Caspase 9, Apoptosis-Related Cysteine Peptidase (CASP9) (AA 364-405) antibody
|Synonyms||MCH6, APAF3, APAF-3, ICE-LAP6, CASPASE-9c, Mch6, AI115399, AW493809, Caspase-9, CASP9, LOC100101592|
Alternatives Western Blotting (WB)
|4 references available|
|Quantity||0.1 mg (0.5 mg/ml)|
|Price||Product not available in this region.|
|Immunogen||Human Caspase-9 Recombinant Protein|
Caspase 9 (ICE-LAP6, Mch-6, Apaf-3) is a member of a family of cysteine proteases which play a critical role in the induction of programmed cell death. Members of this family have been grouped according to sequence homology as being either ICE-like proteases (caspases 1, 4 and 5) or Ced-3- like proteases (caspases 3, 6, 7, 9 and 10a). Caspase-9 is produced as a 48 kD precursor (procaspase-9) which contains an N-terminal prodomain with high homology to caspase-2. Procaspase-9 may be processed into subunits which heterodimerize to form the active enzyme. Activation of caspase-9 occurs in the presence of cytochrome c (Apaf-2), following an interaction between caspase-9 and Apaf-1. Activation may also be triggered directly by the cytotoxic T-cell protease, granzyme B. Active caspase-9 cleaves and thus activates caspase-3 and is also a relevant target of active caspase-3. Caspase- 9 can also cleave the nuclear protein PARP. Northern blot analysis suggests that high expression of caspase-9 is found in the heart, testis and ovary.
Synonyms: ICE-LAP-6, Mch6, Apaf-3
1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
3. Please refer to us for technical protocols.
|Molecular Weight||46-48 kDa|
Related Products: ABIN967389
|Purification||Purified from tissue culture supernatant or ascites by affinity chromatography.|
|Buffer||Aqueous buffered solution.|
|Preservative||0.09% Sodium azide.|
|Storage||Store undiluted at 4°C.|
|Research Area||Apoptosis/Necrosis, Cancer|
|Restrictions||For Research Use only|
Duan, Chinnaiyan, Hudson et al.: "ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis." in: The Journal of biological chemistry, Vol. 271, Issue 3, pp. 1621-5, 1996 (PubMed).
Srinivasula, Fernandes-Alnemri, Zangrilli et al.: "The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32." in: The Journal of biological chemistry, Vol. 271, Issue 43, pp. 27099-106, 1996 (PubMed).
Cohen: "Caspases: the executioners of apoptosis." in: The Biochemical journal, Vol. 326 ( Pt 1), Issue 5693, pp. 1-16, 1997 (PubMed).
Li, Nijhawan, Budihardjo et al.: "Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade." in: Cell, Vol. 91, Issue 4, pp. 479-89, 1997 (PubMed).