Anti-Caspase-3

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Caspase-3 is an enzyme which interacts with Survivin, XIAP, CFLAR, CASP8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located on 4q35 encodes a protein that is a member of the cysteine-aspartic acid protease family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. They 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. CASP3 is the predominant cysteine-aspartic acid protease involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimers disease. And protein activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the proteins 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. Protein function: 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. [The UniProt Consortium]