Caspase 7, Apoptosis-Related Cysteine Peptidase (CASP7) (AA 25-42) antibody

Antigen: Caspase 7, Apoptosis-Related Cysteine Peptidase (CASP7)

Synonyms: MCH3, CMH-1, ICE-LAP3, Mch3, mCASP-7, AI314680, ICE-IAP3, caspase-7, xCaspase-7, mch3, cmh-1, ice-lap3, CASP7, LOC100101591

Binding Site: AA 25-42

Clonality: Monoclonal (B94-1)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunoprecipitation (IP)

Catalog no.: ABIN967551

Additional Information

Alternative name: Caspase-7

Immunogen: Human Capase-7

Format: Liquid

Isotype: IgG1

Clone: B94-1

Description: Caspase-7 is a member of a family of cysteine proteases which play a critical role in the induction of apoptosis. Caspase-7 is structurally and functionally most similar to caspase-3. These proteases are expressed as proenzymes which are processed into large and small subunits that associate to form the active enzyme. Caspase-7 may also exist as alternative splice forms, i.e., Mch3alpha and Mch3beta. A novel interaction between Mch3alpha and the 17 kDa subunit of caspase-3 has been demonstrated in vitro, producing a heteromeric enzyme which is proteolytically active. Active caspase-7 can move to the mitochondrial fraction of cells undergoing Fas-mediated apoptosis, whereas active caspase-3 is primarily cytosolic. Caspase-7 is activated by caspase-31 and by granzyme B. Active caspase-7 can cleave the nuclear substrate PARP1 as well as the sterol regulatory element-binding protein 1 (SREBP-1). Caspase-7 migrates at a molecular weight of 35 kDa in SDS/PAGE. Clone B94-1 recognizes the 35 kDa and 17 kDa form human caspase-7. The specificity of the antibody was verified by immunoprecipitation and western blot analysis of active, recombinant human caspase-7 and of endogenous caspase-7 in cell lysates. A synthetic peptide corresponding to amino acids 25-42 of human caspase-7 was used as immunogen.
Synonyms: Mch3

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: 35 kDa (pro caspase-7), 17 kDa (active capase-7)

Comments:

Related Products: ABIN967389

Application Details

Application Notes: This antibody is routinely tested by western blot analysis (0.5-1.0 µg/ml). Other applications not routinely tested include immunoprecipitation (1-2 µg/1 x 10^6 cells). 293 embryonic kidney (ATCC CRL-1673) are recommended as a positive control. Jurkat T cell leukemia (ATCC TIB-152) and Daudi Burkitt lymphoma (ATCC CCL-213) cell lines may also be used for these applications.

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

Restrictions: For Research Use only

Images

Western blot analysis of caspase-7. Lysates from 293 embryonic kidney cells were probed with anti-human caspase-7 (clone B94-1). Caspase-7 was detected at ~35 kDa.

anti-Caspase 7, Apoptosis-Related Cysteine Peptidase (CASP7) (AA 25-42) antibody (Image 2)

Publications

Product: Fernandes-Alnemri, Takahashi, Armstrong et al.: "Mch3, a novel human apoptotic cysteine protease highly related to CPP32." in: Cancer research, Vol. 55, Issue 24, pp. 6045-52, 1996 (PubMed).

Lippke, Gu, Sarnecki et al.: "Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32." in: The Journal of biological chemistry, Vol. 271, Issue 4, pp. 1825-8, 1996 (PubMed).

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).

Chinnaiyan, Hanna, Orth et al.: "Cytotoxic T-cell-derived granzyme B activates the apoptotic protease ICE-LAP3." in: Current biology : CB, Vol. 6, Issue 7, pp. 897-9, 1997 (PubMed).

Cohen: "Caspases: the executioners of apoptosis." in: The Biochemical journal, Vol. 326 ( Pt 1), Issue 5693, pp. 1-16, 1997 (PubMed).

Chandler, Cohen, MacFarlane: "Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver." in: The Journal of biological chemistry, Vol. 273, Issue 18, pp. 10815-8, 1998 (PubMed).