Cleaved-Caspase 3 p17 Antibody (YA4628),MedChemexpress,HY-P84931

CASP3 is a thiol protease that functions as a major effector caspase in the execution phase of apoptosis. Activated by initiator caspases (such as CASP8, CASP9, or CASP10) through cleavage, it mediates apoptosis by catalyzing the cleavage of numerous proteins. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at the '216-Asp-|-Gly-217' bond. By similarity, it cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Additionally, CASP3 cleaves and activates caspase-6 (CASP6), caspase-7 (CASP7), and caspase-9 (CASP9), while also cleaving and inactivating interleukin-18 (IL18). It is involved in the cleavage of huntingtin and triggers cell adhesion in sympathetic neurons through RET cleavage. Under oxidative stress, CASP3 cleaves and inhibits serine/threonine-protein kinase AKT1. During virus-induced apoptosis, it acts as an inhibitor of type I interferon production by cleaving antiviral proteins CGAS, IRF3, and MAVS, preventing cytokine overproduction. CASP3 also participates in pyroptosis by cleaving and activating gasdermin-E (GSDME). Furthermore, it cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8, and XKR9, promoting phosphatidylserine exposure on apoptotic cell surfaces. Finally, following inhibition of BIRC6-caspase binding by DIABLO/SMAC, CASP3 cleaves BIRC6.

CASP3; CPP32; Caspase-3; CASP-3; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1