BID antibody (AA 50-62)

Catalog No. ABIN968577

Product Details anti-BID Antibody

Target: BID (BH3 Interacting Domain Death Agonist (BID))

Binding Specificity: AA 50-62

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This BID antibody is un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF)

Cross-Reactivity: Human

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.

Purification: The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.

Immunogen: Mouse Bid aa. 50-62

Clone: 7-Bid

Isotype: IgG1

Application Details

Comment:

Related Products: ABIN968537, ABIN967389

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 250 μg/mL

Buffer: Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.

Preservative: Sodium azide

Precaution of Use: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Storage: -20 °C

Storage Comment: Store undiluted at -20° C.

References for anti-BID antibody (ABIN968577)

Devarajan, De Leon, Talasazan, Schoenfeld, Davidowitz, Burk: "The von Hippel-Lindau gene product inhibits renal cell apoptosis via Bcl-2-dependent pathways." in: The Journal of biological chemistry, Vol. 276, Issue 44, pp. 40599-605, (2001) (PubMed).

Gómez-Angelats, Cidlowski: "Protein kinase C regulates FADD recruitment and death-inducing signaling complex formation in Fas/CD95-induced apoptosis." in: The Journal of biological chemistry, Vol. 276, Issue 48, pp. 44944-52, (2001) (PubMed).

Zhuang, Demirs, Kochevar: "p38 mitogen-activated protein kinase mediates bid cleavage, mitochondrial dysfunction, and caspase-3 activation during apoptosis induced by singlet oxygen but not by hydrogen peroxide." in: The Journal of biological chemistry, Vol. 275, Issue 34, pp. 25939-48, (2000) (PubMed).

Kudla, Montessuit, Eskes, Berrier, Martinou, Ghazi, Antonsson: "The destabilization of lipid membranes induced by the C-terminal fragment of caspase 8-cleaved bid is inhibited by the N-terminal fragment." in: The Journal of biological chemistry, Vol. 275, Issue 30, pp. 22713-8, (2000) (PubMed).

Wang, Yin, Chao, Milliman, Korsmeyer: "BID: a novel BH3 domain-only death agonist." in: Genes & development, Vol. 10, Issue 22, pp. 2859-69, (1996) (PubMed).

Target Details for BID

Target: BID (BH3 Interacting Domain Death Agonist (BID))

Alternative Name: Bid (BID Products)

Background: Members of the Bcl-2 protein family function to inhibit (Bcl-2, Bcl-XL, Mcl-1, A1) or promote (Bax, Bak, Bcl-Ls, Bad) apoptosis. Bid is a Bcl-2 family death agonist that heterodimerizes with either agonists (Bax) or antagonists (Bcl-2). Bid contains a centrally located BH3 domain that allows interaction with the BH1 domain of Bax and Bcl-2. However, Bid does not contain other domains commonly found in Bcl-2 family members, such as BH1, BH2, or BH4. In addition, Bid does not contain a C-terminal hydrophobic region that is characteristic of membrane-bound Bcl-2 family members. Singlet oxygen-induced apoptosis in human leukemia cells and Fas-induced apoptosis involve caspase-8 cleavage of Bid, which produces a 15 kDa C-terminal fragment and a 6.5 kDa N-terminal fragment. The C-terminal fragment translocates to the mitochondria and promotes the release of cytochrome C through a mechanism that might involve destabilization of the mitochondrial membrane. Thus, the proapoptotic role of Bid may involve mitochondrial membrane destabilization, as well as multiple protein-protein interactions.

Molecular Weight: 23 kDa

Pathways: Apoptosis, Caspase Cascade in Apoptosis, Positive Regulation of Endopeptidase Activity