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Flow cytometric analysis of apoptotic and non-apoptotic populations for active caspase-3. Jurkat cells (Human T-cell leukemia; ATCC TIB-152) were left untreated (left panel) or treated with 4 µM of camptothecin for 4 hr to induce apoptosis (right panel). Cells were washed once in PBS, then fixed and permeabilized using the BD Cytofix/Cytoperm™ Kit (Cat. No. 554714) for 20 min at room temperature (RT), pelleted and washed with BD Perm/Wash™ buffer (component of Cat. No. 554714). Cells were subsequently stained with the FITC rabbit anti- active caspase-3 antibody (clone C92-605). Cells were then washed and resuspended in BD Perm/Wash™ buffer before analyzing by flow cytometry. The results show that untreated cells were primarily negative for active caspase-3 (left panel, M1); whereas over one third of the treated cells were positive for active caspase-3 staining (right panel, M2).
BD Pharmingen™ FITC Rabbit Anti- Active Caspase-3
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Preparation And Storage
Product Notices
- This reagent has been pre-diluted for use at the recommended Volume per Test. We typically use 1 × 10^6 cells in a 100-µl experimental sample (a test).
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- For fluorochrome spectra and suitable instrument settings, please refer to our Multicolor Flow Cytometry web page at www.bdbiosciences.com/colors.
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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.
Development References (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). View Reference
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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). View Reference
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Thornberry NA, Lazebnik Y. Caspases: enemies within. Science. 1998; 281(5381):1312-1316. (Biology). View Reference
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