Caspase 7, Apoptosis-Related Cysteine Peptidase (CASP7) (full length) antibody
|Synonyms||MCH3, CMH-1, ICE-LAP3, Mch3, mCASP-7, AI314680, ICE-IAP3, caspase-7, xCaspase-7, mch3, cmh-1, ice-lap3, CASP7, LOC100101591|
Alternatives Western Blotting (WB), Immunoprecipitation (IP)
|6 references available|
|Quantity||50 µg (0.5 mg/ml) (Variants)|
|Price||Product not available in this region.|
|Immunogen||Human caspase-7 full-length recombinant protein|
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).
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||20 kDa, 32 kDa, 35 kDa|
Related Products: ABIN967389, ABIN968537
|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.|
|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.|
|Restrictions||For Research Use only|
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).
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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).
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