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

Details for Product No. ABIN967332
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Antigen
Synonyms xCaspase-7, caspase-7, caspase7, cmh-1, ice-lap3, mch3, CASP7, AI314680, CMH-1, ICE-IAP3, Mch3, mCASP-7, CASP-7, ICE-LAP3, LICE2, MCH3, Caspase-7, MCH3/SCA-2, SCA-2
Epitope
full length
(21), (13), (13), (8), (8), (4), (4), (3), (3), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human
(186), (84), (55), (15), (12), (5), (5), (3), (2), (2), (1), (1)
Host
Mouse
(152), (40), (2)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(7), (4), (4), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB), Immunoprecipitation (IP)
(176), (89), (65), (43), (25), (12), (10), (10), (9), (8), (3), (2), (2)
Pubmed 6 references available
Quantity 50 μg
Options
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Catalog No. ABIN967332
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Immunogen Human caspase-7 full-length recombinant protein
Clone 753123
Isotype IgG1
Cross-Reactivity Mouse (Murine)
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.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name Caspase-7
Background 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 caspase-7. Full-length recombinant human caspase-7 protein was used as immunogen. The antibodies are routinely tested by western blot and immunoprecipitation analysis using Jurkat T cells (please refer to Table I for what forms of caspase-7 are identified in a particular application).
Synonyms: Mch3
Molecular Weight 20 kDa, 32 kDa, 35 kDa
Research Area Apoptosis/Necrosis
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.
Comment

Related Products: ABIN967389, ABIN968537

Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/ml
Buffer Aqueous buffered solution.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C
Supplier Images
anti-Caspase 7, Apoptosis-Related Cysteine Peptidase (CASP7) (full length) antibody 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.
anti-Caspase 7, Apoptosis-Related Cysteine Peptidase (CASP7) (full length) antibody (2) 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.
Product cited in: 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).

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