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Key Documents

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S1153

Sigma-Aldrich

N-Succinyl-Leu-Tyr-7-amido-4-methylcoumarin

calpain substrate, solid

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About This Item

Fórmula empírica (notación de Hill):
C29H33N3O8
Número de CAS:
94367-20-1
Peso molecular:
551.59
MDL number:
MFCD00057900
UNSPSC Code:
12352204
PubChem Substance ID:
24899464
NACRES:
NA.32

product name

N-Succinyl-Leu-Tyr-7-amido-4-methylcoumarin, calpain substrate

form

solid

storage temp.

−20°C

SMILES string

CC(C)CC(NC(=O)CCC(O)=O)C(=O)NC(Cc1ccc(O)cc1)C(=O)Nc2ccc3C(C)=CC(=O)Oc3c2

InChI

1S/C29H33N3O8/c1-16(2)12-22(31-25(34)10-11-26(35)36)29(39)32-23(14-18-4-7-20(33)8-5-18)28(38)30-19-6-9-21-17(3)13-27(37)40-24(21)15-19/h4-9,13,15-16,22-23,33H,10-12,14H2,1-3H3,(H,30,38)(H,31,34)(H,32,39)(H,35,36)

InChI key

RIYLNECMTVNMSO-UHFFFAOYSA-N

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Substrates

Substrate for porcine calpain I and II.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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C Crawford
The Biochemical journal, 248(2), 589-594 (1987-12-01)
Inhibition of chicken calpain II by proteins of the cystatin superfamily and alpha 2-macroglobulin was investigated. Human liver cystatins A and B, human cystatin C, chicken cystatin and rat T-kininogen were found not to be inhibitory. Inhibition was, however, observed
Shisong Jing et al.
Virulence, 13(1), 578-588 (2022-04-02)
The resistance of Staphylococcus aureus (S. aureus) to various antibiotics has increased dramatically due to the misuse of antibiotics, and thus the development of new anti-infective drugs with new targets is urgently needed to combat resistance. Caseinolytic peptidase P is
T Sasaki et al.
The Journal of biological chemistry, 259(20), 12489-12494 (1984-10-25)
Homogeneous porcine calpain (Ca2+-dependent cysteine proteinase) was found to hydrolyze a variety of peptides and synthetic substrates. Leu-Trp-Met-Arg-Phe-Ala, eledoisin-related peptide, alpha-neoendorphin, angiotensin I, luteinizing hormone-releasing hormone, neurotensin, dynorphin, glucagon, and oxidized insulin B chain were cleaved with a general preference
Maira Cardoso et al.
Methods in molecular biology (Clifton, N.J.), 1915, 93-101 (2019-01-09)
Detecting calpain activity in Drosophila tissues is a fundamental tool to study calpain function. We use differential centrifugation to prepare membrane- versus cytosol-enriched fractions for measuring calpain activity with the fluorogenic substrate N-LY-AMC. With this method one can measure calpain
Quercetin Reduces the Virulence of S. aureus by Targeting ClpP to Protect Mice from MRSA-Induced Lethal Pneumonia.
Jing, et al.
Microbiology spectrum, 10, e0234021-e0234021 (2022)
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