Caspase 3 protein (Active) (ab52071)
Constituents: 5% Glycerol, 50mM Sodium chloride, 50mM HEPES, 0.1% Chaps, 10mM DTT, 10mM EDTA, pH 7.2
One unit of the recombinant caspase-3 is the enzyme activity that cleaves 1 nmol of the caspase substrate DEVD-pNA (pNA: pnitroanaline) per hour at 37degC.
Not yet tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.
- A830040C14RikApopainCASP 3
- CASP-3CASP3CASP3_HUMANCasp3aCaspase 3Caspase 3, apoptosis-related cysteine peptidaseCaspase 3, apoptosis-related cysteine proteaseCaspase 3, apoptosis-related cysteine protease aCaspase-3 subunit p12CC3CPP 32CPP-32CPP32CPP32BCysteine protease CPP32EC 126.96.36.199LICEMGC100890MGC93645mldyOTTHUMP00000165052OTTHUMP00000165053OTTHUMP00000165054OTTHUMP00000165055OTTHUMP00000224230OTTHUMP00000224231PARP cleavage proteaseProcaspase3Protein YamaSCA 1SCA-1SCA1SREBP cleavage activity 1YamaYama proteinzgc:100890
-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin.
modificationsCleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa.
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.
References for Caspase 3 protein (Active) (ab52071)
ab52071 has not yet been referenced specifically in any publications.