Caspase-3 (Pro)

GWB-24C271

A synthetic peptide corresponding to residues following Ser29 of human caspase-3 (N-terminus of p17 subunit) was used as immunogen. This antibody only detects pro-form (35kD) of caspase-3 and does not recognize any cleaved caspases.

WB: 1:1 000 - 10 000IHC: 1:250ICC: 1:250FC: 1:50IP: 1:100. Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the initiation and execution of apoptosis. Caspase-3 (apopain SCA-1 Yama and CPP32) is a member of the apoptosis execution functional group of caspases and is either partially or totally responsible for the proteolytic cleavage of many key proteins during apoptosis such as poly (ADP-ribose) polymerase (PARP) (1 2 3). Caspase-3 is a cytosolic protein found in cells as an inactive 32 kDa proenzyme. It is activated by proteolytic cleavage into two active subunits only when cells undergo apoptosis (3). 1. Fernandes-Alnemri T. et al. CPP32 a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. J. Biol. Chem. 269:307612. Tewari M. et al. Yama/CPP32 beta a mammalian homolog of CED-3 is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 8013. Nicholson D. W. et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376: 374. Manufactured under U. S. Patents No. 5 675 063 and 7 429 487