BD Transduction Laboratories™ Purified Mouse Anti-Human Caspase-3
Clone 19/Caspase-3/CPP32 (RUO)
Western blot analysis of Caspase-3 on a Jurkat cell lysate (Human T-cell leukemia; ATCC TIB-152) . Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-human Caspase-3 antibody.
Western blot analysis of Caspase-3 on a Jurkat cell lysate (Human T-cell leukemia; ATCC TIB-152) . Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-human Caspase-3 antibody.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- 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.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
Companion Products
Apoptosis, a selective process of genetically programmed cell death, occurs during normal cellular differentiation and development of multicellular organisms. Apoptotic cells are characterized by loss of cell volume, plasma membrane blebbing, nuclear condensation, chromatin aggregation, and endonucleocytic degradation of DNA into nucleosomal fragments. Caspase-3 (CPP32, Yama, apopain) is a member of the family of cysteine proteases which includes interleukin-1β converting enzyme (ICE) and C. elegans protein, Ced-3. An apoptotic signal such as granzyme B of cytotoxic T-cells (CTLs) or ICE-like proteases induces the intracellular cleavage of Caspase-3 from the inactive pro-form (32 kDa) to the active form which consists of the p20, p17, and p12 subunits. The active form of Caspase-3 cleaves several other apoptotic proteins including proteins such as DNA Fragmentation Factor (DFF). Apoptosis can be inhibited by coexpression of Bcl-2 as well as inhibitors of Caspase-3 or other members of the family of cysteine proteases. This antibody recognizes the human pro-form (inactive) of Caspase-3 at 32 kDa. In addition, it has been reported to recognize the active form of Caspase-3 at 20-21 kD in apoptotic cell lysates.
Development References (5)
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Donoghue S, Baden HS, Lauder I, Sobolewski S, Pringle JH. Immunohistochemical localization of caspase-3 correlates with clinical outcome in B-cell diffuse large-cell lymphoma. Cancer Res. 1999; 59(20):5386-5391. (Biology: Immunohistochemistry). View Reference
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Fernandes-Alnemri T, Litwack G, Alnemri ES. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. J Biol Chem. 1994; 269(49):30761-30764. (Biology). View Reference
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Li J, Chen P, Sinogeeva N, et al. Arsenic trioxide promotes histone H3 phosphoacetylation at the chromatin of CASPASE-10 in acute promyelocytic leukemia cells. J Biol Chem. 2002; 277(51):49504-49510. (Biology: Flow cytometry). View Reference
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Scaffidi C, Fulda S, Srinivasan A, et al. Two CD95 (APO-1/Fas) signaling pathways.. EMBO J. 1998; 17(6):1675-1687. (Biology: Apoptosis).
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Takemoto K, Nagai T, Miyawaki A, Miura M. Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects. J Cell Biol. 2003; 160(2):235-243. (Biology: Depletion). View Reference
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