Anti-Caspase-3 (P17) /CASP3 Antibody Picoband® Fluoro488 Conjugated

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.

Caspase-3; CASP-3;3.4.22.56; Apopain; Cysteine protease CPP32; CPP-32; LICE; Protein Yama; SREBP cleavage activity 1; SCA-1; Caspase-3 subunit p17; Caspase-3 subunit p12; Casp3; Cpp32

Alzheimer's Disease, Apoptosis, Apoptotic Markers, Cancer, Caspases, Cell Biology, Cell Death, Intracellular, Invasion/Microenvironment, Neurodegenerative Disease, Neurology Process, Neuroscience

Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly (ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity) . Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. .

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. 2. 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. 3. 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.