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Caspase-3 (human), (recombinant)

BML-SE169-5000 5000 U 531.00 USD
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Product Details

Alternative Name:CPP32, Yama, Apopain
MW:17 + 12 kDa
Source:Produced in E. coli. Caspase-3 (CPP32; Yama; apopain) from human cDNA. The enzyme was cleaved and activated from the proenzyme
UniProt ID:P42574
Formulation:Liquid. In 50mM HEPES, pH 7.4, 100mM sodium chloride, 0.5% CHAPS, 1mM EDTA, 10% glycerol and 10mM dithiothreitol.
Purity:≥95% (SDS-PAGE)
Activity:100 U/µl
Specific Activity:One U=1 pmol/min using Ac-DEVD-pNA (200 µM; Prod. No. ALX-260-033) as substrate at 30°C
Application Notes:Can be used to study enzyme regulation and kinetics, cleave target substrates and screen for inhibitors.
Shipping:Dry Ice
Long Term Storage:-80°C
Handling:Avoid freeze/thaw cycles.
Scientific Background:The major effector caspase of apoptosis, caspase-3 is responsible for cleavage of multiple cellular targets.
Regulatory Status:RUO - Research Use Only

Product Literature References

Conjunctival epitheliopathy induced by topical exposure to bacterial peptidoglycan, muramyl dipeptide: M.P. Langford, et al.; Exp. Eye Res. 227, 109383 (2023), Abstract;
Caspase-10 affects the pathogenesis of primary biliary cholangitis by regulating inflammatory cell death: M. Cho, et al.; J. Autoimmun. 133, 102940 (2022), Abstract;
Enzyme-triggered compound release by using functionalized derivatives using antimicrobial peptide: S. Mizukami, et al.; Chem. Sci. 8, 3047 (2017), Abstract; Full Text
Approaches to design non-covalent inhibitors for human granzyme B (hGrB): M.S. Kim, et al.; Org. Biomol. Chem. 12, 8952 (2014), Abstract;
Propeptide-mediated inhibition of cognate gingipain proteinases: N.L. Huq, et al.; PLoS One 8, e65447 (2013), Abstract;
Vulnerable windows for developmental ethanol toxicity in the Japanese medaka fish (Oryzias latipes): S.L. Oxendine, et al.; Aquat. Toxicol. 80, 396 (2006), Abstract;
Protein kinase C delta blocks immediate-early gene expression in senescent cells by inactivating serum response factor: K. Wheaton, et al.; Mol. Cell Biol. 24, 7298 (2004), Abstract; Full Text
Cross-talk between calpain and caspase proteolytic systems during neuronal apoptosis: R.W. Neumar, et al.; J. Biol. Chem. 278, 14162 (2003), Abstract; Full Text
A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis: N. A. Thornberry et al.; J. Biol. Chem. 272, 17907 (1997), Abstract;
Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone: P. R. E. Mittl et al.; J. Biol. Chem. 272, 6539 (1997), Abstract;
Substrate specificities of caspase family proteases: R. V. Talanian et al.; J. Biol. Chem. 272, 9677 (1997), Abstract;

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