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

Clonality: Monoclonal (22656)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

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

Catalog no.: ABIN967333

Additional Information

Alternative name: Caspase-7

Immunogen: Human caspase-7 full-length recombinant protein

Cross-Reactivity: Mouse (Murine)

Format: Liquid

Isotype: IgG1

Clone: 22656

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 prodomains can be used to catagorize the caspases into functional groups including, apoptotic initiators (long prodomains), apoptotic executioners' (short prodomains), and cytokine processors. Caspase-7, along with caspase-3 and -6 are members of the apoptotic executioners group containing short prodomains, caspase-7 is structurally and functionally most similar to caspase-3. Upon induction of apoptosis, pro-caspase-7 (35 kDa) is first converted to a 32 kDa intermediate, which is further processed into active subunits consisting of 20 kDa and 11 kDa forms (Swiss-Prot P55210). Active caspase-7 has been shown to cleave the nuclear substrate PARP as well as the sterol regulatory element-binding protein 1 (SREBP-1). In cells undergoing Fas-mediated apoptosis in vivo, active caspase-7 has been shown to translocate from the cytosol to the mitochondrial and microsomal fractions, whereas caspase-3 remains cytosolic. This data supports the hypothesis that similar apoptotic executioners cleave distinct substrates in different cellular compartments. The antibody recognizes human and mouse caspase-7. Full-length recombinant human caspase-7 protein was used as immunogen. The antibody is routinely tested by western blot and immunoprecipitation analysis of Jurkat T cells (please refer to Table I for what forms of caspase-7 are identified in a particular application).
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.

Comments:

Related Products: ABIN967389, ABIN968537

Application Details

Application Notes: The antibody is recommended for western blot analysis (0.62-0.25 µg/ml) and immunoprecipitation (4 µg/200 µg cell lysate).Jurkat T cells (ATCC TIB-152) are recommended as a positive control for these applications. antibodies-online offers several monoclonal caspase-7 antibodies. A Jurkat and HepG2 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

Restrictions: For Research Use only

Images

Western blot analysis of caspase-7. Lysates from control (lanes 1-3) and camptothecin-treated Jurkat cells (lanes 4-6) were probed with anti-human caspase-7 (clone 8-1-47, ABIN967331) at the following concentrations: 0.25 (lanes 1,4), 0.125 (lanes 2,5) and 0.062 µg/ml (lanes 3,6). Caspase-7 is identified as a band of 35 kDa (proform), and 32 kDa (intermediate), and 20 kDa (active) in treated cells and the 35 kDa band in control cells.

Immunoprecipitation/western blot analysis of caspase-7. Lysates from control (lane 1) or camptothecin-treated Jurkat cells (lane 2) were each immunoprecipitated with anti-human caspase-7 (clone 8-1-47) and western blotted with anti-human caspase-7 (clone 8-1-47). The 35 kDa full-length caspase-7 was identified in control cells. The 35 kDa (proform), 32 kDa (intermediate) and 20 kDa (active) forms were all identified in camptothecin treated cells.

Publications

Product: Duan, Orth, Chinnaiyan et al.: "ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B." in: The Journal of biological chemistry, Vol. 271, Issue 28, pp. 16720-4, 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).

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).

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).

Germain, Affar, DAmours et al.: "Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7." in: The Journal of biological chemistry, Vol. 274, Issue 40, pp. 28379-84, 1999 (PubMed).

Germain, Mathai, Shore: "BH-3-only BIK functions at the endoplasmic reticulum to stimulate cytochrome c release from mitochondria." in: The Journal of biological chemistry, Vol. 277, Issue 20, pp. 18053-60, 2002 (PubMed).