Species predicted to react based on 100% sequence homology:Bovine, Dog, Pig
Specificity / Sensitivity
Cleaved Caspase-3 (Asp175) Antibody (Alexa Fluor®488 Conjugate) detects endogenous levels of the large fragment (17/19 kDa) of activated caspase-3 resulting from cleavage adjacent to aspartic acid 175. The antibody does not recognize full length caspase-3 or other cleaved caspases. Alexa Fluor®488 conjugates are excited at 494 nm and emit at 520 nm.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino-terminal residues adjacent to Asp175 of human caspase-3. Antibodies are purified by protein A and peptide affinity chromatography. The antibody was conjugated to Alexa Fluor®488 under optimal conditions with an F/P ratio of 2-6.
Description
This Cell Signaling Technology antibody is conjugated to Alexa Fluor®488 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cleaved Caspase-3 (Asp175) Antibody #9661.
Background
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 aspartic acid at the P1 position (2).