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Description
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.
Specifications
Specifications
| Antigen | Caspase-3 |
| Applications | Flow Cytometry |
| Classification | Monoclonal |
| Clone | C92-605 |
| Conjugate | Alexa Fluor 647 |
| Description | CPP32; Yama; Apopain |
| Formulation | Aqueous buffered solution containing BSA and ≤0.09% sodium azide. |
| Host Species | Rabbit |
| Immunogen | Human Active Caspase-3 Fragment |
| Purification Method | Affinity Purified |
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