom, S. Roy, J.P. Vaillancourt, K.T. Chapman, and D.W. Nicholson, J. Biol. Chem., 272, 17907 (1997).

3185-v-20

AA

Ac-Lys-Thr-Lys-Gln-Leu-Arg-MCA[Ac-KTKQLR-MCA]

Vial

5 mg

12,000

Acetyl-L-lysyl-L-threonyl-L-lysyl-L-glutaminyl-L-leucyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 972.14)

C45H73N13O11

Substrate for Hepatocyte Growth Factor-Activator (HGF-A)
1) K. Mizuno, Y. Tanoue, I. Okano, T. Harano, K. Takada, and T. Nakamura, Biochem. Biophys. Res. Commun.,
198, 1161 (1994).

3006

Ac-Phe-OEt

2～10

Acetyl-L-phenylalanine ethyl ester(M.W. 235.28)

C13H17NO3

0.1 g
1g
5g

1,600
2,300
5,000

AA

0.1 g
1g

1,800
4,600

[2361-96-8]

3034

Ac-Trp-OEt

2～10

Acetyl-L-tryptophan ethyl ester(M.W. 274.32)

AA

C15H18N2O3[2382-80-1]

Ac-Trp-Glu-His-Asp-H (aldehyde) See Code 3187 on page 180

3186-v-20

A

Ac-Trp-Glu-His-Asp-MCA[Ac-WEHD-MCA]

Vial

5 mg

10,000

Acetyl-L-tryptophyl-L-glutamyl-L-histidyl-L-aspartic acidα-(4-methylcoumaryl-7-amide)(M.W. 784.77)

C38H40N8O11[189275-74-9]

Substrate for Caspase-1/14
1) T.A. Rano, T. Timkey, E.P. Peterson, J. Rotonda, D.W. Nicholson, J.W. Becker, K.T. Chapman, and N.A. Thornberry,Chem. Biol., 4, 149 (1997).
2) N.A. Thornberry, T.A. Rano, E.P. Peterson, D.M. Rasper, T. Timkey, M.Garcia-Calvo, V.M. Houtzager,
P.A. Nordstrom, S. Roy, J.P. Vaillancourt, K.T. Chapman, and D.W. Nicholson, J. Biol. Chem., 272, 17907 (1997).
3) J. Mikolajczyk, F.L. Scott, S. Krajewski, D.P. Sutherlin, and G.S. Salvesen, Biochemistry, 43, 10560 (2004).

3009

Ac-Tyr-NH2

2～10

Acetyl-L-tyrosine amide(M.W. 222.24)

A
C11H14N2O3[1948-71-6]– 206 –

0.1 g
1g

1,700
3,300

Enzyme Substrates and Related Peptides (continued)
Code

Compound

Grade

3008

Ac-Tyr-OEt • H2O

AA

2～10

Acetyl-L-tyrosine ethyl ester monohydrate(M.W. 251.28 • 18.02)

C13H17NO4 • H2O

Price:Yen
0.1 g
1g

1,700
2,600

[840-97-1]

Substrate for Chymotrypsin and C1s
1) P.E. Wilcox, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, eds.),
Academic Press, New York, 1970, pp. 64-108.
2) R.B. Sim, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, ed.), Academic Press,
New York, 1981, pp. 26-42.

Ac-Tyr-Val-Ala-Asp-H (aldehyde) See Code 3165 on page 180

3161-v-20

A

Ac-Tyr-Val-Ala-Asp-MCA[Ac-YVAD-MCA]

Vial

5 mg

7,000

Acetyl-L-tyrosyl-L-valyl-L-alanyl-L-aspartic acidα-(4-methylcoumaryl-7-amide)(M.W. 665.69)

C33H39N5O10[149231-65-2]

Substrate for Caspase-1
1) N.A. Thornberry, H.G. Bull, J.R. Calaycay, K.T. Chapman, A.D. Howard, M.J. Kostura, D.K. Miller, S.M. Molineaux,
J.R. Weidner, J. Aunins, K.O. Elliston, J.M. Ayala, F.J. Casano, J. Chin, G.J.-F. Ding, L.A. Egger, E.P. Gaffney,
G. Limjuco, O.C. Palyha, S.M. Raju, A.M. Rolando, J.P. Salley, T.-T. Yamin, T.D. Lee, J.E. Shively, M. MacCross,
R.A. Mumford, J.A. Schmidt, and M.J. Tocci, Nature, 356, 768 (1992).

3146

Ac-Tyr-Val-Gly

2～10

Acetyl-L-tyrosyl-L-valylglycine(M.W. 379.41)

AA

0.1 g
1g

7,800
54,400

C18H25N3O6

Substrate for α -Amidating Enzyme
Ac-Tyr-Val-Lys-Asp-H (aldehyde) See Code 3166 on page 181
Ac-Val-Asp-Val-Ala-Asp-H (aldehyde) See Code 3204 on page 181

3203-v-20

A

Ac-Val-Asp-Val-Ala-Asp-MCA[Ac-VDVAD-MCA]

Vial

5 mg

10,000

Acetyl-L-valyl-L-aspartyl-L-valyl-L-alanylL-aspartic acid α-(4-methylcoumaryl-7-amide)(M.W. 716.74)

C33H44N6O12

Substrate for Caspase-2
1) R.V. Talanian, C. Quinlan, S. Trautz, M.C. Hackett, J.A. Mankovich, D. Banach, T. Ghayur, K.D. Brady, andW.W. Wong, J. Biol. Chem., 272, 9677 (1997).

Ac-Val-Glu-Ile-Asp-H (aldehyde) See Code 3182 on page 181

3181-v-20

A

Ac-Val-Glu-Ile-Asp-MCA[Ac-VEID-MCA]

Vial

5 mg

7,000

Acetyl-L-valyl-L-glutamyl-L-isoleucyl-L-aspartic acidα-(4-methylcoumaryl-7-amide)(M.W. 673.71)

C32H43N5O11[219137-97-0]

Substrate for Caspase-6
1) A. Takahashi, P.J. Goldschmidt-Clermont, E.S. Alnemri, T. Fernandes-Alnemri, K. Yoshizawa-Kumagaye,
K. Nakajima, M. Sasada, G.G. Poirier, and W.C. Earnshaw, Exp. Cell Res., 231, 123 (1997).
2) A. Takahashi, H. Hirata, S. Yonehara, Y. Imai, K-K. Lee, R.W. Moyer, P.C. Turner, P.W. Mesner, T. Okazaki,
H. Sawai, S. Kishi, K. Yamamoto, M. Okuma, and M. Sasada, Oncogene, 14, 2741 (1997).

– 207 –

Enzyme Substrates

Ac-Tyr-Val-Ala-Asp-CH2Cl See Code 3180 on page 180

Enzyme Substrates and Related Peptides (continued)
AGLME See Code 3058 Ac-Gly-Lys-OMe • AcOH on page 205
Ala-Ala-Phe-CH2Cl See Code 3202 on page 182

CodeCompoundGrade3201-v

Ala-Ala-Phe-MCA

AA

-20

(Hydrochloride Form)

Price:Yen
Vial

5 mg

4,000

L-Alanyl- L-alanyl-L-phenylalanine 4-methylcoumaryl-7-amide(M.W. 464.51)

C25H28N4O5[62037-41-6]

Substrate for Tripeptidyl Peptidase II (Component of Giant Protease with Some
Proteasome Function)
1) R. Glas, M. Bogyo, J.S. McMaster, M. Gaczynska, and H.L. Ploegh, Nature, 392, 618 (1998).
2) E. Geier, G. Pfeifer, M. Wilm, M. Lucchiari-Hartz, W. Baumeister, K. Eichmann, and G. Niedermann, Science,
283, 978 (1999).

4166
-20

Ala-Arg-Gly-Ile-Lys-Gly-Ile-Arg-Gly-PheSer-Gly • 3AcOH • 5H2O
[Lysine Hydroxylase Substrate L-1]
(M.W. 1218.4 • 180.16 • 90.08)

AA

25 mg

46,000C53H91N19O14 • 3CH3COOH • 5H2O

Substrate for Lysine Hydroxylase
1) K.I. Kivirikko, K. Shudo, S. Sakakibara, and D.J. Prockop, Biochemistry, 11, 122 (1972).

3147-v

Ala-MCA-20

(Tosylate Form)

AA

Vial

5 mg

2,700

L-Alanine 4-methylcoumaryl-7-amide(M.W. 246.26)

C13H14N2O3[77471-41-1]

Substrate for Aminopeptidase
3068

Ala-pNA

2～10

L-Alanine p-nitroanilide(M.W. 209.20)

AA
C9H11N3O3

0.1 g
1g
5g

[1668-13-9]

2,100
6,400
27,200Substrate for Aminopeptidase
1) G. Peleiderer, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, eds.),
Academic Press, New York, 1970, pp. 514-521.

3085
2～10

β-Alanyl-L-Histidine[Carnosine](M.W. 226.23)

AA

C9H14N4O3

AMC

-20

7-Amino-4-methylcoumarinAA
C10H9NO2

2,800
6,800

Vial

5 mg

2,000

Vial

0.5 mg

7,200[305-84-0]

3099-v(M.W. 175.18)

1g
5g[26093-31-2]

Reference Compound for Analysis with Peptidyl-MCAs
4184-v-20

Arg-Arg-Leu-Ile-Glu-Asp-Ala-Glu-Tyr-AlaAla-Arg-Gly[RR-SRC](M.W. 1519.7)

C64H106N22O21

AA[81156-93-6]

Substrate for Tyrosine Protein-Kinase
1) J.E. Casnellie, M.L. Harrison, L.J. Pike, K.E. Hellstro
m, and E.G. Krebs, Proc. Natl. Acad. Sci. U.S.A., 79, 282 (1982).

– 208 –

Enzyme Substrates and Related Peptides (continued)
Code

CompoundGrade3113-v

Arg-MCAAA-20

(Hydrochloride Form)

Price:Yen
Vial

5 mg

3,500

L-Arginine 4-methylcoumaryl-7-amide(M.W. 331.37)

C16H21N5O3[65286-27-3]

Substrate for Cathepsin H
1) Y. Kanaoka, T. Takahashi, H. Nakayama, K. Takada, T. Kimura, and S. Sakakibara, Chem. Pharm. Bull.,25, 3126 (1977).

-20

Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-LeuVal-Ile-His(M.W. 1645.9)

C79H116N22O17

A

Vial

0.5 mg4,300[82048-97-3]

Substrate for Renin
1) D.A. Tewksbury, R.A. Dart, and J. Travis, Biochem. Biophys. Res. Commun., 99, 1311 (1981).

BAEE See Code 3001 Bz-Arg-OEt • HCl on page 213
DL-BAPAL-BAPA

See Code 3013 Bz-DL-Arg-pNA • HCl on page 213
See Code 3057 Bz-L-Arg-pNA • HCl on page 214

Biotinyl-Asp-Glu-Val-Asp-H (aldehyde) See Code 3173 on page 239
Biotinyl-ω-Agatoxin IVA See Code 3402 on page 239

3144-v

Boc-Ala-Gly-Pro-Arg-MCA-20

t-Butyloxycarbonyl-L-alanylglycyl-L-prolylL-arginine 4-methylcoumaryl-7-amide(M.W. 656.73)

C31H44N8O8

A

Vial

5 mg

5,700

[118850-78-5]

Substrate for ANP(Rat) Precursor Processing Enzyme
1) T. Imada, R. Takayanagi, and T. Inagami, Biochem. Biophys. Res. Commun., 143, 587 (1987).
2) T. Imada, R. Takayanagi, and T. Inagami, Biol. Chem. Hoppe-Seyler Suppl., 369, 113 (1988).

3155-v

Boc-Arg-Val-Arg-Arg-MCA-20

t-Butyloxycarbonyl-L-arginyl-L-valylL-arginyl- L-arginine 4-methylcoumaryl-7-amide(M.W. 842.99)

A

Vial

5 mg

6,300

C38H62N14O8

Substrate for Furin
1) K. Hatsuzawa, K. Murakami, and K. Nakayama, J. Biochem., 111, 296 (1992).
2) K. Hatsuzawa, M. Nagahara, S. Takahashi, K. Takada, K. Murakami, and K. Nakayama, J. Biol. Chem., 267, 16094(1992).

3139-v

Boc-Asp(OBzl)-Pro-Arg-MCA-20

t-Butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]L-prolyl- L-arginine 4-methylcoumaryl-7-amide(M.W. 733.81)

C37H47N7O9

AA

Vial

5 mg

5,000

[113866-00-5]

Substrate for α -Thrombin
1) S. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara,
Eur. J. Biochem., 172, 17 (1988).

– 209 –

Enzyme Substrates

4133-v

Enzyme Substrates and Related Peptides (continued)
Code

Compound3135-v

Boc-Gln-Ala-Arg-MCA-20

t-Butyloxycarbonyl-L-glutaminyl-L-alanyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 630.69)

Grade

C29H42N8O8

A

Price:Yen
Vial

5 mg

5,000

[113866-20-9]

Substrate for Trypsin
1) S. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara,
Eur. J. Biochem., 172, 17 (1988).

3122-v

Boc-Gln-Arg-Arg-MCA-20

t-Butyloxycarbonyl-L-glutaminyl-L-arginyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 715.80)

C32H49N11O8

A

Vial

5 mg

5,400

[109376-05-8]

Substrate for Carboxyl Side of Paired Basic Residue Cleaving Enzyme
1) K. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun., 144, 807 (1987).

