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Immunoprecipitation/Western blot analysis of caspase-3 from apoptotic and non-apoptotic cell lysates. Jurkat cells (Human T-cell leukemia; ATCC TIB-152) were left untreated (left panel) or were treated with 6 µM camptothecin for 5 hr to induce apoptosis (right panel). Immunoprecipitation: Cell lysates were immunoprecipitated with 0.25 - 2 µg/ml of the rabbit anti- active caspase-3 antibody [clone C92-605, lanes 1 and 8 (2 µg), lanes 2 and 9, (1 µg), lanes 3 and 10 (0.5 µg), and lanes 4 and 11 (0.25 µg)], 1 - 2 µg/ml of a mAb recognizing both pro and active caspase-3 (Cat. No. 610322), lanes 5 and 12 (2 µg), lanes 6 and 13 (1 µg)] or 1 µg/ml of a rabbit IgG isotype control [Jackson Immunoresearch (Cat. No. 011-00000-3), lanes 7 and 14]. Western blot: Caspase-3 was detected by western blot analysis with an antibody that recognizes both pro- (32 kD) and active (20 and 17 kD, reflecting the presence or absence of the caspase-3 pro-domain) caspase-3 [lanes 1-14]. The results also show that the rabbit anti- active caspase-3 antibody (clone C92-605) immunoprecipitated only the active form of caspase-3 (lanes 8-11) as compared to the mouse anti-human caspase-3 antibody (Cat. No. 610322) which immunoprecipitated both the pro and active forms of caspase-3 (lanes 12 and 13). Bands may be observable at ~25 kD and ~55-60 kD which represent the light and heavy chains, respectively, of IgG used for the immunoprecipitation.
BD Pharmingen™ Purified Rabbit Anti- Active Caspase-3
BD Pharmingen™ Purified Rabbit Anti- Active Caspase-3
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The caspase family of cysteine proteases plays a key role in apoptosis and inflammation. Caspase-3 is a key protease that is activated during the early stages of apoptosis and, like other members of the caspase family, is synthesized as an inactive pro-enzyme that is processed in cells undergoing apoptosis by self-proteolysis and/or cleavage by another protease. The processed forms of caspases consist of large (17-22 kDa) and small (10-12 kDa) subunits which associate to form an active enzyme. Active caspase-3, a marker for cells undergoing apoptosis, consists of a heterodimer of 17 and 12 kDa subunits which is derived from the 32 kDa pro-enzyme. Active caspase-3 proteolytically cleaves and activates other caspases, as well as relevant targets in the cytoplasm, e.g., D4-GDI and Bcl-2, and in the nucleus (e.g. PARP). This antibody has been reported to specifically recognize the active form of caspase-3 in human and mouse cells. It has not been reported to recognize the pro-enzyme form of caspase-3.
研发参考 (3)
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Dai C, Krantz SB. Interferon gamma induces upregulation and activation of caspases 1, 3, and 8 to produce apoptosis in human erythroid progenitor cells. Blood. 1999; 93(10):3309-3316. (Biology). 查看参考
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Fujita N, Tsuruo T. Involvement of Bcl-2 cleavage in the acceleration of VP-16-induced U937 cell apoptosis. Biochem Biophys Res Commun. 1998; 246(2):484-488. (Biology). 查看参考
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Thornberry NA, Lazebnik Y. Caspases: enemies within. Science. 1998; 281(5381):1312-1316. (Biology). 查看参考
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