Cleaved+pro Caspase-3 Recombinant Rabbit Monoclonal Antibody - BSA and Azide free [SU38-04] (HA750159)

UNIPROT #

P42574

PROTEIN NAME

Cleaved+pro Caspase-3

SYNONYMS

Caspase3;A830040C14Rik antibody;Apopain antibody;CASP 3 antibody;CASP-3 antibody;CASP3 antibody;CASP3_HUMAN antibody;Casp3a antibody;Caspase 3 antibody;Caspase 3, apoptosis-related cysteine peptidase antibody;Caspase 3, apoptosis-related cysteine protease antibody;Caspase 3, apoptosis-related cysteine protease a antibody;Caspase-3 subunit p12 antibody;Caspase3 antibody;CC3 antibody;CPP 32 antibody;CPP-32 antibody;CPP32 antibody;CPP32B antibody;Cysteine protease CPP32 antibody;EC 3.4.22.56 antibody;ICE3 antibody;LICE antibody;mldy antibody;OTTHUMP00000165052 antibody;OTTHUMP00000165053 antibody;OTTHUMP00000165054 antibody;PARP cleavage protease antibody;Procaspase3 antibody;Protein Yama antibody;SCA 1 antibody;SCA-1 antibody;SCA1 antibody;SREBP cleavage activity 1 antibody;Yama antibody;Yama protein antibody

SEQUENCE SIMILARITIES

Belongs to the peptidase C14A family.

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.

POST-TRANSLATIONAL MODIFICATION

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.; 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.

SUBCELLULAR LOCATION

Cytoplasm.

FUNCTION

Caspase-3 is a caspase protein that interacts with caspase-8 and caspase-9. It is encoded by the CASP3 gene. CASP3 orthologs have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts. Caspase-3 shares many of the typical characteristics common to all currently-known caspases. For example, its active site contains a cysteine residue (Cys-163) and histidine residue (His-121) that stabilize the peptide bond cleavage of a protein sequence to the carboxy-terminal side of an aspartic acid when it is part of a particular 4-amino acid sequence. This specificity allows caspases to be incredibly selective, with a 20,000-fold preference for aspartic acid over glutamic acid. A key feature of caspases in the cell is that they are present as zymogens, termed procaspases, which are inactive until a biochemical change causes their activation. Each procaspase has an N-terminal large subunit of about 20 kDa followed by a smaller subunit of about 10 kDa, called p20 and p10, respectively.