3136-v

Boc-Gln-Gly-Arg-MCA-20

t-Butyloxycarbonyl-L-glutaminylglycyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 616.67)

A

Vial

5 mg

5,000

C28H40N8O8

Substrate for Factor XIIa
1) S. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara,
Eur. J. Biochem., 172, 17 (1988).

3151

Boc-Gln-Pro

2～10

t-Butyloxycarbonyl-L-glutaminyl-L-proline(M.W. 343.38)

AA
C15H25N3O6

0.1 g
1g

3,200
15,000[2419-99-0]

Substrate for Peptidoglutaminase
1) J.S. Hamada and W.E. Marshall, J. Food Sci., 53, 1132 (1988).

3105-v

Boc-Glu-Lys-Lys-MCA-20

t-Butyloxycarbonyl-L-glutamyl-L-lysyl-L-lysine
4-methylcoumaryl-7-amide(M.W. 660.76)

C32H48N6O9

A

Vial

5 mg

6,000

[73554-85-5]

Substrate for Plasmin
1) H. Kato, N. Adachi, Y. Ohno, S. Iwanaga, K. Takada, and S. Sakakibara, J. Biochem., 88, 183 (1980).

3134-v

Boc-Glu(OBzl)-Ala-Arg-MCA-20

t-Butyloxycarbonyl-[(2S)-2-amino-4-(benzyloxycarbonyl)butanoyl]L-alanyl- L-arginine 4-methylcoumaryl-7-amide(M.W. 721.80)

C36H47N7O9

AA

Vial

5 mg

5,000

[113866-16-3]

Substrate for Factor XIa
1) S. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara,
Eur. J. Biochem., 172, 17 (1988).

– 210 –

Enzyme Substrates and Related Peptides (continued)
Code

CompoundGrade3115-v

Boc-Glu(OBzl)-Gly-Arg-MCA-20

(Hydrochloride Form)A

Price:Yen
Vial

5 mg

5,000

t-Butyloxycarbonyl-[(2S)-2-amino-4-(benzyloxycarbonyl)butanoyl]glycylL-arginine 4-methylcoumaryl-7-amide(M.W. 707.77)

C35H45N7O9[73554-94-6]

1) S. Iwanaga, T. Morita, H. Kato, T. Harada, N. Adachi, T. Sugo, I. Maruyama, K. Takada, T. Kimura, and
S. Sakakibara, In, KININS-II: Biochemistry, Pathophysiology, and Clinical Aspects, (S. Fujii, H. Moriya, andT. Suzuki eds.), Plenum Publishing Co., 1979, pp.147-163.

3142-v

Boc-Gly-Arg-Arg-MCA-20

t-Butyloxycarbonylglycyl-L-arginyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 644.72)

C29H44N10O7

A

Vial

5 mg

5,400

[113866-14-1]

Substrate for Carboxyl Side of Paired Basic Residue Cleaving Enzyme
1) K. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun., 144, 807 (1987).

3143-v

Boc-Gly-Lys-Arg-MCA-20

t-Butyloxycarbonylglycyl-L-lysyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 616.71)

C29H44N8O7

A

Vial

5 mg

5,700

[109358-48-7]

Substrate for Carboxyl Side of Paired Basic Residue Cleaving Enzyme
1) K. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun., 144, 807 (1987).

3094-v

Boc-Ile-Glu-Gly-Arg-MCA-20

t-Butyloxycarbonyl-L-isoleucyl-L-glutamylglycylL-arginine 4-methylcoumaryl-7-amide(M.W. 730.81)

C34H50N8O10

A

Vial

5 mg

5,400

[65147-06-0]

Substrate for Factor Xa
1) T. Morita, H. Kato, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, J. Biochem., 82, 1495 (1977).

3140-v

Boc-Leu-Arg-Arg-MCA-20

t-Butyloxycarbonyl-L-leucyl-L-arginyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 700.83)

A

Vial

5 mg

5,400

C33H52N10O7

Substrate for Carboxyl Side of Paired Basic Residue Cleaving Enzyme and Proteasome
1) K. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun., 144, 807 (1987).
2) M. Aki, N. Shimbara, M. Takashina, K. Akiyama, S. Kagawa, T. Tamura, N. Tanahashi, T. Yoshimura, K. Tanaka, andA. Ichihara, J. Biochem., 115, 257 (1994).

3102-v

Boc-Leu-Gly-Arg-MCA-20

(Hydrochloride Form)

AA

Vial

5 mg

5,000

t-Butyloxycarbonyl-L-leucylglycyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 601.69)

C29H43N7O7[65147-09-3]

Substrate for Horseshoe Crab Clotting Enzyme
1) S. Iwanaga, T. Morita, T. Harada, S. Nakamura, M. Niwa, K. Takada, T. Kimura, and S. Sakakibara, Haemostasis,
7, 183 (1978).

– 211 –

Enzyme Substrates2) S. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara,
Eur. J. Biochem., 172, 17 (1988).

Enzyme Substrates and Related Peptides (continued)
Code

Compound3141-v

Boc-Leu-Lys-Arg-MCA-20

t-Butyloxycarbonyl-L-leucyl-L-lysyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 672.82)

Grade

C33H52N8O7

A

Price:Yen
Vial

5 mg

5,700

[109358-47-6]

Substrate for Carboxyl Side of Paired Basic Residue Cleaving Enzyme
1) K. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, and H. Matsuo, Biochem. Biophys. Res. Commun., 144, 807 (1987).

3112-v

Boc-Leu-Ser-Thr-Arg-MCA-20

t-Butyloxycarbonyl-L-leucyl-L-seryl-L-threonylL-arginine 4-methylcoumaryl-7-amide(M.W. 732.82)

C34H52N8O10

A

Vial

5 mg

6,000

[73554-93-5]

Substrate for Activated Protein C1) Y. Ohno, H. Kato, T. Morita, S. Iwanaga, K. Takada, S. Sakakibara, and J. Stenflo, J. Biochem., 90, 1387 (1981).

3125

Boc-Leu-Ser-Thr-Arg-pNA

2～10

t-Butyloxycarbonyl-L-leucyl-L-serylL-threonyl-L-arginine p-nitroanilide(M.W. 695.76)

A

25 mg
100 mg20,00060,000

5 mg

5,000

C30H49N9O10

Substrate for Activated Protein C
3106-v

Boc-Leu-Thr-Arg-MCA-20

t-Butyloxycarbonyl-L-leucyl-L-threonylL-arginine 4-methylcoumaryl-7-amide(M.W. 645.75)

A

Vial

C31H47N7O8

Substrate for Factor VIIa-Tf
1) Y. Shigematsu, T. Miyata, S. Higashi, T. Miki, J.E. Sadler, and S. Iwanaga, J. Biol. Chem., 267, 21329 (1992).

3107-v

Boc-Phe-Ser-Arg-MCA-20

t-Butyloxycarbonyl-L-phenylalanyl-L-serylL-arginine 4-methylcoumaryl-7-amide(M.W. 665.74)

C33H43N7O8

AA

Vial

5 mg

5,000

[73554-90-2]

Substrate for Trypsin, Tryptase, 73K Protease, and Arg-Gingipain
1) S. Iwanaga, T. Morita, H. Kato, T. Harada, N. Adachi, T. Sugo, I. Maruyama, K. Takada, T. Kimura, and
S. Sakakibara, In, KININS-II: Biochemistry, Pathophysiology, and Clinical Aspects, (S. Fujii, H. Moriya, andT. Suzuki eds.), Plenum Publishing Co., 1979, pp.147-163.
2) M. Muramatsu, T. Itoh, M. Takei, and K. Endo, Biol. Chem. Hoppe-Seyler, 369, 617 (1988).
3) A. Molla, T. Yamamoto, and H. Maeda, J. Biochem., 104, 616 (1988).

3104-v

Boc-Val-Leu-Lys-MCA-20

t-Butyloxycarbonyl-L-valyl-L-leucyl-L-lysine
4-methylcoumaryl-7-amide(M.W. 615.76)

C32H49N5O7

A

Vial

5 mg

5,700

[73554-84-4]

Substrate for Plasmin and Calpain
1) H. Kato, N. Adachi, Y. Ohno, S. Iwanaga, K. Takada, and S. Sakakibara, J. Biochem., 88, 183 (1980).
2) T. Sasaki, T. Kikuchi, N. Yumoto, N. Yoshimura, and T. Murachi, J. Biol. Chem., 259, 12489 (1984).

– 212 –

Enzyme Substrates and Related Peptides (continued)
Code

CompoundGrade3093-v

Boc-Val-Pro-Arg-MCA

AA

-20

t-Butyloxycarbonyl-L-valyl-L-prolyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 627.73)

C31H45N7O7

Price:Yen
Vial

5 mg

4,800

[65147-04-8]

Substrate for α -Thrombin
1) T. Morita, H. Kato, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, J. Biochem., 82, 1495 (1977).
2) S. Kawabata, T. Morita, S. Iwanaga, and H. Igarashi, J. Biochem., 97, 1073 (1985).

Bz-Ala-OMe

2～10

Benzoyl-L-alanine methyl ester(M.W. 207.23)

AA
C11H13NO33092-v

Bz-Arg-MCA-20

(Hydrochloride Form)

0.1 g
1g

1,900
5,200

[7244-67-9]

A

Vial

5 mg

3,500

Benzoyl-L-arginine 4-methylcoumaryl-7-amide(M.W. 435.48)

C23H25N5O4[83701-04-6]

Substrate for Trypsin
1) Y. Kanaoka, T. Takahashi, H. Nakayama, K. Takada, T. Kimura, and S. Sakakibara, Chem. Pharm. Bull.,25, 3126 (1977).

3002

Bz-Arg-NH2 • HCl • H2O

2～10

Benzoyl-L-arginine amide monohydrochloride monohydrate(M.W. 277.32 • 36.46 • 18.02)

AA
C13H19N5O2 • HCl • H2O

1g
5g

2,700
6,900

[4299-03-0]

Substrate for Trypsin
1) K.A. Walsh, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, eds.),
Academic Press, New York, 1970, pp. 41-63.

3001
2～10

A

Bz-Arg-OEt • HCl[BAEE]
Benzoyl-L-arginine ethyl ester monohydrochloride(M.W. 306.36 • 36.46)

C15H22N4O3 • HCl

1g
5g
25 g

2,200
4,400
17,000[2645-08-1]

Substrate for Trypsin
1) K.A. Walsh, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, eds.),
Academic Press, New York, 1970, pp. 41-63.

3013
2～10

A

Bz-DL-Arg-pNA • HCl[DL-BAPA]
Benzoyl-DL-arginine p-nitroanilide monohydrochloride(M.W. 398.42 • 36.46)

C19H22N6O4•HCl

0.1 g
1g
5g

1,700
3,800
11,800[911-77-3]

Substrate for Trypsin-like Proteases
1) K.A. Thomas and R.A. Bradshaw, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, ed.),Academic Press, New York, 1981, pp. 609-620.
2) G.A. Grant, A.Z. Eisen, and R.A. Bradshaw, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80,(L. Lorand, ed.), Academic Press, New York, 1981, pp. 722-734.

– 213 –

Enzyme Substrates

3084

Enzyme Substrates and Related Peptides (continued)
Code

Compound

Grade

3057

Bz-L-Arg-pNA • HCl[L-BAPA]

AA

2～10

Benzoyl-L-arginine p-nitroanilide monohydrochloride(M.W. 398.42 • 36.46)

C19H22N6O4 • HCl

Price:Yen
0.1 g
1g
5g

2,600
9,800
37,000[21653-40-7]

Substrate for Trypsin-like Proteases and Papain
1) K.A. Walsh, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, eds.),
Academic Press, New York, 1970, pp. 41-63.
2) R. Arnon, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, eds.),
Academic Press, New York, 1970, pp. 226-244.
3) G.A. Grant, A.Z. Eisen, and R.A. Bradshaw, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80,(L. Lorand, ed.), Academic Press, New York, 1981, pp. 722-734.

3126
2～10

AA

Bz-Gly-Ala-Pro[Hippuryl-Alanyl-Proline]

0.1 g
1g

4,300
26,200

Benzoylglycyl-L-alanyl-L-proline(M.W. 347.37)

C17H21N3O5[73167-84-7]

Substrate for ACE (Angiotensin I Converting Enzyme)
1) H.S. Cheung, F.L. Wang, M.A. Ondetti, E.F. Sabo, and D.W. Cushman, J. Biol. Chem., 255, 401 (1980).

3059
2～10

Bz-Gly-Arg[Hippuryl-Arginine]

AA

0.1 g
1g

2,500
10,700

AA

0.1 g
1g

2,900
14,200

Benzoylglycyl-L-arginine(M.W. 335.36)

3128
2～10

C15H21N5O4[744-46-7]

Bz-Gly-Gly-Gly[Hippuryl-Glycyl-Glycine]
Benzoylglycylglycylglycine(M.W. 293.28)

C13H15N3O5[31384-90-4]

Substrate for ACE (Angiotensin I Converting Enzyme)
1) H.Y.T. Yang, E.G. Erdos, and Y. Levin, J. Pharmacol. Exp. Ther., 177, 291 (1971).
2) T. Nakajima, G. Oshima, H.S.J. Yeh, R. Igic, and E.G. Erdos, Biochim. Biophys. Acta, 315, 430 (1973).
3) G. Oshima, K. Nagasawa, and J. Kato, J. Biochem., 80, 477 (1976).

