Caspase-3/CASP3 Protein, Human (His, Strep)

Caspase-3/CASP3 protein is a thiol protease critical in apoptosis and is activated by initiating caspases (CASP8, CASP9 and/or CASP10). It catalyzes the cleavage of multiple proteins in sympathetic neurons, including PARP1, SREBP, caspase-6, -7 and -9, huntingtin, and RET. Caspase-3/CASP3 Protein, Human (His, Strep) is the recombinant human-derived Caspase-3/CASP3 protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of Caspase-3/CASP3 Protein, Human (His, Strep) is 277 a.a., .

Caspase-3/CASP3 Protein functions as a pivotal thiol protease in the execution phase of apoptosis, serving as a major effector caspase. Upon cleavage and activation by initiator caspases (CASP8, CASP9, and/or CASP10), it orchestrates apoptosis by catalyzing the cleavage of numerous proteins. In the early stages of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1, targeting the '216-Asp-|-Gly-217' bond. CASP3 also activates sterol regulatory element-binding proteins (SREBPs), cleaves and activates caspase-6, -7, and -9, participates in the cleavage of huntingtin, and induces cell adhesion in sympathetic neurons through RET cleavage. Additionally, CASP3 cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. It acts as an inhibitor of type I interferon production during virus-induced apoptosis by cleaving antiviral proteins CGAS, IRF3, and MAVS, thus preventing cytokine overproduction. CASP3 is also involved in pyroptosis, mediating the cleavage and activation of gasdermin-E (GSDME). Furthermore, it cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8, and XKR9, promoting phosphatidylserine exposure on the apoptotic cell surface.

Human

E. coli

N-Strep;N-6*His

P42574 (M1-H277)

836

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.