Recombinant Protein of Active Caspase-3

The antibody detects endogenous cleaved Caspase-3 protein p17 isoform.

CASP3

Caspase3

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

This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits , large and small , that dimerize to form the active enzyme. This protein cleaves and activates caspases 6 , 7 and 9 , and the protein itself is processed by caspases 8 , 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein , which is associated with neuronal death in Alzheimer's disease. Alternative splicing of this gene results in two transcript variants that encode the same protein. [provided by RefSeq , Jul 2008] ,

Catalytic activity:Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3 , although Val or Ala are also accepted at this position. ,enzyme regulation:Inhibited by isatin sulfonamides. ,Function:Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly (ADP-ribose) polymerase (PARP) at a '216-Asp-|-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. ,PTM:Cleavage 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. ,PTM: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. ,similarity:Belongs to the peptidase C14A family. ,subunit:Heterotetramer that consists of two anti-parallel arranged heterodimers , each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit. ,tissue specificity:Highly expressed in lung , spleen , heart , liver and kidney. Moderate levels in brain and skeletal muscle , and low in testis. Also found in many cell lines , highest expression in cells of the immune system. ,

Cytoplasm.

>>Platinum drug resistance ;
>>MAPK signaling pathway ;
>>p53 signaling pathway ;
>>Apoptosis ;
>>Apoptosis - multiple species ;
>>Natural killer cell mediated cytotoxicity ;
>>IL-17 signaling pathway ;
>>TNF signaling pathway ;
>>Serotonergic synapse ;
>>Non-alcoholic fatty liver disease ;
>>AGE-RAGE signaling pathway in diabetic complications ;
>>Alcoholic liver disease ;
>>Alzheimer disease ;
>>Parkinson disease ;
>>Amyotrophic lateral sclerosis ;
>>Huntington disease ;
>>Prion disease ;
>>Pathways of neurodegeneration - multiple diseases ;
>>Epithelial cell signaling in Helicobacter pylori infection ;
>>Pathogenic Escherichia coli infection ;
>>Salmonella infection ;
>>Pertussis ;
>>Legionellosis ;
>>Toxoplasmosis ;
>>Amoebiasis ;
>>Tuberculosis ;
>>Hepatitis C ;
>>Hepatitis B ;
>>Measles ;
>>Human cytomegalovirus infection ;
>>Influenza A ;
>>Human papillomavirus infection ;
>>Kaposi sarcoma-associated herpesvirus infection ;
>>Herpes simplex virus 1 infection ;
>>Epstein-Barr virus infection ;
>>Human immunodeficiency virus 1 infection ;
>>Pathways in cancer ;
>>Viral carcinogenesis ;
>>Proteoglycans in cancer ;
>>MicroRNAs in cancer ;
>>Colorectal cancer ;
>>Small cell lung cancer ;
>>Viral myocarditis ;
>>Lipid and atherosclerosis