3064
2～10

Bz-Gly-His-Leu • H2O[Hippuryl-Histidyl-Leucine]

AA

0.1 g
1g

4,300
26,200

AA

0.1 g
1g

2,700
12,500

AA

0.1 g
1g
5g

1,600
2,300
5,400

Benzoylglycyl-L-histidyl-L-leucine(M.W. 429.47• 18.02)

C21H27N5O5 • H2O[31373-65-6]

Substrate for ACE (Angiotensin I Converting Enzyme)
1) D.W. Cushman and H.S. Cheung, Biochem. Pharmacol., 20, 1637 (1971).

3047
2～10

Bz-Gly-Lys[Hippuryl-Lysine]
Benzoylglycyl-L-lysine(M.W. 307.34)

C15H21N3O4[740-63-6]

3010

Bz-Tyr-OEt

2～10

Benzoyl-L-tyrosine ethyl ester(M.W. 313.35)

C18H19NO4[3483-82-7]

Substrate for Chymotrypsin
1) P.E. Wilcox, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, eds.),
Academic Press, New York, 1970, pp. 64-108.

– 214 –

Enzyme Substrates and Related Peptides (continued)
Code

Compound

Grade

3015

Bz-Tyr-pNA

A

2～10

Benzoyl-L-tyrosine p-nitroanilide(M.W. 405.40)

C22H19N3O5

Price:Yen
0.1 g
1g

2,700
10,800[6154-45-6]

Substrate for Chymotrypsin
1) G.A. Grant, A.Z. Eisen, and R.A. Bradshaw, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80,(L. Lorand, ed.), Academic Press, New York, 1981, pp. 722-734.

Carnosine See Code 3085 β-Alanyl-L-Histidine on page 192 and 208

3088-v

Dnp-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-20

2,4-Dinitrophenyl-L-glutaminylglycyl-L-isoleucylL-alanylglycyl-L-glutaminyl- D-arginine(M.W. 894.89)

B

Vial

2.5 mg8,800

C35H54N14O14

Reference Substrate for Collagenase Assay with Code 3087-v
1) Y. Masui, T. Takemoto, S. Sakakibara, H. Hori, and Y. Nagai, Biochem. Med., 17, 215 (1977).

3083-v

Dnp-Leu-Gly-Ile-Ala-Gly-Arg-NH2-20

2,4-Dinitrophenyl-L-leucylglycyl-L-isoleucylL-alanylglycyl-L-arginine amide(M.W. 750.80)

A

Vial

2.5 mg7,800

C31H50N12O10

Substrate for Serum Peptidase
1) Y. Masui, T. Takemoto, S. Sakakibara, H. Hori, and Y. Nagai, Biochem. Med., 17, 215 (1977).

3089

Dnp-Pro-Gln-Gly

2～10

2,4-Dinitrophenyl-L-prolyl-L-glutaminylglycine(M.W. 466.40)

C18H22N6O9

AA

0.1 g
1g

7,300
42,400[65080-33-3]

Reference Compound to Measure Collagenase Activity with Code 3087-v
3087-v

Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-20

2,4-Dinitrophenyl-L-prolyl-L-glutaminylglycylL-isoleucyl-L-alanylglycyl-L-glutaminyl- D-arginine(M.W. 992.00)

C40H61N15O15

B

Vial

2.5 mg9,100[63014-08-4]

Substrate for Animal Collagenase
1) Y. Masui, T. Takemoto, S. Sakakibara, H. Hori, and Y. Nagai, Biochem. Med., 17, 215 (1977).

3082

Dnp-Pro-Leu-Gly

2～10

2,4-Dinitrophenyl-L-prolyl-L-leucylglycine(M.W. 451.43)

AA

0.1 g
1g

5,000
31,500C19H25N5O8

Reference Compound to Measure Collagenase Activity with Code 3073-v
3073-v

Dnp-Pro-Leu-Gly-Ile-Ala-Gly-Arg-NH2-20

2,4-Dinitrophenyl-L-prolyl-L-leucylglycylL-isoleucyl-L-alanylglycyl-L-arginine amide(M.W. 847.92)

A

Vial

2.5 mg

C36H57N13O11

Substrate for Animal Collagenase
1) Y. Masui, T. Takemoto, S. Sakakibara, H. Hori, and Y. Nagai, Biochem. Med., 17, 215 (1977).

– 215 –

8,400

Enzyme Substrates

Caspase Inhibitors & Substrates See List of Inhibitors and Substrates for Various Proteases on page 162

Enzyme Substrates and Related Peptides (continued)
Code

CompoundGrade3224-s

FRETS-VWF73-20

(Trifluoroacetate Form)

Price:Yen
Vial

0.1 mg30,000

Asp-Arg-Glu-A2pr(Nma)-Ala-Pro-Asn-Leu-Val-TyrMet-Val-Thr-Gly-A2pr(Dnp)-Pro-Ala-Ser-Asp-GluIle-Lys-Arg-Leu-Pro-Gly-Asp-Ile-Gln-ValVal-Pro-Ile-Gly-Val-Gly-Pro-Asn-Ala-AsnVal-Gln-Glu-Leu-Glu-Arg-Ile-Gly-Trp-ProAsn-Ala-Pro-Ile-Leu-Ile-Gln-Asp-Phe-GluThr-Leu-Pro-Arg-Glu-Ala-Pro-Asp-Leu-ValLeu-Gln-Arg
A2pr(Nma): N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acidA2pr(Dnp): N β-(2,4-Dinitrophenyl)-2,3-diaminopropionic acid
(M.W. 8314.3) C370H583N103O113S
Purity: higher than 95% by HPLC

Fluorescence-Quenching Substrate for ADAMTS-13
1) K. Kokame, M. Matsumoto, Y. Fujimura, and T. Miyata, Blood, 103, 607 (2004). (VWF73 Sequence)2) K. Kokame, Y. Nobe, Y. Kokubo, A. Okayama, and T. Miyata, Br. J. Haematol., 129, 93 (2005). (FRETS-VWF73)
3) E. Groot, J.J.J. Hulstein, C.N. Rison, P.G. De Groot, and R. Fijnheer, J. Thromb. Haemost., 4, 698 (2006).
(ADAMTS-13 Assay)• This compound is produced by Peptide Institute, Inc. under the license of National Cardiovascular Center.

3154-v

Glt-Ala-Ala-Phe-MCA-20

Glutaryl-L-alanyl-L-alanyl-L-phenylalanine
4-methylcoumaryl-7-amide(M.W. 578.61)

A

Vial

5 mg

5,400

C30H34N4O8

Substrate for Chymotrypsin
3129

Glt-Ala-Ala-Pro-Leu-pNA

2～10

Glutaryl-L-alanyl-L-alanyl-L-prolylL-leucine p-nitroanilide(M.W. 604.65)

AA

0.1 g
1g

7,800
54,400C28H40N6O9

Substrate for Pancreatic Elastase1) E.G. Del Mar, C. Largman, J.W. Brodrick, M. Fassett, and M.C. Geokas, Biochemistry, 19, 468 (1980).

3097-v

Glt-Gly-Arg-MCA*-20

Glutarylglycyl-L-arginine 4-methylcoumaryl-7-amide(M.W. 502.52)

A

C23H30N6O7

Vial

5 mg

4,100

[65147-16-2]

Substrate for u-PA (Urokinase)* 本品は第十五改正日本薬局方「一般試験法」収載試薬です。
1) T. Morita, H. Kato, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, J. Biochem., 82, 1495 (1977).
2) S. Iwanaga, T. Morita, H. Kato, T. Harada, N. Adachi, T. Sugo, I. Maruyama, K. Takada, T. Kimura, and S. Sakakibara,In, KININS-II: Biochemistry, Pathophysiology, and Clinical Aspects, (S. Fujii, H. Moriya, and T. Suzuki eds.), Plenum
Publishing Co., 1979, pp.147-163.

3080

Glu-Glu

2～10

L-Glutamyl- L-glutamic acid

(M.W. 276.24)

C10H16N2O7

0.1 g
1g

3,400
17,800

A

0.1 g
1g
5g

1,700
4,900
18,000

A

0.1 g
1g

2,400
7,800

[3929-61-1]

3066

Glu(pNA) • H2O

2～10

L-Glutamic acid γ-p-nitroanilide(M.W. 267.24 • 18.02)

A

C11H13N3O5 • H2O [122864-94-2]

Substrate for γ -Glutamyl Transpeptidase
3067

Glu-pNA • H2O-20

L-Glutamic acid α-p-nitroanilide(M.W. 267.24 • 18.02)

C11H13N3O5 • H2O– 216 –

Enzyme Substrates and Related Peptides (continued)
Code

Compound

3050

Glu(Cys-Gly)[Glutathione; GSH]

2～10

Grade

Price:Yen

B

1g
5g
25 g

1,800
2,700
6,100

AA

5g
25 g
100 g

1,800
2,800
7,000

AA

1g
5g
25 g

2,600
7,000
27,500

A

0.1 g
1g

4,400
30,000

0.1 g
1g

5,800
30,000γ-L-Glutamyl-L-cysteinylglycine(M.W. 307.32)

C10H17N3O6S[70-18-8]

Glutathione See Code 3050 Glu(Cys-Gly) above

3028

Gly-Gly

2～10

Glycylglycine
C4H8N2O3

3061

Gly-Gly-Gly

2～10

Glycylglycylglycine(M.W. 189.17)

C6H11N3O4

3076

Gly-Gly-His

2～10

Glycylglycyl-L-histidine(M.W. 269.26)

C10H15N5O4[556-50-3][556-33-2][93404-95-6]

Cu-Binding Peptide1) S. Lau, T.P.A. Kruch, and B. Sarkar, J. Biol. Chem., 249, 5878 (1974).

A

3119

Gly-Gly-Tyr-Arg

2～10

Glycylglycyl-L-tyrosyl-L-arginine(M.W. 451.48)

C19H29N7O6[70195-20-9]

Affinity Ligand for Papain
1) M.O. Funk, Y. Nakagawa, J. Skochdopole, and E.T. Kaiser, Int. J. Pept. Protein Res., 13, 296 (1979).

3022

Gly-Leu

2～10

Glycyl-L-leucine(M.W. 188.22)

C8H16N2O3

3053

Gly-Phe2～10

Glycyl-L-phenylalanine(M.W. 222.24)

C11H14N2O3

Gly-Phe-NH2
Glycyl-L-phenylalanine amide

3052

Gly-Pro2～10

Glycyl-L-proline(M.W. 172.18)

3090-v

Gly-Pro-MCA-20

(Tosylate Form)

C7H12N2O3

1,700
3,100
9,000

AA

0.1 g
1g

1,800
3,200

AA

0.1 g
1g

2,300
7,100

AA

0.1 g
1g

1,900
5,000

[3321-03-7]

2～10

C11H15N3O2

0.1 g
1g
5g

[869-19-2]

3023(M.W. 221.26)

AA[13467-26-0][704-15-4]

AA

Vial

Glycyl-L-proline 4-methylcoumaryl-7-amide(M.W. 329.35)

C17H19N3O4[67341-42-8]

Substrate for X-Prolyl Dipeptidyl-Aminopeptidase
1) T. Kato, T. Nagatsu, T. Kimura, and S. Sakakibara, Biochem. Med., 19, 351 (1978).

– 217 –

5 mg

3,000

Enzyme Substrates(M.W. 132.12)

Enzyme Substrates and Related Peptides (continued)
Code

CompoundGrade3074-v

Gly-Pro-pNA • Tos[GPNT]

AA-20

Price:Yen
Vial

10 mg

2,700

Glycyl-L-proline p-nitroanilide monotosylate(M.W. 292.29 • 172.20)

C13H16N4O4 • C7H8O3S[65096-46-0]

Substrate for X-Prolyl Dipeptidyl-Aminopeptidase
1) T. Nagatsu, M. Hino, H. Fuyamada, T. Hayakawa, S. Sakakibara, Y. Nakagawa, and T. Takemoto, Anal. Biochem.,
74, 466 (1976).
2) K. Fujita, M. Hirano, J. Ochiai, M. Funabashi, I. Nagatsu, T. Nagatsu, and S. Sakakibara, Clin. Chim. Acta, 88, 15(1978).

GPNT See Code 3074 Gly-Pro-pNA • Tos above
Hippuryl-Alanyl-Proline See Code 3126 Bz-Gly-Ala-Pro on page 214
Hippuryl-Arginine See Code 3059 Bz-Gly-Arg on page 214
Hippuryl-Glycyl-Glycine See Code 3128 Bz-Gly-Gly-Gly on page 214
Hippuryl-Histidyl-Leucine See Code 3064 Bz-Gly-His-Leu on page 214
Hippuryl-Lysine See Code 3047 Bz-Gly-Lys on page 214

3065

His-Leu

2～10

L-Histidyl- L-leucine(M.W. 268.31)

AA
C12H20N4O3

0.1 g
1g

2,500
8,800

[7763-65-7]

KYS-1 See Code 3225 MOCAc-Gly-Ser-Pro-Ala-Phe-Leu-Ala-Lys(Dnp)-D-Arg-NH2 on page 220

3024

Leu-Gly

2～10

L-Leucylglycine(M.W. 188.22)

C8H16N2O3

3025

Leu-Gly-Gly

2～10

L-Leucylglycylglycine(M.W. 245.28)

3091-v

Leu-MCA-20

(Tosylate Form)

C10H19N3O4

AA

0.1 g
1g

2,000
4,600

AA

0.1 g
1g

2,400
9,700

[686-50-0][1187-50-4]

AA

Vial

5 mg

2,700

L-Leucine 4-methylcoumaryl-7-amide(M.W. 288.34)

C16H20N2O3

Substrate for Aminopeptidase
1) K. Saifuku, T. Sekine, T. Namihisa, T. Takahashi, and Y. Kanaoka, Clin. Chim. Acta, 84, 85 (1978).

