Caspase3, His-Tag Recombinant
Recombinant human Caspase3 (CASP3), full length, encompassing amino acids 1-277(end). This construct contains a C-terminal His-tag (6xHis). Procaspase-3 is self-cleaved into two subunits, MW=17 kDa and 13 kDa, to form the active heterotetrameric complex. The recombinant protein was affinity purified.
This product has been cited 2 times.
≥90%
40 mM Tris-HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 0.04% Tween-20, 20% glycerol, and 3 mM DTT
≥6784 pmol/min/µg
Caspase3, also known as cysteine-aspartic acids protease 3, belongs to the C14A peptidase family of proteins and is the primary caspase responsible for apoptosis-associated proteolysis. It cleaves several substrates, such as beta-catenin, PARP (poly ADP ribose polymerase) and other caspases when in the procaspase form (6, 7 and 9). Cells synthetize procaspase3, which forms an inactive homodimer that resides in the cytosol. Activation signals lead to procaspase3 proteolytic cleavage and generation two subunits able to heterodimerize, and then bind to another heterodimer and form an active antiparallel homodimer. Dysregulation of caspase-mediated apoptosis can result in inflammatory diseases, neurological and metabolic disorders and cancer. The development of therapeutical approaches targeting caspase3 may be beneficial to patients suffering from a range of diseases.
2. Suzuki, Y., et al., Proc Natl Acad Sci USA. 2001 Jul 17;98(15):866-7.
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