Cleaved-Caspase-5 p10 (S331) Polyclonal Antibody

CASP5 encodes 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 which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. Overexpression of the active form of caspase 5 induces apoptosis in fibroblasts. Max, a central component of the Myc/Max/Mad transcription regulation network important for cell growth, differentiation, and apoptosis, is cleaved by caspase 5; this process requires Fas-mediated dephosphorylation of Max. The expression of CASP5 is regulated by interferon-gamma and lipopolysaccharide. Alternatively spliced transcript variants have been identified for CASP5.

1 mg/ml

47814

-20°C for one year