|Application ||WB, IHC|
|Calculated MW||31608 Da|
|Positive Control||WB: Jurkat cell lysates; IHC: human breast cancer tissues|
|Application & Usage||IHC: 1:1000 -1:2500 dilution; WB: 1:1000 - 1:2000 dilution|
|Alias Symbol||Caspase 3|
|Other Names||CPP32, CASP3, apopain, procaspase3, CPP32B, SCA-1, CPP-32, Apopain, Yama|
|Formulation||In 50% Glycerol/PBS with 1% BSA and 0.09% sodium azide|
|Reconstitution & Storage||-20 °C|
|Precautions||Anti-Caspase-3 Rabbit Monoclonal Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.|
|Tissue Location||Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system|
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Provided below are standard protocols that you may find useful for product applications.
Caspase family of cysteine proteases has been shown to play a key role in apoptosis. Caspase-3 is synthesized as an inactive pro-enzyme (32 kDa) that is processed in cells undergoing apoptosis by self-proteolysis and/or cleavage by another upstream protease. The processed form of caspase-3 consists of large (17 kD) and small (12 kD) subunits which associate to form an active enzyme. The active caspase-3 proteolytically cleaves and activates other caspases, as well as relevant targets in the cells (e.g., PARP and DFF).
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