BID Research Reagents

BH3-interacting domain death agonist is a protein in humans that is encoded by BID gene. 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.

The following BID reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

BID Antibodies

BID Antibodies for Homo sapiens (Human)

BID Proteins

BID Proteins for Mus musculus (Mouse)

BID Proteins for Homo sapiens (Human)

BID Proteins for Sus scrofa (Pig)

BID Proteins for Gallus gallus (Chicken)

BID Proteins for Rattus norvegicus (Rat)

BID Background

The BID gene encodes the BH3-interacting domain death agonist (BID), a pro-apoptotic member of the Bcl-2 protein family [1]. BID possesses a single BH3 (Bcl-2 homology 3) domain and lacks a C-terminal transmembrane domain for the outer mitochondrial membrane[1]. BID is localized in the cytosolic or on the plasma membrane. BID is inactive, but becomes activated after Caspase-8 cleavage [2][3][4]. Truncated BID (tBID) may expose the BH3 motif buried in the uncleaved molecule. Protease-cleaved BID subsequently translocates to mitochondria where it induces permeabilization of the mitochondrial outer membrane (MOM) dependent on the pro-apoptotic proteins Bax and/or Bak. BID, therefore, acts as a sentinel for protease-mediated death signals [7]. Mutagenesis study indicated that the BH3 domain is required for the apoptotic activity of BID since BID with an intact BH3 domain may retain interaction with BAX [4][5]. Cells generate pro-apoptotic proteins with a single active domain called BH3 in stress or damage. BID acts as an activator to induce the overexpression of effector pro-apoptotic proteins such as BAX (BCL2-associated X) and BAK (BCL2 antagonist/killer 1) [6]. The production of BAX and BAK further leads to cytochrome c release into the cytoplasm, following caspase activation and apoptosis [6].

[1] Wang K, Yin XM, et al. BID: a novel BH3 domain-only death agonist [J]. Genes Dev. 1996, 10 (22): 2859-9.
[2] Gross A., Yin X.-M., et al. Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not TNF-R1/Fas death [J]. J. Biol. Chem. 1999; 274: 1156-1163.
[3] Li H., Zhu H., et al. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis [J]. Cell. 1998; 94: 491-501.
[4] Luo X., Budihardjo I. et al. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors [J]. Cell. 1998; 94: 481-490.
[5] Wang K., Gross A., et al. Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing [J]. Mol. Cell. Biol. 1998; 18: 6083-6089.
[6] Korsmeyer SJ, Wei MC, et al. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c [J]. Cell Death Differ 2001; 7: 1166-173.

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