|Other Names||BH3-interacting domain death agonist, p22 BID, BID, BH3-interacting domain death agonist p15, p15 BID, BH3-interacting domain death agonist p13, p13 BID, BH3-interacting domain death agonist p11, p11 BID, BID|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1307a was selected from the region of human Bid BH3 Domain. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2.|
|Cellular Location||Cytoplasm. Mitochondrion membrane. Note=When uncleaved, it is predominantly cytoplasmic. BH3-interacting domain death agonist p13: Mitochondrion membrane. Note=Associated with the mitochondrial membrane. Isoform 3: Cytoplasm.|
|Tissue Location||Isoform 2 and isoform 3 are expressed in spleen, bone marrow, cerebral and cerebellar cortex. Isoform 2 is expressed in spleen, pancreas and placenta (at protein level) Isoform 3 is expressed in lung, pancreas and spleen (at protein level). Isoform 4 is expressed in lung and pancreas (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
Bid is a death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. Bid 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.
Wang, X., et al., J. Biol. Chem. 278(31):29184-29191 (2003).Cartron, P.F., et al., Mol. Cell. Biol. 23(13):4701-4712 (2003).Fischer, B., et al., Biochem. Biophys. Res. Commun. 306(2):516-522 (2003).Degli Esposti, M., et al., J. Biol. Chem. 278(18):15749-15757 (2003).Kuwana, T., et al., Cell 111(3):331-342 (2002).
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