3027

Leu-NH2 • HCl

2～10

L-Leucine amide monohydrochloride(M.W. 130.19 • 36.46)

C6H14N2O • HCl

AA

0.1 g
1g

1,900
4,300

AA

0.1 g
1g
5g

1,800
4,100
14,300[10466-61-2]

Substrate for Aminopeptidase3014

Leu-pNA

2～10

L-Leucine p-nitroanilide(M.W. 251.28)

C12H17N3O3[4178-93-2]

Substrate for Aminopeptidase
1) G. Peleiderer, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, eds.),
Academic Press, New York, 1970, pp. 514-521.

– 218 –

Enzyme Substrates and Related Peptides (continued)
Code

CompoundGrade3124-v

Lys-Ala-MCA

A

-20

(Tartarate Form)

Price:Yen
Vial

5 mg

3,600

L-Lysyl-L-alanine 4-methylcoumaryl-7-amide(M.W. 374.43)

C19H26N4O4

Substrate for Dipeptidyl-Aminopeptidase II
1) D. Mantle, M.F. Hardy, B. Lauffart, J.R. McDermott, A.I. Smith, and R.J.T. Pennington,
Biochem. J., 211, 567 (1983).

Lys-MCA-20

(Hydrochloride Form)

A

Vial

5 mg

3,600

L-Lysine 4-methylcoumaryl-7-amide(M.W. 303.36)

C16H21N3O3

Substrate for Aminopeptidase
Lysine Hydroxylase Substrate L-1 See Code 4166 Ala-Arg-Gly-Ile-Lys-Gly-Ile-Arg-Gly-Phe-Ser-Gly
on page 208

3197-v-20

B

4-Methoxyphenylazoformyl-Phe[AAFP]

Vial

5 mg

3,000

Vial

5 mg

3,500

(Potassium Salt)

N-(4-Methoxyphenylazoformyl)-L-phenylalanine(M.W. 327.33)

C17H17N3O4[396717-86-5]

Substrate for Carboxypeptidase A
1) W.L. Mock, Y. Liu, and D.J. Stanford, Anal. Biochem., 239, 218 (1996).

3149-v

Met-MCA-20

(Tosylate Form)A

L-Methionine 4-methylcoumaryl-7-amide(M.W. 306.38)

C15H18N2O3S

Substrate for Aminopeptidase
3152

Met-Met2～10

L-Methionyl- L-methionine(M.W. 280.41)

3216-v-20

A
C10H20N2O3S2

0.1 g
1g

3,200
15,000

1 mg

10,000[7349-78-2]

MOCAc-Ala-Pro-Ala-Lys-Phe-Phe-Arg-LeuLys(Dnp)-NH2

A

Vial

(Trifluoroacetate Form)(7-Methoxycoumarin-4-yl)acetyl-L-alanyl-L-prolyl-L-alanyl-L-lysylL-phenylalanyl- L-phenylalanyl- L-arginyl- L-leucylN ε-(2,4-dinitrophenyl)-L-lysine amide(M.W. 1458.6)

C71H95N17O17

Fluorescence-Quenching Substrate for Proteinase A / Pepsin
1) H. Kondo, Y. Shibano, T. Amachi, N. Cronin, K. Oda, and B.M. Dunn, J. Biochem., 124, 141 (1998).
• This compound is distributed under the license of Suntory Limited.

– 219 –

Enzyme Substrates

3132-v

Enzyme Substrates and Related Peptides (continued)
Code

Compound3167-v

MOCAc-Arg-Pro-Lys-Pro-Tyr-Ala-NvaTrp-Met-Lys(Dnp)-NH2[NFF-2]

-20

Grade
B

Price:Yen
Vial

1 mg

8,000

1 mg

8,000

(7-Methoxycoumarin-4-yl)acetyl-L-arginyl-L-prolyl-L-lysyl-L-prolylL-tyrosyl-L-alanyl- L-norvalyl- L-tryptophyl- L-methionylN ε-(2,4-dinitrophenyl)-L-lysine amide(M.W. 1656.9)

C79H105N19O19S[158584-08-8]

Fluorescence-Quenching Substrate for Matrix Metalloproteinases
1) H. Nagase, C.G. Fields, and G.B. Fields, J. Biol. Chem., 269, 20952 (1994).

3168-v-20

MOCAc-Arg-Pro-Lys-Pro-Val-Glu-NvaTrp-Arg-Lys(Dnp)-NH2[NFF-3]B

Vial(7-Methoxycoumarin-4-yl)acetyl-L-arginyl-L-prolyl-L-lysyl-L-prolylL-valyl- L-glutamyl- L-norvalyl- L-tryptophyl- L-arginylN ε-(2,4-dinitrophenyl)-L-lysine amide(M.W. 1675.8)

C78H110N22O20[158584-09-9]

Fluorescence-Quenching Substrate for Matrix Metalloproteinase-3 (Stromelysin 1)
1) H. Nagase, C.G. Fields, and G.B. Fields, J. Biol. Chem., 269, 20952 (1994).

3184-v-20

A

MOCAc-Asp-Glu-Val-Asp-Ala-ProLys(Dnp)-NH2

Vial

1 mg

15,0001 mg

16,000(7-Methoxycoumarin-4-yl)acetyl-L-aspartyl-L-glutamyl-L-valylL-aspartyl- L-alanyl-L-prolyl-N ε-(2,4-dinitrophenyl)- L-lysine amide(M.W. 1154.1)

C50H63N11O21

Fluorescence-Quenching Substrate for Caspase-3
1) M. Enari, R.V. Talanian, W.W. Wong, and S. Nagata, Nature, 380, 723 (1996).

3200-v-20

A

MOCAc-Gly-Lys-Pro-Ile-Leu-Phe-PheArg-Leu-Lys(Dnp)-D-Arg-NH2

Vial(7-Methoxycoumarin-4-yl)acetylglycyl-L-lysyl-L-prolyl-L-isoleucylL-leucyl-L-phenylalanyl- L-phenylalanyl- L-arginyl- L-leucyl[N ε-(2,4-dinitrophenyl)-L-lysyl]-D-arginine amide(M.W. 1756.0)

C85H122N22O19

Fluorescence-Quenching Substrate for Cathepsin D/E
1) Y. Yasuda, T. Kageyama, A. Akamine, M. Shibata, E. Kominami, Y. Uchiyama, and K. Yamamoto, J. Biochem., 125, 1137 (1999).

3225-v-20

MOCAc-Gly-Ser-Pro-Ala-Phe-Leu-AlaLys(Dnp)-D-Arg-NH2[KYS-1]

A

Vial

1

mg

10,000(Trifluoroacetate Form)(7-Methoxycoumarin-4-yl)acetylglycyl-L-seryl-L-prolyl-L-alanylL-phenylalanyl-L-leucyl-L-alanyl-[N ε-(2,4-dinitrophenyl)-L-lysyl]D-arginine amide(M.W. 1327.4)

C61H82N16O18

Fluorescence-Quenching Substrate for Cathepsin E
1) Y. Yasuda, K. Kohmura, T. Kadowaki, T. Tsukuba, and K. Yamamoto, Biol. Chem., 386, 299 (2005).
2) Y. Yasuda, T. Tsukuba, K. Okamoto, T. Kadowaki, and K. Yamamoto, J. Biochem., 138, 621 (2005).
• This compound is produced by Peptide Institute, Inc. under the license of Kyushu TLO Co., Ltd.

– 220 –

Enzyme Substrates and Related Peptides (continued)
Code

Compound3226-v

MOCAc-Lys-Pro-Leu-Gly-Leu-A2pr(Dnp)-AlaArg-NH2

-20

Grade
A

Price:Yen
Vial

1 mg

8,000

(Trifluoroacetate Form)(7-Methoxycoumarin-4-yl)acetyl-L-lysyl-L-prolyl-L-leucylglycylL-leucyl-[N β-(2,4-dinitrophenyl)- L-2,3-diaminopropionyl]L-alanyl- L-arginine amide(M.W. 1221.3)

C55H80N16O161) U. Neumann, H. Kubota, K. Frei, V. Ganu, and D. Leppert, Anal. Biochem., 328, 166 (2004).
2) A. Trifilieff, C. Walker, T. Keller, G. Kottirsch, and U. Neumann, Br. J. Pharmacol., 135, 1655 (2002).
3) M.C. Riitano, H. Pfister, P. Engelhardt, U. Neumann, M. Reist, A. Zurbriggen, M. Stoffel, J. Peel, T. Jungi,
P. Schawalder, and D.E. Spreng, Am. J. Vet. Res., 63, 1423 (2002).

3164-s

MOCAc-Pro-Leu-Gly-20

(7-Methoxycoumarin-4-yl)acetyl-L-prolylL-leucylglycine(M.W. 501.53)

C25H31N3O8

AA

Vial

0.1 mg2,000[140430-56-4]

Reference Compound for MOCAc-type Fluorescence-Quenching Substrate
1) C.G. Knight, F. Willenbrock, and G. Murphy, FEBS Lett., 296, 263 (1992).

3163-v-20

A

MOCAc-Pro-Leu-Gly-Leu-A2pr(Dnp)Ala-Arg-NH2

Vial

1 mg

6,000

1 mg

15,000(7-Methoxycoumarin-4-yl)acetyl-L-prolyl-L-leucylglycylL-leucyl-[N β-(2,4-dinitrophenyl)- L-2,3-diaminopropionyl]L-alanyl- L-arginine amide(M.W. 1093.1)

C49H68N14O15[140430-53-1]

Fluorescence-Quenching Substrate for Matrix Metalloproteinases
1) C.G. Knight, F. Willenbrock, and G. Murphy, FEBS Lett., 296, 263 (1992).

3212-v-20

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

B

Vial

(Trifluoroacetate Form)(7-Methoxycoumarin-4-yl)acetyl-L-seryl-L-glutamyl-L-valylL-asparaginyl-L-leucyl-L-aspartyl- L-alanyl- L-glutamyl- L-phenylalanylL-arginyl-[N ε-(2,4-dinitrophenyl)- L-lysyl]- L-arginyl- L-arginine amide(M.W. 2001.1)

C86H125N27O29

Fluorescence-Quenching Substrate for β -Secretase

Normal-type APP:
Swedish-type APP:
Fluorescence-quenching substrate:

β -Cleavage Site↓...........ISEVKM -DAEFRH........
...........ISEVNL-DAEFRH........
MOCAc-SEVNL-DAEFRK(Dnp)RR-NH2

1) H. Koike, H. Seki, Z. Kouchi, M. Ito, T. Kinouchi, S. Tomioka, H. Sorimachi, T.C. Saido, K. Maruyama,
K. Suzuki, and S. Ishiura, J. Biochem., 126, 235 (1999).

– 221 –

Enzyme Substrates

Fluorescence-Quenching Substrate for Matrix Metalloproteinases and ADAM-17 /Tumor Necrosis Factor Converting Enzyme (TACE)Enzyme Substrates and Related Peptides (continued)
Code

Compound3183-v

MOCAc-Tyr-Val-Ala-Asp-Ala-Pro-Lys(Dnp)-NH2-20

(7-Methoxycoumarin-4-yl)acetyl-L-tyrosyl-L-valyl-L-alanyl-L-aspartylL-alanyl- L-prolyl-N ε-(2,4-dinitrophenyl)- L-lysine amide(M.W. 1144.1)

Grade
A

Price:Yen
Vial

1 mg

15,000C53H65N11O18

Fluorescence-Quenching Substrate for Caspase-1
1) M. Enari, R.V. Talanian, W.W. Wong, and S. Nagata, Nature, 380, 723 (1996).

