Detection of pro-CASP2 (p51) , an intermediate cleavage product of CASP2 (p32) and activated CASP2 (p19) in FDC-P1 cells (mouse IL-3 dependent promyelocytic line) during growth factor with drawal induced apoptosis. Activation of CASP2 is inhibited in the presence of the caspase inhibitor Z-VAD-FMK.
Western blot analysis of cell lysates from human and mouse cell lines with CASP2 monoclonal antibody, clone 11B4 (Cat # MAB3485). Clone 11B4 demonstrates its ability to recognize an approximately 51 kDa protein that corresponds to endogenous pro-CASP2. Hsp-70 was used as an equal loading control, and -/- CASP2 cells were used as a negative control.
This gene encodes a protein which 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 which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. The proteolytic cleavage of this protein is induced by a variety of apoptotic stimuli. Alternative splicing of this gene results in multiple transcript variants that encode different isoforms. [provided by RefSeq