Caspase-3/CASP3 Protein, Mouse (His, Myc)

Caspase-3/CASP3 Protein, Mouse (His, Myc) is the recombinant mouse-derived Caspase-3/CASP3 protein, expressed by E. coli, with N-10*His & C-Myc tag.

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.

Mouse

E. coli

N-10*His;C-Myc

P70677 (S29-H277)

12367

Full Length of Mature Protein

SGIYLDSSYKMDYPEMGICIIINNKNFHKSTGMSSRSGTDVDAANLRETFMGLKYQVRNKNDLTREDILELMDSVSKEDHSKRSSFVCVILSHGDEGVIYGTNGPVELKKLTSFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGTDEEMACQKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCSMLKLYAHKLEFMHILTRVNRKVATEFESFSLDSTFHAKKQIPCIVSMLTKELYFYH

<1 EU/μg, determined by LAL method.