NFF-2 See Code 3167 MOCAc-Arg-Pro-Lys-Pro-Tyr-Ala-Nva-Trp-Met-Lys(Dnp)-NH2 on page 220
NFF-3 See Code 3168 MOCAc-Arg-Pro-Lys-Pro-Val-Glu-Nva-Trp-Arg-Lys(Dnp)-NH2 on page 220

3217-v-20

Nma-Gly-Gly-Val-Val-Ile-Ala-Thr-Val-Lys(Dnp)D-Arg-D-Arg-D-Arg-NH2

B

Vial

1 mg

15,000(Trifluoroacetate Form)[2-(Methylamino)benzoyl]glycylglycyl-L-valyl-L-valyl-L-isoleucylL-alanyl- L-threonyl- L-valyl-[N ε-(2,4-dinitrophenyl)- L-lysyl]D-arginyl- D-arginyl- D-arginine amide(M.W. 1609.8)

C70H116N26O18

Fluorescence-Quenching Substrate for γ -Secretase
1) M.R. Farmery, L.O. Tjernberg, S.E. Pursglove, A. Bergman, B. Winblad, and J. Na
slund,J. Biol. Chem., 278, 24277 (2003). (Original)

3229-vNew

Nma-Ile-His-Pro-Phe-His-Leu-Val-Ile-HisThr-Lys(Dnp)-D-Arg-D-Arg-NH2-20

(Trifluoroacetate Form)

A

Vial

1 mg

15,000[2-(Methylamino)benzoyl]-L-isoleucyl-L-histidyl-L-prolyl-L-phenylalanylL-histidyl- L-leucyl-L-valyl-L-isoleucyl- L-histidyl- L-threonyl[N ε-(2,4-dinitrophenyl)-L-lysyl]-D-arginyl-D-arginine amide(M.W. 1952.2)

C91H134N30O19

Fluorescence-Quenching Substrate for Human Renin
1) S. Takahashi, K. Hori, M. Shinbo, K. Hiwatashi, T. Gotoh, and S. Yamada, Biosci. Biotechnol. Biochem., 72, 3232
(2008).

3148-vPhe-MCA-20

(Tosylate Form)AA

L-Phenylalanine 4-methylcoumaryl-7-amide(M.W. 322.36)

C19H18N2O3[98516-72-4]

Substrate for Aminopeptidase– 222 –

Vial

5 mg

2,700

Enzyme Substrates and Related Peptides (continued)
Code

CompoundGrade3096-v

Pro-Phe-Arg-MCA-20

(Hydrochloride Form)A

Price:Yen
Vial

5 mg

5,400

L-Prolyl- L-phenylalanyl- L-arginine
4-methylcoumaryl-7-amide(M.W. 575.66)

C30H37N7O5[115918-56-4]

Substrate for Pancreatic / Urinary Kallikrein and Proteasome
1) T. Morita, H. Kato, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, J. Biochem., 82, 1495 (1977).
2) V. Ustrell, G. Pratt, and M. Rechesteiner, Proc. Natl. Acad. Sci. U.S.A., 92, 584 (1995).

Pyr-Ala2～10

L-Pyroglutamyl- L-alanine(M.W. 200.19)

AA
C8H12N2O4

0.1 g
1g

2,700
11,400[21282-08-6]

Substrate for Pyroglutamyl Peptidase
1) R.F. Doolittle, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, eds.),
Academic Press, New York, 1970, pp. 555-569.

3159-v

Pyr-Arg-Thr-Lys-Arg-MCA-20

L-Pyroglutamyl- L-arginyl- L-threonyl- L-lysyl-

A

Vial

5 mg

6,500

L-arginine 4-methylcoumaryl-7-amide(M.W. 827.93)

C37H57N13O9[155575-02-3]

Substrate for Furin
1) K. Hatsuzawa, M. Nagahama, S. Takahashi, K. Takada, K. Murakami, and K. Nakayama, J. Biol. Chem.,
267, 16094 (1992).

3145-v

Pyr-Gly-Arg-MCA-20

L-Pyroglutamylglycyl- L-arginine

A

Vial

5 mg

5,400

A

Vial

5 mg

25,0004-methylcoumaryl-7-amide(M.W. 499.52)

C23H29N7O6

Substrate for t-PA and u-PA (Urokinase)4237-v-20

Pyr-Lys-Arg-Pro-Ser-Gln-Arg-Ser-Lys-TyrLeu(M.W. 1373.6)

C60H100N20O17[136132-68-8]

Substrate for Protein Kinase C1) I. Yasuda, A. Kishimoto, S. Tanaka, M. Tominaga, A. Sakurai, and Y. Nishizuka, Biochem. Biophys. Res. Commun.,
166, 1220 (1990).

3101-v

Pyr-MCA-20

L-Pyroglutamic acid 4-methylcoumaryl-7-amide(M.W. 286.28)

AA
C15H14N2O4[66642-36-2]

Substrate for Pyroglutamyl Peptidase
1) K. Fujiwara and D. Tsuru, J. Biochem., 83, 1145 (1978).

– 223 –

Vial

5 mg

3,500

Enzyme Substrates

3079

Enzyme Substrates and Related Peptides (continued)
Code

Compound

Grade

3130

Pyr-Phe-Leu-pNA

AA

2～10

L-Pyroglutamyl-L-phenylalanyl- L-leucine p-nitroanilide(M.W. 509.55)

C26H31N5O6

Price:Yen
0.1 g
1g

4,800
29,700[85901-57-1]

Substrate for Thiol Proteases
1) I.Y. Filippova, E.N. Lysogorskaya, E.S. Oksenoit, G.N. Rudenskaya, and V.M. Stepanov, Anal. Biochem.,
143, 293 (1984).

3228-vNew

Pyr-Pro-Val-pNA
L-Pyroglutamyl- L-prolyl- L-valine p-nitroanilide-20

(M.W. 445.47)

C21H27N5O6

AA

Vial

5 mg

6,000

[83329-36-6]

Selective Substrate for Human Granulocyte Elastase
1) J.A. Kramps, Ch. van Twisk and A.C. van der Linden, Scand. J. Clin. Lab. Investig., 43, 427 (1983).
2) L. Persson, J. Bergstro
m, H. Ito, and A. Gustafsson, J. Periodontol., 72, 90 (2001).
3) I. Groth and S. Alban, Planta Med., 74, 852 (2008).

Renin Substrate See Code 3110 Suc-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-MCA on page 225
See Code 4133 Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His on page 209
RR-SRC See Code 4184 Arg-Arg-Leu-Ile-Glu-Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Gly on page 208

4236-v

Ser-Gln-Asn-Tyr-Pro-Ile-Val-20

(M.W. 819.90)

AA

Vial

5 mg

15,000C37H57N9O12

Substrate for HIV-1 Protease1) S. Billich, M.-T. Knoop, J. Hansen, P. Strop, J. Sedlacek, R. Mertz, and K. Moeliling, J. Biol. Chem., 263, 17905(1988).
2) P.L. Darke, R.F. Nutt, S.F. Brady, V.M. Garsky, T.M. Ciccarone, C.-T. Leu, P.K. Lumma, R.M. Freidinger, D.F. Veber,and I.S. Sigal, Biochem. Biophys. Res. Commun., 156, 297 (1988).
3) P.L. Darke, C-T. Leu, L.J. Davis, J.C. Heimbach, R.E. Diehl, W.S. Hill, R.A.F. Dixon, and I.S. Sigal, J. Biol. Chem.,
264, 2307 (1989).

STANA See Code 3071 Suc-Ala-Ala-Ala-pNA on page 225

3153-vSuc(OMe)-Ala-Ala-Pro-Val-MCA-20

N-Methoxysuccinyl-L-alanyl-L-alanyl-L-prolylL-valine 4-methylcoumaryl-7-amide(M.W. 627.69)

C31H41N5O9

AA

Vial

5 mg

6,000

[72252-90-5]

Substrate for Human Leukocyte / Porcine Pancreatic Elastase1) M.J. Castrillo, K. Nakajima, M. Zimmerman, and J.C. Powers, Anal. Biochem., 99, 53 (1979).

3133-v

Suc-Ala-Ala-Ala-MCA-20

Succinyl-L-alanyl-L-alanyl-L-alanine
4-methylcoumaryl-7-amide(M.W. 488.49)

C23H28N4O8

AA

Vial

5 mg

6,000

[73617-90-0]

Substrate for Elastase
1) R.A. Mumford, A.W. Strauss, J.C. Powers, P.A. Pierzchala, N. Nishino, and M. Zimmerman, J. Biol. Chem.,
255, 2227 (1980).

– 224 –

Enzyme Substrates and Related Peptides (continued)
Code

CompoundGrade3071-v

Suc-Ala-Ala-Ala-pNA[STANA]AA-20

Price:Yen
Vial

5 mg

1,900

Succinyl-L-alanyl-L-alanyl-L-alanine p-nitroanilide(M.W. 451.43)

3071
2～10

C19H25N5O8[52299-14-6]

AA

Suc-Ala-Ala-Ala-pNA[STANA]

0.1 g
1g

4,400
26,000

0.1 g
1g

3,200
15,800

Succinyl-L-alanyl-L-alanyl-L-alanine p-nitroanilide(M.W. 451.43)

C19H25N5O8[52299-14-6]

1) J. Bieth, B. Spiess, and C.G. Wermuth, Biochem. Med., 11, 350 (1974).

3117

Suc-Ala-Ala-pNA

2～10

Succinyl-L-alanyl-L-alanine p-nitroanilide(M.W. 380.35)

AA

C16H20N4O7

3114-v

Suc-Ala-Ala-Pro-Phe-MCA-20

Succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine
4-methylcoumaryl-7-amide(M.W. 661.70)

C34H39N5O9

A

Vial

5 mg

6,000

5 mg

4,300

10 mg

10,000[88467-45-2]

Substrate for Chymotrypsin
1) H. Sawada, H. Yokosawa, M. Hoshi, and S. Ishii, Experientia, 39, 377 (1983).

3160-v

Suc-Ala-Glu-MCA-20

Succinyl-L-alanyl-L-glutamic acidα-(4-methylcoumaryl-7-amide)(M.W. 475.45)

A

Vial

C22H25N3O9

Substrate for Ingensin / Proteasome
1) S. Ishiura, T. Tsukahara, T. Tabira, and H. Sugita, FEBS Lett., 257, 388 (1989).

3162-v

Suc-Ala-Leu-Pro-Phe-pNA-20

Succinyl-L-alanyl-L-leucyl-L-prolylL-phenylalanine p-nitroanilide(M.W. 666.72)

A

Vial

C33H42N6O9

Substrate for PPIase (Peptidyl Prolyl cis-trans Isomerase)
1) J.L. Kofron, P. Kuzmic, V. Kishore, E. Colon-Bonilla, and D.H. Rich, Biochemistry, 30, 6127 (1991).

3116

Suc-Ala-pNA

2～10

Succinyl-L-alanine p-nitroanilide(M.W. 309.27)

AA

2,500
8,800

C13H15N3O6

3100-v

Suc-Ala-Pro-Ala-MCA-20

Succinyl-L-alanyl-L-prolyl-L-alanine
4-methylcoumaryl-7-amide(M.W. 514.53)

0.1 g
1g

C25H30N4O8

A

Vial

[88467-44-1]

Substrate for Elastase
1) G. Oshima, K. Akashi, and M. Yamada, Arch. Biochem. Biophys., 233, 212 (1984).

– 225 –

5 mg

6,000

Enzyme Substrates

Substrate for ElastaseEnzyme Substrates and Related Peptides (continued)
Code

Compound

Grade

3118

Suc-Ala-Pro-Ala-pNA

AA

2～10

Succinyl-L-alanyl-L-prolyl-L-alanine p-nitroanilide(M.W. 477.47)

Price:Yen
0.1 g
1g

4,800
29,700C21H27N5O8

Substrate for Elastase3110-v

Suc-Arg-Pro-Phe-His-Leu-Leu-Val-Tyr-MCA-20

Succinyl-L-arginyl-L-prolyl-L-phenylalanylL-histidyl-L-leucyl-L-leucyl- L-valyl- L-tyrosine
4-methylcoumaryl-7-amide(M.W. 1301.5)

C66H88N14O14

A

Vial

1 mg

5,400

[76524-84-0]

Substrate for Renin and Proteinase A
1) K. Murakami, T. Ohsawa, S. Hirose, K. Takada, and S. Sakakibara, Anal. Biochem., 110, 232 (1981).
2) H. Yokosawa, H. Ito, S. Murata, and S. Ishii, Anal. Biochem., 134, 210 (1983).

3222-v

Suc-D-Asp-MCA-20

Succinyl-D-aspartic acid α-(4-methylcoumaryl-7-amide)(M.W. 390.34)

AA

Vial

5 mg

6,000

C18H18N2O8Selective Substrate for D-Aspartyl Endopeptidase
1) T. Kinouchi, S. Ishiura, Y. Mabuchi, Y. Urakami-Manaka, H. Nishio, Y. Nishiuchi, M. Tsunemi, K. Takada,
M. Watanabe, M. Ikeda, H. Matsui, S. Tomioka, H. Kawahara, T. Hamamoto, K. Suzuki, and Y. Kagawa,
Biochem. Biophys. Res. Commun., 314, 730 (2004).

3108-v

Suc-Gly-Pro-Leu-Gly-Pro-MCA-20

Succinylglycyl-L-prolyl-L-leucylglycylL-proline 4-methylcoumaryl-7-amide(M.W. 696.75)

C34H44N6O10

A

Vial

5 mg

6,000

[72698-36-3]

Substrate for Collagenase-like Peptidase
1) K. Kojima, H. Kinoshita, T. Kato, T. Nagatsu, K. Takada, and S. Sakakibara, Anal. Biochem., 100, 43 (1979).

3109-v

Suc-Gly-Pro-MCA-20

Succinylglycyl-L-proline
4-methylcoumaryl-7-amide(M.W. 429.42)

C21H23N3O7

AA

Vial

5 mg

4,100

[80049-85-0]

Substrate for Propyl Endopeptidase (Post-Proline Cleaving Enzyme)
1) T. Kato, T. Nakano, K. Kojima, T. Nagatsu, and S. Sakakibara, J. Neurochem., 35, 527 (1980).

