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S1153

Sigma-Aldrich

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

calpain substrate

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About This Item

Empirical Formula (Hill Notation):
C29H33N3O8
CAS Number:
94367-20-1
Molecular Weight:
551.59
MDL number:
MFCD00057900
UNSPSC Code:
12352204
PubChem Substance ID:
24899464
NACRES:
NA.32

Quality Level

200

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
Levente E Dókus et al.
European journal of medicinal chemistry, 82, 274-280 (2014-06-11)
Calpains are intracellular cysteine proteases with important physiological functions. Up- or downregulation of their expression can be responsible for several diseases, therefore specific calpain inhibitors may be considered as promising candidates for drug discovery. In this paper we describe the

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