Caspase 9, Apoptosis-Related Cysteine Peptidase (CASP9) (N-Term,AA 1-134) antibody

Antigen: Caspase 9, Apoptosis-Related Cysteine Peptidase (CASP9)

Synonyms: MCH6, APAF3, APAF-3, ICE-LAP6, CASPASE-9c, Mch6, AI115399, AW493809, Caspase-9, CASP9, LOC100101592

Binding Site: N-Term,AA 1-134

Clonality: Monoclonal (44593)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB)

Catalog no.: ABIN967339

Additional Information

Alternative name: Caspase-9

Immunogen: Human caspase-9 fragment aa 1-134

Format: Liquid

Isotype: IgG1

Clone: 44593

Description: The caspase family of cysteine proteases plays a key role in apoptosis and inflammation. Caspases are synthesized as inactive proenzymes containing three domains, that are processed into large and small subunits that associate to form the active enzyme. Processing can occur in apoptotic cells by either transactivation, self-proteolysis or cleavage by another protease. While caspases share a common structure, there are some differences, such as the preferred substrate specificity. These sequence differences in specificity, as well as the size of the NH2 -terminal prodomain, can be used to catagorize the caspases into functional groups including apoptotic initiators (long prodomains), apoptotic executioners (short prodomains), and cytokine processors. Caspase-9 is a member of the apoptotic initiator group of caspases which include caspases-2, -8, and -10. Activation of caspase-9 occurs in the presence of cytochrome c, 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. The antibody recognizes the 47 kDa proform and 37 kDa cleaved form of human caspase-9. The N-terminal fragment (amino acids 1-134) of human caspase-9 was used as an immunogen.
Synonyms: ICE-LAP-6, Mch6, Apaf-3

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. 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.

Molecular Weight: 47, 37 kDa

Comments:

Related Products: ABIN967389

Application Details

Application Notes: Applications include western blot analysis (0.5 - 1.0 µg/ml). Jurkat cells (ATCC TIB-152) are suggested as a positive control. Antibodies-online offers several caspase-9 antibodies. A Jurkat model cell system was used to evaluate these antibodies, these results are summarized in the following table. However, actual bands observed could vary according to the cell model system or treatment used.

Concentration: 0.5 mg/ml

Purity: Purified

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

Images

Western blot analysis of caspase-9. Lysates from control (lanes 1-3) and amptothecin treated Jurkat cells (lanes 4-6) were probed with anti-human caspase-9 (clone 2-22, ABIN967339) at concentrations of: 1.0 (lane 1), 0.5 (lane 2), and 0.25 µg/ml (lane 3). Caspase-9 is identified as a band of 47 kDa (proform), and 37 kDa (intermediate) in treated cells, and the 47 kDa band in control cells.

Publications

Product: 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).

Thornberry, Rano, Peterson et al.: "A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis." in: The Journal of biological chemistry, Vol. 272, Issue 29, pp. 17907-11, 1997 (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).

Wolf, Green: "Suicidal tendencies: apoptotic cell death by caspase family proteinases." in: The Journal of biological chemistry, Vol. 274, Issue 29, pp. 20049-52, 1999 (PubMed).