Recombinant Human Caspase-3 protein - BSA and Azide free (denatured) (Tag Free)
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Recombinant Human Caspase-3 protein - BSA and Azide free (denatured) (Tag Free) is a Human Full Length protein, in the 176 to 277 aa range, expressed in Escherichia coli, with >80%, suitable for SDS-PAGE.
View Alternative Names
CPP32, CASP3, Caspase-3, CASP-3, Apopain, Cysteine protease CPP32, Protein Yama, SREBP cleavage activity 1, CPP-32, SCA-1
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Caspase-3 protein - BSA and Azide free (denatured) (Tag Free) (AB180336)
3ug by SDS-PAGE under reducing conditions and visualized by coomassie blue stain.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
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.
Target data
Product promise
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