3158-v

Suc-Ile-Ala-MCA-20

Succinyl-L-isoleucyl-L-alanine
4-methylcoumaryl-7-amide(M.W. 459.49)

C23H29N3O7

A

Vial

5 mg

4,300

[126103-95-5]

Substrate for Amyloid A4-Generating Enzyme
1) S. Ishiura, T. Tsukahara, T. Tabira, T. Shimizu, K. Arahata, and H. Sugita, FEBS Lett., 260, 131 (1990).
2) S. Ishiura, T. Nishikawa, T. Tsukahara, T. Momoi, H. Itoh, K. Suzuki, and H. Sugita, Neurosci. Lett., 115, 329 (1990).

3150-v

Suc-Ile-Ile-Trp-MCA-20

Succinyl-L-isoleucyl-L-isoleucyl-L-tryptophan
4-methylcoumaryl-7-amide(M.W. 687.78)

C37H45N5O8A[133525-12-9]– 226 –

Vial

5 mg

6,000

Enzyme Substrates and Related Peptides (continued)
Code

Compound3120-v

Suc-Leu-Leu-Val-Tyr-MCA-20

Succinyl-L-leucyl-L-leucyl-L-valylL-tyrosine 4-methylcoumaryl-7-amide(M.W. 763.88)

Grade

C40H53N5O10

A

Price:Yen
Vial

5 mg

6,000

[94367-21-2]

Substrate for Chymotrypsin, Ingensin / Proteasome and Calpain

TAME See Code 3003 Tos-Arg-OMe • HCl below
TMRIA-K4 See Code 3401 on page 240

3003
2～10

A

Tos-Arg-OMe • HCl[TAME]

5g
25 g
100 g

Tosyl-L-arginine methyl ester monohydrochloride(M.W. 342.41 • 36.46)

C14H22N4O4S • HCl

3,000
8,400
27,200[1784-03-8]

Substrate for Trypsin
1) K.A. Walsh, In, Proteolytic Enzymes, Methods in Enzymology, Vol. 19, (G.E. Perlmann and L. Lorand, eds.),
Academic Press, New York, 1970, pp. 41-63.

3054

Tos-Lys-OMe • HCl

2～10

Tosyl-L-lysine methyl ester monohydrochloride(M.W. 314.40 • 36.46)

A
C14H22N2O4S • HCl

0.1 g
1g

1,900
3,600

[5266-48-8]

Substrate for Trypsin
1) F. Widmer and J.T. Johansen, Carlsberg Res. Commun., 44, 37 (1979).
2) F. Widmer, K. Breddam, and J.T. Johansen, In, Peptides 1980, Proceedings of 16th. European Peptide Symposium(K. Brunfeldt, ed.), Scriptor, Copenhagen, 1981, pp. 46-55.

3209-v

Z-Ala-Ala-Asn-MCA-20

Benzyloxycarbonyl-L-alanyl-L-alanyl-L-asparagine
4-methylcoumaryl-7-amide(M.W. 565.57)

C28H31N5O8

A

Vial

5 mg

5,000

[149697-16-5]

Substrate for Legumain
Legumain is an asparaginyl endopeptidase first identified in seeds of leguminous plants1) and subsequently
in mammalian lysosome2). Recently, two interesting reports on this widespread enzyme "legumain" have been
published under the following titles: i) "An asparaginyl endopeptidase processes a microbial antigen for class II
MHC presentation"3) and ii) "Identification of human asparaginyl endopeptidase (legumain) as an inhibitor ofosteoclast formation and bone resorption"4). Characterization of porcine kidney enzyme is given in ref.5)
1) A.A. Kembhavi, D.J. Buttle, C.G. Knight, and A.J. Barrett, Arch. Biochem. Biophys., 303, 208 (1993).
2) J.-M. Chen, P.M. Dando, N.D. Rawlings, M.A. Brown, N.E. Young, R.A. Stevens, E. Hewitt, C. Watts, and A.J. Barrett,
J. Biol. Chem., 272, 8090 (1997).
3) B. Manoury, E.W. Hewitt, N. Morrice, P.M. Dando, A.J. Barrett, and C. Watts, Nature, 396, 695 (1998).
4) S.J. Choi, S.V. Reddy, R.W. Devlin, C. Menaa, H. Chung, B.F. Boyce, and G.D. Roodman, J. Biol. Chem., 274, 27747(1999).
5) P.M. Dando, M. Fortunato, L. Smith, C.G. Knight, J.E. McKendrick, and A.J. Barrett, Biochem. J., 339, 743 (1999).

– 227 –

Enzyme Substrates

1) H. Sawada, H. Yokosawa, M. Hoshi, and S. Ishii, Experientia, 39, 377 (1983).
2) T. Sasaki, T. Kikuchi, N. Yumoto, N. Yoshimura, and T. Murachi, J. Biol. Chem., 259, 12489 (1984).
3) S. Ishiura, M. Sano, K. Kamakura, and H. Sugita, FEBS Lett., 189, 119 (1985).
4) T. Tsukahara, S. Ishiura, and H. Sugita, Eur. J. Biochem., 177, 261 (1988).

Enzyme Substrates and Related Peptides (continued)
Code

Compound

Grade

3127

Z-Ala-Ala-Leu-pNA

AA

2～10

Benzyloxycarbonyl-L-alanyl-L-alanyl-L-leucine
p-nitroanilide(M.W. 527.57)

C26H33N5O7

Price:Yen
0.1 g
1g

4,400
26,700[61043-33-2]

Substrate for Subtilisin A and Serine Protease of Bacillus subtilis IFO3027 / Neprilysin
1) V.M. Stepanov, A.Y. Strongin, L.S. Izotova, Z.T. Abramov, L.A. Lyublinskaya, L.M. Ermakova, L.A. Baratova, and L.P.
Belyanova, Biochem. Biophys. Res. Commun., 77, 298 (1977).
2) Y. Shimizu, T. Nishino, and S. Murao, Agric. Biol. Chem., 47, 1775 (1983).
3) Y. Takaki, N. Iwata, S. Tsubuki, S. Taniguchi, S. Toyoshima, B. Lu, N.P. Gerard, C. Gerard, H.-J. Lee, K. Shirotani, andT.C. Saido, J. Biochem., 128, 897 (2000).
4) N. Iwata, Y. Takaki, S. Fukami, S. Tsubuki, and T.C. Saido, J. Neurosci. Res., 70, 493 (2002).

3123-v

Z-Arg-Arg-MCA-20

(Hydrochloride Form)

A

Vial

5 mg

4,100

Benzyloxycarbonyl-L-arginyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 621.69)

C30H39N9O6[88937-61-5]

Substrate for Cathepsin B
1) A.J. Barrett and H. Kirschke, In, Proteolytic Enzymes Part C, Methods in Enzymology, Vol. 80, (L. Lorand, ed.),Academic Press, New York, 1981, pp. 535–561.

3157

Z-Arg-OBzl(p-NO2) • HBr

2～10

Benzyloxycarbonyl-L-arginine p-nitrobenzyl estermonohydrobromide(M.W. 443.45 • 80.91)

C21H25N5O6 • HBr

A

0.1 g
1g

3,000
19,000AA

1g
5g

15,00045,000[96723-72-7]

Z-Asp-CH2-DCB See Code 3174 on page 199

3190

Z-Gln-Gly

2～10

Benzyloxycarbonyl-L-glutaminylglycine(M.W. 337.33)

C15H19N3O6[6610-42-0]

Substrate for Transglutaminase
1) J.E. Folk and P.W. Cole, J. Biol. Chem., 241, 5518 (1966).
2) H. Ando, M. Adachi, K. Umeda, A. Matsuura, M. Nonaka, R. Uchio, H. Tanaka, and M. Motoki, Agric. Biol. Chem.,
53, 2613 (1989).

Z-Glu-Lys(bio)-Asp-aomk See Code 3189 Z-Glu-Lys(Biotinyl)-Asp-CH2-DMB on page 199– 228 –

Enzyme Substrates and Related Peptides (continued)
Code

Compound

Grade

3018

Z-Glu-Tyr

AA

2～10

Benzyloxycarbonyl-L-glutamyl-L-tyrosine

0.1 g
1g

2,100
6,400

AA

25 mg
100 mg
1g

5,200
14,00091,000(M.W. 444.43)

C22H24N2O8[988-75-0]

3111

Z-Gly-Gly-Leu-pNA

2～10

Benzyloxycarbonylglycylglycyl-L-leucine
p-nitroanilide(M.W. 499.52)

C24H29N5O7

Price:Yen[53046-98-3]

1) M. Orlowski and S. Wilk, In, Peptides, Structure and Biological Function, (E. Gross and J. Meienhofer, eds.),
Pierce Chemical Co., 1980, pp. 925-928.

3019

Z-Gly-Leu

2～10

Benzyloxycarbonylglycyl-L-leucine(M.W. 322.36)

C16H22N2O5

Z-Gly-Leu-NH2

2～10

Benzyloxycarbonylglycyl-L-leucine amide
C16H23N3O4

Z-Gly-Phe

2～10

Benzyloxycarbonylglycyl-L-phenylalanine
C19H20N2O5

Z-Gly-Phe-NH2

2～10

Benzyloxycarbonylglycyl-L-phenylalanine amide
C19H21N3O4

Z-Gly-Pro

2～10

Benzyloxycarbonylglycyl-L-proline
C15H18N2O5

3208-v

Z-Gly-Pro-Arg-MCA-20

(Hydrochloride Form)

0.1 g
1g

2,300
7,100

AA

0.1 g
1g
5g

1,800
4,600
20,000

AA

0.1 g
1g

2,300
7,100

AA

0.1 g
1g

1,800
4,600

[5513-69-9]3055(M.W. 306.31)

AA[1170-76-9]

3021(M.W. 355.39)

2,000
5,300

[7535-72-0]

3020(M.W. 356.37)

0.1 g
1g

[1421-69-8]

3037(M.W. 321.37)

AA[1160-54-9]

AA

Vial

5 mg

5,000

Benzyloxycarbonylglycyl-L-prolyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 619.67)

C31H37N7O7[201928-42-9]

Substrate for Cathepsin K
1) K. Aibe, H. Yazawa, K. Abe, K. Teramura, M. Kumegawa, H. Kawashima, and K. Honda, Biol. Pharm. Bull.,
19, 1026 (1996).
2) F. Bu
hling, A. Gerber, C. Ha
ckel, S. Kru
ger, T. Kohnlein, D. Bro
mme, D. Reinhold, S. Ansorge, and T. Welte,
Am. J. Respir. Cell Mol. Biol., 20, 612 (1999).

3039

Z-Gly-Pro-Leu

2～10

Benzyloxycarbonylglycyl-L-prolyl-L-leucine(M.W. 419.47)

C21H29N3O6

0.1 g
1g

3,200
15,800

AA

0.1 g
1g

4,800
29,700[2646-63-1]

3040

Z-Gly-Pro-Leu-Gly

2～10

Benzyloxycarbonylglycyl-L-prolyl-L-leucylglycine(M.W. 476.52)

AA

C23H32N4O7– 229 –

Enzyme Substrates

Substrate for Neutral Endopeptidase

Enzyme Substrates and Related Peptides (continued)
Code

Compound

3029

Z-Gly-Pro-Leu-Gly-Pro

2～10

Benzyloxycarbonylglycyl-L-prolyl-L-leucylglycyl-L-proline(M.W. 573.64)

Grade

C28H39N5O8Price:Yen
0.1 g
1g

AA

7,800
54,400[2646-61-9]

Crystalline: Substrate for Bacterial Collagenase
1) Y. Nagai, S. Sakakibara, H. Noda, and S. Akabori, Biochim. Biophys. Acta, 37, 567 (1960).

3215-v

Z-His-Glu-Lys-MCA-20

(Hydrochloride Form)

AA

Vial

5 mg

5,700

Benzyloxycarbonyl-L-histidyl-L-glutamyl-L-lysine
4-methylcoumaryl-7-amide(M.W. 703.74)

C35H41N7O9

Substrate for Lys-Gingipain
1) N. Abe, A. Baba, T. Kadowaki, K. Okamoto, S. Okazaki, T. Asao, and K. Yamamoto, J. Biochem., 128, 877 (2000).

Z-Ile-Glu(OBut)-Ala-Leu-H (aldehyde) See Code 3169 on page 200

3176-v

Z-Leu-Arg-Gly-Gly-MCA-20

Benzyloxycarbonyl-L-leucyl-L-arginylglycylglycine
4-methylcoumaryl-7-amide(M.W. 692.76)

C34H44N8O8

A

Vial

5 mg

7,000

Vial

5 mg

5,000

[167698-68-2]

Substrate for Isopeptidase T
1) R.L. Stein, Z. Chen, and F. Melandri, Biochemistry, 34, 12616 (1995).

3210-v

Z-Leu-Arg-MCA-20

(Hydrochloride Form)AA

Benzyloxycarbonyl-L-leucyl-L-arginine 4-methylcoumaryl-7-amide(M.W. 578.66)

C30H38N6O6

Substrate for Cathepsin K/S/V
1) D. Bro
mme, K. Okamoto, B.B. Wang, and S. Biroc, J. Biol. Chem., 271, 2126 (1996).
2) D. Bro
mme, Z. Li, M. Barnes, and E. Mehler, Biochemistry, 38, 2377 (1999).

