Anti-Caspase-3 (P10) /CASP3 Antibody Picoband® Fluoro594 Conjugated

Caspase 3 is a caspase protein which interacts with Survivin, XIAP, CFLAR, Caspase 8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located at 4q35 encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7, and 9; and the protein itself is processed by caspases 8, 9, and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. And the caspase-3 activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the caspase-3 influence on bone mineral density should be considered in any in vivo application of caspase-3 inhibitors to the treatment of human disease. In erythroid precursors undergoing terminal differentiation, Hsp70 prevents active CASP3 from cleaving GATA1 and inducing apoptosis.

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

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. Chang, J.; Wei, L.; Otani, T.; Youker, K. A.; Entman, M. L.; Schwartz, R. J. : Inhibitory cardiac transcription factor, SRF-N, is generated by caspase 3 cleavage in human heart failure and attenuated by ventricular unloading. Circulation 108: 407-413, 2003. 2. Miura, M.; Chen, X.-D.; Allen, M. R.; Bi, Y.; Gronthos, S.; Seo, B.-M.; Lakhani, S.; Flavell, R. A.; Feng, X.-H.; Robey, P. G.; Young, M.; Shi, S. : A crucial role of caspase-3 in osteogenic differentiation of bone marrow stromal stem cells. J. Clin. Invest. 114: 1704-1713, 2004. 3. Ribeil, J.-A.; Zermati, Y.; Vandekerckhove, J.; Cathelin, S.; Kersual, J.; Dussiot, M.; Coulon, S.; Moura, I. C.; Zeuner, A.; Kirkegaard-Sorensen, T.; Varet, B.; Solary, E.; Garrido, C.; Hermine, O. : Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1. Nature 445: 102-105, 2007.