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 the active (cleaved) form of Caspase-3 and does not recognize the pro form of Caspase-3.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
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).
Related Pathway
Apoptosis
MAPK signaling pathway
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Western blot analysis of Jurkat cell lysate using (A & B )anti-Pro-Caspase-3, dilution 1:10,000 (C & D) anti-Caspase-3, 1:500 dilution. (A & C) Jurkat cell lysate (B & D) Jurkat cell lysate + Camptothecin