|Application ||WB, IP|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||34277 Da|
|Application & Usage||Western blot analysis (0.5-2 µg/ml) and immunoprecipitation (4-10 µg/ml). However the optimal conditions should be determined individually. Detects both pro-caspase-7 (34 kDa) and the large subunit of cleaved caspase-7 (19 kDa) in apoptosis cells on SDS-PAGE immunoblots.|
|Other Names||CASP7, CASP-7, ICE-LAP3, CMH-1, MCH3, EC 188.8.131.52|
|Formulation||100 µg (0.5 µg/ml) in PBS containing 1 mg/ml BSA and 1.5 mM thimerosal and 50% glycerol|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||Caspase-7 Antibody (Clone B4-G2) 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. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly- 217' bond. Overexpression promotes programmed cell death.|
|Tissue Location||Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. No expression in the brain|
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Provided below are standard protocols that you may find useful for product applications.
The caspase family of cysteine proteases plays a key role in apoptosis. Caspase-7, also known as Mch3α, ICE/LAP3 and CMH1, is a 34 kDa protein that is activated during Fas- and TNF-induced apoptosis. Caspase-7 has been identified as a major contributor to the execution phase of cellular apoptosis. It cleaves essential cellular machinery following its own cleavage from an inactive proenzyme to an active heterodimeric form. Caspase-7 is processed by caspase-3, -6, -8, -9, and –10 as well as by Granzyme B.
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