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.
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).
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