Z-Leu-Leu-H (aldehyde) See Code 3178 on page 200

3179-v

Z-Leu-Leu-Glu-MCA-20

Benzyloxycarbonyl-L-leucyl-L-leucyl-L-glutamic acidα-(4-methylcoumaryl-7-amide)(M.W. 664.75)

C35H44N4O9

A

Vial

5 mg

6,000

A

Vial

5 mg

5,000

[348086-66-8]

Substrate for Proteasome
Z-Leu-Leu-Leu-H (aldehyde) See Code 3175 on page 200

3177-v

Z-Leu-Leu-Leu-MCA-20

Benzyloxycarbonyl-L-leucyl-L-leucyl-L-leucine
4-methylcoumaryl-7-amide(M.W. 648.79)

C36H48N4O7

Substrate for Proteasome
1) S. Tsubuki, H. Kawasaki, Y. Saito, N. Miyashita, M. Inomata, and S. Kawashima, Biochem. Biophys. Res. Commun.,
196, 1195 (1993).

Z-Leu-Leu-Nva-H (aldehyde) See Code 3170 on page 201– 230 –

Enzyme Substrates and Related Peptides (continued)
Code

CompoundGrade3095-v

Z-Phe-Arg-MCA

AA

-20

(Hydrochloride Form)

Price:Yen
Vial

5 mg

3,500

Benzyloxycarbonyl-L-phenylalanyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 612.68)

C33H36N6O6[65147-22-0]

Substrate for Plasma Kallikrein, Cathepsin B/L and Arg-Gingipain
1) T. Morita, H. Kato, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara, J. Biochem., 82, 1495 (1977).
2) A.J. Barret, Biochem. J., 187, 909 (1980).

Z-Phe-Tyr

2～10

Benzyloxycarbonyl-L-phenylalanyl-L-tyrosine(M.W. 462.49)

0.1 g
1g

2,300
7,100

AA

0.1 g
1g

7,800
54,400

5 mg

5,400

C26H26N2O63131

Z-Phe-Tyr-Leu

2～10

Benzyloxycarbonyl-L-phenylalanyl-L-tyrosyl-L-leucine(M.W. 575.65)

AA

C32H37N3O7

Substrate for Metalloproteinase3138-v

Z-Pyr-Gly-Arg-MCA-20

(Hydrochloride Form)

A

Vial

Benzyloxycarbonyl-L-pyroglutamylglycyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 633.65)

C31H35N7O8

Substrate for Factor Xa
1) S. Kawabata, T. Miura, T. Morita, H. Kato, K. Fujikawa, S. Iwanaga, K. Takada, T. Kimura, and S. Sakakibara,
Eur. J. Biochem., 172, 17 (1988).

3069

Z-Tyr-Glu

2～10

Benzyloxycarbonyl-L-tyrosyl-L-glutamic acid
(M.W. 444.43)

C22H24N2O8

Z-Tyr-ONp-20

Benzyloxycarbonyl-L-tyrosine p-nitrophenyl ester
C23H20N2O7

3156-v

Z-Val-Lys-Met-MCA-20

(Hydrochloride Form)

0.1 g
1g

2,600
9,800

A-B

0.1 g
1g

1,900
5,000

[988-70-5]

3016(M.W. 436.41)

AA[3556-56-7]

A

Vial

5 mg

5,700

Benzyloxycarbonyl-L-valyl-L-lysyl-L-methionine
4-methylcoumaryl-7-amide(M.W. 667.82)

C34H45N5O7S[141223-71-4]

Substrate for Amyloid A4-Generating Enzyme and Proteasome
1) S. Ishiura, T. Nishikawa, T. Tsukahara, T. Momoi, H. Ito, K. Suzuki, and H. Sugita, Neurosci. Lett., 115, 329 (1990).

3211-v

Z-Val-Val-Arg-MCA-20

(Hydrochloride Form)

AA

Vial

5 mg

6,000

Benzyloxycarbonyl-L-valyl-L-valyl-L-arginine
4-methylcoumaryl-7-amide(M.W. 663.76)

C34H45N7O7

Substrate for Cathepsin S/L
1) D. Bro
mme, A. Steinert, S. Friebe, S. Fittkau, B. Wiederanders, and H. Kirschke, Biochem. J., 264, 475 (1989).
2) H. Kirschke and B. Wiederanders, In, Proteolytic Enzymes: Serine and Cysteine Peptidases, Methods in Enzymology,
Vol. 244, (A.J. Barrett ed.), Academic Press, New York, 1994, pp. 500-511.

– 231 –

Enzyme Substrates

3044

FRETS (Peptide) Library
FRETS*-25Xaa Series* FRETS : Fluorescence Resonance Energy Transfer Substrates

Design of FRETS-25Xaa
Dnp

Nma

NO2

H
N
O

NO2
Phe ProAla Tyr
D-A2pr-Gly- Val - Lys - Xaa -Ala-Phe-Pro-Lys-D-Arg-D-Arg
Glu IleArg Asp

Zaa

Yaa

Each substrate (Code 3701-v - Code 3719-v) in the FRETS-25Xaa series contains a highly fluorescent2-(N-methylamino)benzoyl (Nma) group linked to the side chain of the amino-terminal D-2,3-diamino propionic acid(D-A2pr) residue, which is efficiently quenched by a 2,4-dinitrophenyl (Dnp) group linked to the ε-amino function of
Lys. Xaa represents a fixed position of each of the 19 natural amino acids excluding Cys (noted in product name Code3701-v - Code 3719-v). A mixture of 5 amino acid residues (P, Y, K, I, and D) is at the Yaa position along with a mixtureof 5 amino acid residues (F, A, V, E, and R) at the Zaa position for each fixed Xaa. This provides a peptide mixture of 25
combinations of each Xaa series resulting in a combinatorial library totaling 475 peptide substrates. Both Nma and
Dnp groups are linked to the side chain of the individual residues, allowing for the determination of the cleavage siteby a specific enzyme through mass spectrometric analysis and Edman degradation as well.

Principle
When an enzyme of interest cleaves any peptide bond between D-A2pr(Nma) and Lys(Dnp) in the substrate, thefluorescence at λex = 340 nm and λem = 440 nm increases in proportion to the release of the Nma fluorophore fromthe internal Dnp quencher.

Reagents
1) Each substrate stock solutions: each FRETS-25Xaa (Code 3701-v - Code 3719-v) in 1.0 ml of DMSO (1 mM, totalof peptides)
2) Reference compounds stock solution: a 1:1 mixture of two solutions of Code 3720-v and Code 3721-v, each ofwhich is reconstituted by dissolving peptides in 0.5 ml of DMSO at the concentration of 2 mM (1 mM, eachreference compound)3) Enzyme solution: an enzyme of interest in an appropriate buffer
4) Buffer– 232 –

FRETS (Peptide) Library (continued)
Procedure for the deduction of the substrate specificity of an enzyme with unidentified
cleavage specificity
Choose the proper conditions for the measurement, such as substrate concentration and sensitivity setting,depending on the purpose of the experiment and the instrument available. Described here is one of the recommended
procedures for determining the enzymatic cleavage site by the combination of the fluorometric analysis and liquid
chromatography-mass spectrometry (LC-MS) analysis.

i) Primary screening: selection of the favored Xaa
1980 μl of an appropriate buffer (10 μM)

・Reference compounds solution for primary screening (PR solution): Dilute 20 μl of the above reference compounds
stock solution with 1980 μl of an appropriate buffer (10 μM)
1) Set a fluorescence spectrophotometer at λex = 340 nm and λem = 440 nm
2) Mix one of the PS solution and the PR solution in ratios of 10/0, 9/1, 8/2, 5/5 and 0/10
3) Measure the fluorescence of the prepared solutions to obtain the calibration curve for the cleaved products
4) Pipette 200 μl each of all PS solutions into the cells and incubate them in the fluorescence spectrophotometer for
3 min (temperature equilibration)5) Measure the fluorescence of each solution (initial fluorescence blank)
6) Add an appropriate volume of enzyme solution
7) Record the increase of the fluorescence intensity8) Terminate the enzymatic reaction by using a proper inhibitor (leupeptin, E-64, pepstatin, EDTA and so on) or
changing the pH of the reaction medium (using TCA, AcOH, NaOH and so on)9) Choose the best Xaa-containing substrate for secondary screeningii) Secondary screening: identification of the specificity of the enzyme (I)・ Substrate solution for secondary screening (SS solution) : Dilute 200 μ l of the stock solution of the best
Xaa-containing substrate chosen by the above primary screening with 1800 μl of an appropriate buffer (100 μM)

・Reference compounds solution for secondary screening (SR solution): Dilute 200 μl of the above referencecompounds stock solution with 1800 μl of an appropriate buffer (100 μM)
1) Set a fluorescence spectrophotometer at λex = 340 nm and λem = 440 nm
2) Mix the SS solution and the SR solution in ratios of 100/0, 95/5, 90/10, 80/20, 50/50 and 0/100
3) Measure the fluorescence of the prepared solutions to obtain the calibration curve for the cleaved products
4) Pipette 200 μl of the SS solution into the cells and incubate them in the fluorescence spectrophotometer for 3 min(temperature equilibration)5) Measure the fluorescence of each solution (initial fluorescence blank)
6) Add an appropriate volume of enzyme solution
7) Record the increase of the fluorescence intensity8) Terminate the enzymatic reaction by using a proper inhibitor or changing the pH of the reaction medium uponcompletion of the reaction at the points of 0%, 5%, 10% and 20% of the total
9) Subject 100 μl aliquots to LC-MS– 233 –

Enzyme Substrates

・Substrate solution for primary screening (PS solution): Dilute 20 μl of each of the above substrate stock solution with

FRETS (Peptide) Library (continued)iii) LC-MS: identification of the specificity of the enzyme (II)・Analytical conditions
column: ODS
eluant: A) H2O containing 0.05% TFA, B) CH3CN containing 0.05% TFA
gradient: 10% to 40% B) in A) over 50 min
detection: UV at 220 nm and 400 nm or fluorescence1) Inject 100 μl aliquots of each terminated solution at different stage of the reaction2) Measure the MW of the cleaved product(s) in the peak(s) with the absorbance at 220 nm but not with 400 nm[identification of the N-terminal segment(s)]3) Deduce their structure from the attached list of the theoretical MW for the cleaved products* Comment 1: If the N-terminal segment has the identical retention time to the C-terminal segment or one of the starting
uncleaved substrates, detection of the products by fluorescence is recommended.
* Comment 2: In the accidental case where the two products with the same MW (ex. Zaa-Yaa=Phe-Asp and Val-Tyr, Glu-Asp
and Phe-Pro) are generated from one of the substrate, their analyses should be carried out by MS-MS sequencing and/or by
Edman degradation.

Usefulness and limitation of FRETS-25Xaa series for screening of substrate specificities ofproteases
We have confirmed that FRETS-25Xaa series are effectively used for the assay of numerous proteases such astrypsin, chymotyrpsin, elastase, thrombin, papain, calpain, pepsin and thermolysin. However, they did not work wellfor the assay of caspase-3 and furin, probably because they have only three changeable sites (Zaa-Yaa-Xaa) in each
substrate (deficiency of P4 site). This fact implies that FRETS-25Xaa might not be applicable to the assay of an enzyme
with wide range interacting sites with substrate.

Custom services for secondary screening (Domestic Service only)
For the procedure iii) above using FRETS25-Xaa library, we will accept the analysis of the enzymatic reaction
mixture by ESI-MS in a LC mode. The analytical data to identify the specificity of the enzyme of interest will be
provided within 3 weeks. Please refer other conditions concerning this custom service on page 360 in this catalog(only in Japanese). For further information, please contact us at custom＠peptide.co.jp (E-mail).

References of FRETS-25Xaa series
1) K. Takada, M. Tsunemi, Y. Nishiuchi, and T. Kimura, A Fluorescence Resonance Energy Transfer Substrate (FRETS) Library for
Determining Protease Specificity. Peptide Revolution: Genomics, Proteomics & Therapeutics (Proceedings of the 18th American
Peptide Symposium), 327 (2003).
2) S. Tanskul, K. Oda, H. Oyama, N. Noparatnaraporn, M. Tsunemi, and K. Takada, Substrate specificity of alkaline serine proteinase
isolated from photosynthetic bacterium, Rubrivivax gelatinosus KDDS1. Biochem. Biophys. Res. Commun., 309, 547 (2003).

