Anti-Caspase 3/CASP3 Antibody Picoband® Fluoro488 Conjugated

Caspase 3 (caspase 3, apoptosis-related cysteine peptidase) is a caspase protein that interacts with caspase 8 and caspase 9, also known as Caspase-3, PARP CLEAVAGE PROTEASE, APOPAIN, CPP32, CPP32B, YAMA. It is a member of the cysteine-aspartic acid protease (caspase) family. PCR analysis of 16 human tissues revealed expression of full-length CASP3, as well as CASP3s at somewhat lower levels, in all tissues tested. Western blot analysis of 3 cell lines revealed the prominent CASP3 band at 32 kD and CASP3s at 20 kD. Several human cancer cell lines showed coexpression of both variants at the mRNA and protein levels. Overexpression of the catalytically inactive CASP3s by human kidney cells offered some resistance to inducers of apoptosis, and CASP3s accumulation could be enhanced with addition of proteasome inhibitors. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Alternative splicing of this gene results in two transcript variants that encode the same protein. Encoded by the CASP3 gene, CASP3 orthologs have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts. Nicholson et al. developed a potent peptide aldehyde inhibitor and showed that it prevented apoptotic events in vitro, suggesting that apopain/CPP32 is important for the initiation of apoptotic cell death.

Caspase-3; CASP-3;3.4.22.56; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1; Caspase-3 subunit p17; Caspase-3 subunit p12; CASP3; CPP32

A synthetic peptide corresponding to a sequence at the C-terminal of human Caspase 3, identical to the related mouse sequence, and different from the related rat sequence by one amino acid.

Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.

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. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. .

1. Huang, Y., Shin, N.-H., Sun, Y., Wang, K. K. W.Molecular cloning and characterization of a novel caspase-3 variant that attenuates apoptosis induced by proteasome inhibition.Biochem. Biophys. Res. Commun. 283: 762-769, 2001. 2. Nicholson, D. W., Ali, A., Thornberry, N. A., Vaillancourt, J. P., Ding, C. K., Gallant, M., Gareau, Y., Griffin, P. R., Labelle, M., Lazebnik, Y. A., Munday, N. A., Raju, S. M., Smulson, M. E., Yamin, T.-T., Yu, V. L., Miller, D. K. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376: 37-43, 1995.