Preparation And Storage
Recommended Assay Procedures
This antibody is routinely tested by western blot analysis (0.5-1.0 µg/ml). Other applications not routinely tested at BD Biosciences Pharmingen 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.
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
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., Mch3α and Mch3β. A novel interaction between Mch3α 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.
Development References (6)
-
Chandler JM, Cohen GM, MacFarlane M. Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver. J Biol Chem. 1998; 273(18):10815-10818. (Clone-specific: Apoptosis). View Reference
-
Chinnaiyan AM, Hanna WL, Orth K. Cytotoxic T-cell-derived granzyme B activates the apoptotic protease ICE-LAP3. Curr Biol. 1996; 6(7):897-899. (Clone-specific: Immunoprecipitation). View Reference
-
Cohen GM. Caspases: the executioners of apoptosis. Biochem J. 1997; 326(1):1-16. (Biology). View Reference
-
Duan H, Chinnaiyan AM, Hudson PL, Wing JP, He WW, Dixit VM. 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. J Biol Chem. 1996; 271(3):1621-1625. (Biology). View Reference
-
Fernandes-Alnemri T, Takahashi A. Mch3, a novel human apoptotic cysteine protease highly related to CPP32. Cancer Res. 1995; 55(24):6045-6052. (Clone-specific: Activation). View Reference
-
Lippke JA, Gu Y, Sarnecki C, Caron PR, Su MS. Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32. J Biol Chem. 1996; 271(4):1825-1828. (Biology). View Reference
Please refer to Support Documents for Quality Certificates
Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
