Mouse Anti-CASP3 Recombinant Antibody (3F49) (CBMAB-C1122-LY)

Caspase 3

The protein encoded by this gene is a cysteine-aspartic acid protease that plays a central role in the execution-phase of cell apoptosis. The encoded protein cleaves and inactivates poly(ADP-ribose) polymerase while it cleaves and activates sterol regulatory element binding proteins as well as caspases 6, 7, and 9. This 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. [provided by RefSeq, Aug 2017]

Caspase 3; Caspase 3, Apoptosis-Related Cysteine Peptidase; Caspase 3, Apoptosis-Related Cysteine Protease; SREBP Cleavage Activity 1; Cysteine Protease CPP32; Protein Yama; EC 3.4.22.56; Apopain; CASP-3;

Involved in the activation cascade of caspases responsible for apoptosis execution (PubMed:7596430).
At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond (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. Cleaves and activates caspase-6, -7 and -9 (PubMed:7596430).
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).

Anterior neural tube closure Source: Ensembl
Apoptotic DNA fragmentation Source: Reactome
Apoptotic process Source: UniProtKB
Apoptotic signaling pathway Source: BHF-UCL
Axonal fasciculation Source: Ensembl
B cell homeostasis Source: Ensembl
Cell fate commitment Source: Ensembl
Cellular response to DNA damage stimulus Source: Ensembl
Cellular response to staurosporine Source: CAFA
Cytokine-mediated signaling pathway Source: Reactome
Erythrocyte differentiation Source: UniProtKB
Execution phase of apoptosis Source: UniProtKB
Extrinsic apoptotic signaling pathway in absence of ligand Source: Reactome
Glial cell apoptotic process Source: Ensembl
Heart development Source: Ensembl
Hippocampus development Source: Ensembl
Hippo signaling Source: Reactome
Intrinsic apoptotic signaling pathway in response to osmotic stress Source: Ensembl
Keratinocyte differentiation Source: GO_Central
Learning or memory Source: Ensembl
Leukocyte apoptotic process Source: Ensembl
Luteolysis Source: Ensembl
Negative regulation of activated T cell proliferation Source: Ensembl
Negative regulation of apoptotic process Source: MGI
Negative regulation of B cell proliferation Source: Ensembl
Neuron apoptotic process Source: Ensembl
Neuron differentiation Source: GO_Central
Neurotrophin TRK receptor signaling pathway Source: MGI
Platelet formation Source: UniProtKB
Positive regulation of amyloid-beta formation Source: UniProtKB
Positive regulation of apoptotic process Source: GO_Central
Positive regulation of neuron apoptotic process Source: Ensembl
Protein processing Source: Ensembl
Proteolysis Source: UniProtKB
Regulation of macroautophagy Source: ParkinsonsUK-UCL
Regulation of protein stability Source: UniProtKB
Response to amino acid Source: Ensembl
Response to antibiotic Source: Ensembl
Response to cobalt ion Source: Ensembl
Response to drug Source: Ensembl
Response to estradiol Source: Ensembl
Response to glucocorticoid Source: Ensembl
Response to glucose Source: Ensembl
Response to hydrogen peroxide Source: Ensembl
Response to hypoxia Source: Ensembl
Response to lipopolysaccharide Source: Ensembl
Response to nicotine Source: Ensembl
Response to tumor necrosis factor Source: BHF-UCL
Response to UV Source: Ensembl
Response to X-ray Source: Ensembl
Sensory perception of sound Source: Ensembl
Striated muscle cell differentiation Source: Ensembl
T cell homeostasis Source: Ensembl
Wound healing Source: Ensembl

Cytoplasm

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.