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Description :Rabbit Polyclonal Antibody
Specificity :Recognizes the BID protein
Cited Applications :WB, ELISA, IF, IHC
Cross Reactivity :Human and Mouse
Host / Isotype / Clone# :Rabbit, IgG
Immunogen :BID antibody was raised against a peptide corresponding to 14 amino acids near the carboxy terminus of human BID
Formulation :PBS + 0.02% sodium azide.
Purification :Affinity chromatography
Stability :Store at 4oC (add 0.1% NaN3) for several months, and at -20oC for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
Sample Data :Western blot analysis of BID in mouse lung cell lysates with BID antibody at (A) 0.5, (B) 1, and (C) 2 ug/ml.
Sample Data :Immunohistochemical staining of mouse lung tissue using BID antibody at 2 ug/ml.
Scientific Background :BID is a BH3 interacting death domain that heterodimerizes with either agonist BAX or antagonist BCL2 (1). BID is a member of the BCL-2 family of cell death regulators and is a mediator of mitochondrial damage induced by caspase-8 (CASP8). BID initiates apoptosis by binding to regulatory sites on prosurvival BCL2 proteins to directly neutralize their function. Multiple alternatively spliced transcript variants of BID have been found, but the full-length nature of some variants has not been defined. BID together with Cathepsins play an important role in the actions of Camptothecin on breast cancer cells (2).
1. Hayakawa, A. et al:, Bid truncation mediated by caspases-3 and -9 in vinorelbine-induced apoptosis. Apoptosis. 2008;13(4):523-30.
2. Lamparska-Przybysz. M. et al: Cathepsins and BID are involved in the molecular switch between apoptosis and autophagy in breast cancer MCF-7 cells exposed to camptothecin. J Physiol Pharmacol. 2005 Jun;56 Suppl 3:159-79.
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Research Areas :Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Neurobiology, Cancer, Neurobiology, Cardiovascular Disease, Apoptosis/Autophagy