Replaces Prod. #: BML-P130
Substrate for porcine calpain I and II. Also cleaved by papain and E. coli protease Ti. Ex.: 340-360nm, Em.: 440-460nm. This substrate is useful for inhibitor screening and kinetic analysis.
Product Details
| Alternative Name: | Suc-LY-AMC |
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| Sequence: | Suc-Leu-Tyr-AMC (AMC=7-Amino-4-methylcoumarin) |
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| Formula: | C29H33N3O8 |
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| MW: | 551.6 |
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| CAS: | 94367-20-1 |
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| Purity: | ≥95% |
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| Appearance: | White to off-white powder. |
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| Solubility: | Soluble in 80% acetic acid, DMSO or methanol. |
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| Shipping: | Ambient Temperature |
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| Long Term Storage: | -20°C |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Cisplatin-induced apoptosis inhibits autophagy, which acts as a pro-survival mechanism in human melanoma cells: B. Del Bello, et al.; PLoS One
8, e57236 (2013),
Abstract;
Full Text
Synthesis of a reported calpain inhibitor isolated from Streptomyces griseus: I.O. Donkor & M.L. Sanders; Bioorg. Med. Chem. Lett.
11, 2647 (2001),
Abstract;
Na+, K+-specific inhibition of protein and peptide hydrolyses by proteasomes from human hepatoma tissues: J.H. Seol, et al.; FEBS Lett.
247, 197 (1989),
Abstract;
Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides: K.M. Woo, et al.; J. Biol. Chem.
264, 2088 (1989),
Abstract;
Full Text
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),
Abstract;
