The cleaved-CASP3 (D175) antibody is raised in rabbits against the synthesized peptide mapping within N-terminal residues adjacent to D175 of human CASP3 protein. It occurs as an unconjugated IgG. It has undergone affinity-chromatography purification using epitope-specific immunogen. This cleaved CASP3 (D175) antibody detects endogenous levels of the large fragment of activated caspase-3 derived from cleavage adjacent to D175 and fails to recognize the full-length caspase-3 or other cleaved caspases. It can cross-react with human, mouse, and rat CASP3 protein. And it is available in WB, IHC, and ELISA assays. The target protein CASP3 is the main executioner of apoptosis, and its activation requires proteolytic cleavage of its zymogen into activated p17 and p12 fragments.
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