Caspase-6 Antibody recognizes endogenous levels of both full length caspase-6 (35 kDa) and the small subunit of caspase-6 resulting from cleavage at aspartic acid 193 (15 kDa). This antibody does not recognize other caspases.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding the cleavage site of caspase-6. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Caspase-6 (Mch2) is one of the major executioner caspases functioning in cellular apoptotic processes (1,2). Upon apoptotic stimulation, initiator caspases such as caspase-9 are cleaved and activated (3). The activated upstream caspases further process downstream executioner caspases, such as caspase-3 and caspase-6, by cleaving them into large and small subunits, thereby initiating a caspase cascade leading to apoptosis (4,5). One of the major targets for caspase-6 is the membrane associated protein lamin A (6). The cleavage of this protein causes cell membrane malfunction, membrane blebbing and eventual cell death.