Recombinant human Cleaved Caspase-3 protein (Active)

Specifications

Form

Lyophilized

General info

Function

Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis (PubMed : 18723680, PubMed : 20566630, PubMed : 23650375, PubMed : 35338844, PubMed : 35446120, PubMed : 7596430). Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins (PubMed : 18723680, PubMed : 20566630, PubMed : 23650375, PubMed : 7596430). At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond (PubMed : 10497198, PubMed : 16374543, PubMed : 7596430, PubMed : 7774019). Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain (By similarity). Cleaves and activates caspase-6, -7 and -9 (CASP6, CASP7 and CASP9, respectively) (PubMed : 7596430). Cleaves and inactivates interleukin-18 (IL18) (PubMed : 37993714, PubMed : 9334240). Involved in the cleavage of huntingtin (PubMed : 8696339). Triggers cell adhesion in sympathetic neurons through RET cleavage (PubMed : 21357690). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress (PubMed : 23152800). Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (PubMed : 30878284). Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (PubMed : 35338844, PubMed : 35446120). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (PubMed : 23845944, PubMed : 33725486). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (PubMed : 36758104, PubMed : 36758106).

Sequence similarities

Belongs to the peptidase C14A family.

Post-translational modifications

Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits (PubMed:35338844, PubMed:35446120, PubMed:7596430, PubMed:8755496). Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease (PubMed:7596430, PubMed:8755496). Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa (PubMed:7596430, PubMed:8755496).. S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol.. Ubiquitinated by BIRC6; this activity is inhibited by DIABLO/SMAC.. (Microbial infection) ADP-riboxanation by C.violaceum CopC blocks CASP3 processing, preventing CASP3 activation and ability to recognize and cleave substrates.