BH3 Interacting Domain Death Agonist Recombinant Protein | BID recombinant protein
Recombinant Human BH3 Interacting Domain Death Agonist
Sterile Filtered colorless solution.
Introduction: BID accession number NP_001187 is a pro-apoptotic Bcl-2 protein having only the BH3 domain. In reaction to apoptotic signaling, BID interacts with another Bcl-2 family of cell death regulators, called Bax, they form a heterodimer resulting to the insertion of Bax into the outer mitochondrial membrane. Bax induces the opening of the mitochondrial voltage-dependent anion channel which lead to the release of cytochrome c and other pro-apoptotic factors from the mitochondria resulting in activation of caspases. BID is a mediator of mitochondrial damage induced by caspase-8 (CASP8). CASP8 cleaves BID, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. The major proteolytic product p15 BID releasea cytochrome c. Isoform 1, Isoform 2 and Isoform 4 induce ice-like proteases and apoptosis while Isoform 3 does not induce apoptosis.
NCBI and Uniprot Product Information
NCBI Description
This gene encodes a death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. The encoded protein is a member of the BCL-2 family of cell death regulators. It is a mediator of mitochondrial damage induced by caspase-8 (CASP8); CASP8 cleaves this encoded protein, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. Multiple alternatively spliced transcript variants have been found, but the full-length nature of some variants has not been defined. [provided by RefSeq, Jul 2008]
Uniprot Description
BID: a pro-apoptotic member of the Bcl-2 superfamily. Targets intracellular membranes and contains a BH3 death domain. Heterodimerizes with either the pro-apoptotic protein BAX or the anti-apoptotic protein BCL2, antagonizing its protective effect. The activity of BID is regulated by Caspase 8-mediated cleavage, exposing the BH3 domain and significantly changing the surface charge and hydrophobicity, causing translocation to mitochondria where it triggers cytochrome c release. Multiple alternatively spliced variants have been found.
Protein type: Mitochondrial; Apoptosis
Chromosomal Location of Human Ortholog: 22q11.1
Cellular Component: mitochondrial outer membrane; membrane; mitochondrion; cytosol
Molecular Function: protein binding; ubiquitin protein ligase binding; death receptor binding
Biological Process: caspase activation; release of cytochrome c from mitochondria; positive regulation of apoptosis; positive regulation of protein homooligomerization; apoptosis; DNA damage response, signal transduction; response to estradiol stimulus; regulation of cell proliferation; positive regulation of protein oligomerization; apoptotic mitochondrial changes; neuron apoptosis; induction of apoptosis via death domain receptors; brain development; protein targeting to mitochondrion; protein homooligomerization