Suc-Leu-Leu-Val-Tyr-AMC

Suc-Leu-Leu-Val-Tyr-AMC

Product Number: 4011369

CAS Number: 94367-21-2

€ 178.70 – € 535

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Product Description

The fluorogenic substrate Suc-LLVY-AMC is used for measuring the chymotrypsin-like activity of the 20S proteasome, in combination with e.g. Bz-VGR-AMC (for assaying its trypsin-like activity) and Z-LLE-AMC (for determining its PGPH activity). Suc-LLVY-AMC is also cleaved by a chymotrypsin-like enzyme from sperm extract of the ascidian Halocynthia roretzi, a strong inhibitor of fertilization. The substrate has also been used to analyze the chymotrypsin-like activity of trypsins as well as chymase from rat mast cells. Furthermore, Suc-LLVY-AMC is a substrate for carboxypeptidase Y, proteinase yscE (kexin), ingensin, as well as for porcine calpain isozymes I and II and for papain.

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New synthetic substrates for pepsin.

K.Inouye et al., Biochemistry, 5, 2473 (1966)

An ATP-dependent protease and ingensin, the multicatalytic proteinase, in K562 cells.

T.Tsukahara et al., Eur. J. Biochem., 177, 261 (1988)

Ascidian sperm chymotrypsin-like enzyme; participation in fertilization.

H.Sawada et al., Experientia, 39, 377 (1983)

Purification and characterization of a high-molecular-weight protease, ingensin, from human placenta.

M.Nojima et al., J. Biochem. (Tokyo), 99, 1605 (1986)

Purification and gene cloning of Fundulus heteroclitus hatching enzyme. A hatching enzyme system composed of high choriolytic enzyme and low choriolytic enzyme is conserved between two different teleosts, Fundulus heteroclitus and medaka Oryzias latipes.

M.Kawaguchi et al., FEBS J., 272, 4315 (2005)

Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival.

W.Heinemeyer et al., EMBO J., 10, 555 (1991)

Purification and gene cloning of Fundulus heteroclitus hatching enzyme. A hatching enzyme system composed of high choriolytic enzyme and low choriolytic enzyme is conserved between two different teleosts, Fundulus heteroclitus and medaka Oryzias latipes.

M.Kawaguchi et al., FEBS J., 272, 4315 (2005)

Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival.

W.Heinemeyer et al., EMBO J., 10, 555 (1991)

Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin.

L.Graf et al., Biochemistry, 26, 2616 (1987)

A new structural class of selective and non-covalent inhibitors of the chymotrypsin-like activity of the 20S proteasome.

C.Garcia-Echeverria et al., Bioorg. Med. Chem. Lett., 11, 1317 (2001)

Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates.

T.Sasaki et al., J. Biol. Chem., 259, 12489 (1984)

Molecular weight: 763.89

Sum Formula: C₄₀H₅₃N₅O₁₀

Storage Temperature: < -15°C

Synonyms: Chymotrypsin Substrate III, Fluorogenic

One Letter code: Suc-LLVY-AMC

Source: Synthetic

Old Product Number: I-1395

Substrates
Chymase
Papain
Multicatalytic Endopeptidase Complex
Calpain
Carboxypeptidase C
Calpain-2
Envelysin
Proteasome Endopeptidase Complex
Kexin

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