Clone: LAAP6 96 2-22
Background: Caspases are key effectors of programmed cell death. They are synthesized as inactive proenzymes which are activated by cleavage at a specific aspartate residue to form two subunits. These subunits are normally linked together by a linker which may be involved in the regulation of the different caspases. Caspase-9 is a member of the CED-3 family and bear high similarity to caspase-3. Procaspase-9 can be activated by either caspase-3 or granzyme B, although they cleave the proenzyme to different size subunits. Cleavage by granzyme B produces an active enzyme which is capable of cleaving PARP. Also, the ability of caspase-3 to activate caspase-9 seems to suggest that caspase-9 is further downstream of caspase-3 and may be involved in later changes in cells observed undergoing apoptosis.
Positive Control: MCF-7 cell lines
Immunogen: Hybridoma produced by the fusion of splenocytes from mice immunized with recombinant human capase-9 protein and mouse myeloma cells.
Purification Method: Protein A/G Chromatography
Concentration: See vial for concentration
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide
References: 1. Cohen, G.M., et al. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326, 1-162. Stennicke, H.R., et al. Caspase-9 can be activated without proteolytic processing. J. Biol. Chem. 1999, 274, 8359-83623. Kuida, K. Caspase-9. Int. J. Biochem. Cell Biol. 2000, 32, 121-124
UniProt: P55211
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
English
Deutsch
