

Supplier:
BOSTER IMMUNOLEADERCat no: PA1961
Polyclonal Anti-CASP3(p17)
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SPECIFICATIONS
Price
200.00 USD
Catalog Number
PA1961
Size
100ug/vial
Applications
WB
Reactivities
Hum
Form
Lyophilized
Format
Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.
Gene Id
CASP3
References
1. Fernandes-Alnemri, T., Litwack, G., Alnemri, E. S. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. J. Biol. Chem. 269: 30761-30764, 1994. \n2. Tewari, M., Quan, L. T., O'Rourke, K., Desnoyers, S., Zeng, Z., Beidler, D. R., Poirier, G. G., Salvesen, G. S., Dixit, V. M. Yama/CPP32-beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 801-809, 1995.\n3. Tiso, N., Pallavicini, A., Muraro, T., Zimbello, R., Apolloni, E., Valle, G., Lanfranchi, G., Danieli, G. A. Chromosomal localization of the human genes, CPP32, Mch2, Mch3, and Ich-1, involved in cellular apoptosis. Biochem. Biophys. Res. Commun. 225: 983-989, 1996.\n
Swiss Prot
P42574
Storage Temp
At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time.Avoid repeated freezing and thawing.
Additional Info
A synthetic peptide corresponding to a sequence at the N-terminal of human CASP3(p17)
Scientific Background
CASP3 (Caspase3 Apoptosis-Related Cysteine Protease), also known as YAMA, CPP32 or APOPAIN, is a caspase protein that interacts with caspase 8 and caspase 9. It is encoded by the CASP3 gene. The CASP3 protein is a member of the cysteine-aspartic acid protease (caspase) family. Tiso et al. (1996) used radiation hybrid mapping to localize the CPP32 gene to human chromosome 4q33-q35.1. Fernandes-Alnemri et al. (1994) found that overexpression of CPP32 in insect cells induced apoptosis. Coexpression of the 2 CPP32 subunits in insect cells also resulted in apoptosis. Tewari et al. (1995) showed that purified human ICE cleaved the Yama proenzyme into a proteolytically active form and that activated Yama cleaved PARP into the 85-kD apoptotic form.
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