Apoptosis Marker: Cleaved Caspase-3 (Asp175) Western Detection Kit offers an efficient way of detecting caspase-3 processing and activation by Western blotting. The kit contains enough primary and secondary antibodies to perform 10 Western mini blots, as well as a set of pre-stained and biotinylated markers, cell lysates and LumiGLO® reagent.
Cleaved Caspase-3 (Asp175) Antibody detects endogenous levels of the large fragment (17/19 kDa) of activated caspase-3 resulting from cleavage adjacent to (Asp175). This antibody does not recognize full length caspase-3 or other cleaved caspases. Caspase-3 Antibody detects endogenous levels of full length caspase-3 (35 kDa) and the large fragment of caspase-3 resulting from cleavage (17 kDa).
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding the cleavage site and the amino terminus of the large fragment of human caspase-3. Antibodies are purified by protein A and peptide affinity chromatography.
Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (1). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires the aspartic acid residue at the P1 position (2).
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