– 234 –

FRETS (Peptide) Library (continued)
Code

Compound3701-v

FRETS-25Ala-20

(Trifluoroacetate Form)

Price:YenVial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Ala-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
FRETS-25Arg-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Arg-Ala-Phe-Pro-Lys(Dnp)-D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3703-v

FRETS-25Asn-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Asn-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3704-v

FRETS-25Asp-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Asp-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3705-v

FRETS-25Gln-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Gln-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3706-v

FRETS-25Glu-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Glu-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3707-v

FRETS-25Gly-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Gly-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library– 235 –

Enzyme Substrates

3702-v

FRETS (Peptide) Library (continued)
Code

Compound3708-v

FRETS-25His-20

(Trifluoroacetate Form)

Price:YenVial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-His-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3709-v

FRETS-25Ile-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Ile-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3710-v

FRETS-25Leu-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Leu-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3711-v

FRETS-25Lys-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Lys-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3712-v

FRETS-25Met-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Met-Ala-Phe-Pro-Lys(Dnp)-D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3713-v

FRETS-25Phe-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Phe-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3714-v

FRETS-25Pro-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Pro-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library– 236 –

FRETS (Peptide) Library (continued)
Code

Compound3715-v

FRETS-25Ser-20

(Trifluoroacetate Form)

Price:YenVial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Ser-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
FRETS-25Thr-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Thr-Ala-Phe-Pro-Lys(Dnp)-D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3717-v

FRETS-25Trp-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Trp-Ala-Phe-Pro-Lys(Dnp)-D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library
3718-v

FRETS-25Tyr-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Tyr-Ala-Phe-Pro-Lys(Dnp)-D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library3719-v

FRETS-25Val-20

(Trifluoroacetate Form)

Vial

1 μmol

10,000D-A2pr(Nma)-Gly-[Phe/Ala/Val/Glu/Arg]-[Pro/Tyr/Lys/Ile/Asp]-Val-Ala-Phe-Pro-Lys(Dnp)- D-Arg- D-Arg
A2pr(Nma):N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid
(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)

Fluorescence-Quenching Substrate Library– 237 –

Enzyme Substrates

3716-v

FRETS (Peptide) Library (continued)
Code

CompoundPrice:Yen

3720-v

FRETS-25-STD1-20

D-A2pr(Nma)-GlyVial

1 μmol2,000(A2pr(Nma): N β-[2-(Methylamino)benzoyl]-2,3-diaminopropionic acid)(M.W. 294.31)

C13H18N4O4

HNO
D-A2pr-Gly

Standard Compound 1 for Fluorescence-Quenching Substrate Library
FRETS-25Xaa Series
3721-v

FRETS-25-STD2-20

(Trifluoroacetate Form)

Vial

Ala-Phe-Pro-Lys(Dnp)-D-Arg-D-Arg(Lys(Dnp): N ε-(2,4-Dinitrophenyl)lysine)(M.W. 940.02)

1 μmolNO2

C41H61N15O11

NO2

Ala-Phe-Pro-Lys-D-Arg-D-Arg

Standard Compound 2 for Fluorescence-Quenching Substrate Library
FRETS-25Xaa Series– 238 –

2,000

Peptide Tools
Code

CompoundPrice:Yen

3402-sNew

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

(Trifluoroacetate Form)

Vial

0.1 mg35,000

Enzyme Substrates

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)

3173-v-20

Vial

Biotinyl-Asp-Glu-Val-Asp-H (aldehyde)[Biotin-DEVD-CHO]

1 mg

10,000

Biotinyl-L-aspartyl-L-glutamyl-L-valyl-L-aspart-1-al(M.W. 686.73)

C28H42N6O12S

O[178603-73-1]

Synthetic Product
O

OH

O

NH

O

O

H
N

HN

H
N

N
H
S

N
H
O

H
OH

O
O
O

OH

Inhibitor for Caspase-3/7/8
1) D.W. Nicholson, A. Ali, N.A. Thornberry, J.P. Vaillancourt, C.K. Ding, M. Gallant, Y. Gareau, P.R. Griffin,
M. Labelle, Y.A. Lazebnik, N.A. Munday, S.M. Raju, M.E. Smulson, T.-T. Yamin, V.L. Yu, and D.K. Miller,
Nature, 376, 37 (1995).

– 239 –

Peptide Tools (continued)
Code

Compound3401-vTMRIA-K4

New

-20

Price:Yen
Vial

10 μg

16,000(Trifluoroacetate Form)

S-[2-({4-[3,6-Bis(dimethylamino)xanthylium-9-yl]-3carboxyphenyl}amino)-2-oxoethyl]-Cys-(Lys-Ile-Ala-Ala-Leu-Lys-Glu)4(M.W. 3578.4)

C169H282N40O42S

Fluorophore Peptide in Coiled-Coil Tag-Probe Labeling System
Genetic fusion of a fluorescent protein to a target protein for specific labeling in living cells has been widelyused. However, the use of fluorescent proteins with a considerable size, such as GFP (ca 27 kDa), may give
artifactual results, for example, formation of aggregates or impairment of protein function. Post-translationallabeling methods with smaller fluorophores are superior to those with fluorescent proteins.
Recently, Professor Matsuzaki of Kyoto University developed a useful receptor detection method called"coiled-coil tag-probe system" 1). This is a rapid method with a small tag (21 amino acids) for the fluorescencelabeling of cell-surface receptors using a high affinity coiled-coil formation without metals or enzymes. The
concept of this method is as follows: 1) E3 [E3 = (EIAALEK)3] is fused to the expressed receptor of interest as thetag, 2) K4 [K4 = (KIAALKE) 4 ] probe is labeled by the fluorophore at its α -amino group, such as
tetramethylrhodamine (abbreviated as TMR-K4), and 3) interaction of E3 tag with TMR-K4 probe by forming
heterodimeric coiled-coil makes the detection of the expressed receptor in living cells possible. Labeling by
TMR-K4 is sensitive (Kd = 6 nM) as well as non-toxic to cells. A low concentration of 20 nM is sufficient forpractical use.
In collaboration with Professor Matsuzaki, we have now successfully synthesized an analog of TMR-K4
called TMRIA-K4 [TMRIA = tetramethylrhodamine-5-iodoacetamide]. Actually, in contrast to TMR-K4 inwhich the fluorophore was attached to the α-amino group, the fluorophore functionality of TMRIA-K4 wasintroduced via the side-chain SH group of the Cys residue, which was extended at the amino-terminus of K4.
We have confirmed this novel probe exhibits compatible characteristics to TMR-K4 (Kd = 2 nM).
This newly designed fluorescent-tag probe, TMRIA-K4, should be an alternative to the originally designed
TMR-K4, which is now available from Peptide Institute, Inc.
1) Y. Yano, A. Yano, S. Oishi, Y. Sugimoto, G. Tsujimoto, N. Fujii, and K. Matsuzaki, ACS Chem. Biol., 3, 341, (2008).
(TMR-K4; Reference Paper to TMRIA-K4 )• This compound is distributed through Peptide Institute, Inc. under the license of Kyoto University.

– 240 –

Peptide Tools (continued)
Code

Compound4075-v[Tyr8]-Bradykinin
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Tyr-Arg-20

(M.W. 1076.2)

Price:Yen

C50H73N15O12Vial

0.5 mg3,500[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)-20

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

C59H82N16O13

Vial

0.5 mg3,200[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)

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

0.1 mg14,000(Disulfide bond between Cys10-Cys26)(M.W. 3627.2)

C152H253N51O44S4
Purity Information : QX See page IV (XVI)For Radioimmunoassay
4141-s-20

Tyrosyl-CRF (Human, Rat)
Tyrosyl-Corticotropin Releasing Factor (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(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.

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.)– 241 –

Enzyme Substrates

4056-v

Peptide Tools (continued)
Code

Compound4038-v[Tyr1]-Somatostatin
Tyr-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-ThrPhe-Thr-Ser-Cys-20

Price:Yen
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)

4059-v-20

[Tyr8]-Substance P
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Tyr-Gly-LeuMet-NH2(M.W. 1363.6) C63H98N18O14S [55614-10-3]
Purity Information : Qx See page IV (XVI)For Radioimmunoassay– 242 –

Vial

0.5 mg4,900

Enzymes
Code

CompoundPrice:Yen

3504

Thermolysin
100 mg(Daiwa Kasei K.K.)
1g(Crystallized and lyophilized from Bacillus thermoproteolyticus)
Powder containing ca. 30% buffer salts as calcium and sodium acetate
ca. 8000 PU/mg protein

5,800
32,0004

Enzyme Substrates– 243 –

Polypeptides
Code

CompoundPrice:Yen

4005(Pro-Pro-Gly)5 • xH2O

-20

(M.W. 1274.4)

25 mg
100 mg
1g

C60H87N15O16
Purity: higher than 97% by HPLC

5,000
14,700112,000

1) K. Kivirrikko, K. Suga, Y. Kishida, S. Sakakibara, and D.J. Prockop, Biochem. Biophys. Res. Commun.,45, 1591 (1971). (Chem. Synthesis & Biochem.)

4006(Pro-Pro-Gly)10 • xH2O

-20

(M.W. 2530.8)

25 mg
100 mg
1g

C120H172N30O31
Purity: higher than 95% by HPLC

7,300
22,000180,000

1) S. Sakakibara, Y. Kishida, Y. Kikuchi, R. Sakai, and K. Kakiuchi, Bull. Chem. Soc. Jpn., 41, 1273 (1968).
(Chem. Synthesis)4032(Pro-Hyp-Gly)5 • xH2O

-20

(M.W. 1354.4)

25 mg
100 mg

C60H87N15O21

35,000120,000

Purity: higher than 96% by HPLC
1) S. Sakakibara, K. Inouye, K. Shudo, Y. Kishida, Y. Kobayashi, and D.J. Prockop, Biochim. Biophys. Acta,
303, 198 (1973). (Chem. Synthesis)4033(Pro-Hyp-Gly)10 • xH2O

-20

(M.W. 2690.8)

25 mg
100 mg

C120H172N30O41
Purity: higher than 90% by HPLC

52,000185,000

1) S. Sakakibara, K. Inouye, K. Shudo, Y. Kishida, Y. Kobayashi, and D.J. Prockop, Biochim. Biophys. Acta,
303, 198 (1973). (Chem. Synthesis)3063

Poly-L-Glutamic Acid Sodium Salt

2～10

M.W. ＞8000, cut off by dialysis,

0.1 g
1g

6,000
30,000

0.1 g
1g

6,000
30,000

0.1 g
1g

6,000
30,000NCA polymerized product3056

Poly-L-Lysine Hydrobromide

2～10

M.W. ＞8000, cut off by dialysis,
NCA polymerized product[25988-63-0]

3075

Poly-L-Lysine Hydrochloride

2～10

M.W. ＞8000, cut off by dialysis,
NCA polymerized product[26124-78-7]– 244 –

Oligopeptides
Dipeptides
CompoundQuantity

Price:Yen

Page

3085

β-Ala-His[Carnosine]

1g
5g

2,800
6,800

208

2～10

3080

Glu-Glu

0.1 g
1g

3,400
17,800216

Gly-Gly

5g
25 g
100 g

1,800
2,800
7,000

217

Gly-Leu

0.1 g
1g
5g

1,700
3,100
9,000

217

Gly-Phe

0.1 g
1g

1,800
3,200

217

Gly-Phe-NH2 • AcOH

0.1 g
1g

2,300
7,100

217

Gly-Pro

0.1 g
1g

1,900
5,000

217

His-Leu

0.1 g
1g

2,500
8,800

218

Leu-Gly • 1/2 H2O

0.1 g
1g

2,000
4,600

218

25 mg
100 mg

4,100
11,40095-20cyclo (Leu-Gly)[Morphine Tolerance Peptide]3152

Met-Met

0.1 g
1g

3,200
15,000219

Pyr-Ala

0.1 g
1g

2,700
11,400

223

2～10

3028
2～10

3022
2～10

3053
2～10

3023
2～10

3052
2～10

3065
2～10

3024
2～10

4070

2～10

3079
2～10

– 245 –

Enzyme Substrates

CodeTripeptides
Code

CompoundQuantity

Price:Yen

Page

3050
2～10

Glu(Cys-Gly)[Glutathione; GSH]

1g
5g
25 g

1,800
2,700
6,100

217

3061

Gly-Gly-Gly

1g
5g
25 g

2,600
7,000
27,500217

Gly-Gly-His

0.1 g
1g

4,400
30,000217

Gly-His-Lys • AcOH • H2O[Liver-Cell Growth Factor]

25 mg
100 mg

7,500
15,40089

25 mg
100 mg

4,800
13,300187-20

Ile-Pro-Ile • H2O[Diprotin A]

3025

Leu-Gly-Gly

0.1 g
1g

2,400
9,700

218

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

25 mg
100 mg

2,200
5,000

94

Pyr-His-Pro-NH2 • H2O[Thyrotropin Releasing Hormone; TRH]

25 mg
100 mg

4,500
12,200147

Thr-Val-Leu[Schizophrenia Related Peptide]

25 mg
100 mg

8,300
17,000138

25 mg
100 mg24,00075,00023-20

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

3119

Gly-Gly-Tyr-Arg • AcOH •2H2O

0.1 g
1g

5,800
30,000217

Phe-Met-Arg-Phe-NH2 • 1 1/2 AcOH • 2H2O
[FMRF-Amide]

25 mg
100 mg23,00065,00095

Thr-Lys-Pro-Arg • 2AcOH • 4H2O
[Tuftsin]

25 mg
100 mg12,00036,000147

Trp-Met-Asp-Phe-NH2 • HCl • H2O[CCK-Tetrapeptide (30-33)]

25 mg
100 mg

9,000
27,00036

Tyr-Pro-Phe-Phe-NH2 • AcOH • H2O[Endomorphin-2]

25 mg

48,00058

Tyr-Pro-Trp-Phe-NH2 • AcOH • H2O[Endomorphin-1]

25 mg

48,000

57

2～10

3076
2～10

4022
-20

4132

2～10

4024
-20

4011
-20

4061
-20

Tetrapeptides
4171

2～10

4142
-20

4020
-20

4083
-20

4334
-20

4333
-20

– 246 –