Cleaved-Caspase 4/5 p20 polyclonal antibody

CASP4 (caspase 4) 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 composed of a prodomain and a large and small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This caspase is able to cleave and activate its own precursor protein, as well as caspase 1 precursor. When overexpressed, caspase 4 induces cell apoptosis. Alternative splicing results in transcript variants encoding distinct isoforms.

Western blot analysis of Cleaved-Caspase 4/5 p20 in Jurkat lysates using Caspase 4/5 antibody. The lane on the right is blocked with the Caspase 4/5 peptide.