Anti-Capase-3 (P17) /CASP3 Antibody Picoband® fluoro594 Vervoeging

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

CASP3

12367

P70677

Mouse, Rat

No cross-reactivity with other proteins

A synthetic peptide corresponding to a sequence at the N-terminus of mouse Caspase-3 (P17), different from the related rat sequence by one amino acid.

Highest expression in spleen, lung, liver, kidney and heart. Lower expression in brain, skeletal muscle and testis.

Flow Cytometry

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

Immunogen affinity purified.

Liquid

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.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

31475 MW

No cross reactivity with other proteins.

6

Caspase-3

Cytoplasm.

Caspase-3

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.