Immunohistochemistry-Paraffin: Bid Antibody [NB100-56107] - Six representative cores from a human gastric carcinoma formalin-fixed, paraffin-embedded tissue microarray stained for Bid expression using this antibody at ...read more
Immunohistochemistry-Paraffin: Bid Antibody [NB100-56107] - Formalin-fixed, paraffin-embedded human gastric carcinoma tissue array stained for Bid expression using this antibody at 1:2000. Hematoxylin-eosin ...read more
Hu, Mu, Rt, CaSpecies Glossary
WB, IHC, IHC-Fr, IHC-P, IP
This product is unpurified. The exact concentration of antibody is not quantifiable.
A recombinant protein fragment corresponding to amino acids 1-55 of mouse Bid was used as immunogen.
Full-length Bid is known to undergo cleavage/truncation (reviewed in Yin, 2006). Bid was initially found to be cleaved and activated by capspase-8 following death receptor activation. The term "Bid" was first used to described the caspase-8 cleaved/truncated C-terminal Bid. Bid can be also cleaved by other proteases such as Granzyme B, calpains and cathepsin. The C-terminal portion is considered to be the active Bid moiety. This active form can translocate from the cytosol to the mitochondria. Therefore, the appearance of Bid in the mitochondria is considered to be an indication of active Bid. However, it should also be noted that Bid has been shown to translocate to the mitochondria without cleavage in some model systems. The proteolytic cleavage of Bid usually occurs in the unstructured loop region between the alpha 2 and alpha 3 helices, which is between amino acids (aa) 41 and 79 of Bid. For example, the caspase-8/3 cleavage site is at 60 (human) and 59 (mouse). It should be noted that after cleavage, the smaller N-terminal portion of Bid is not necessarily separated from the larger C-terminal portion. The exact size of the C-terminal cleavage products depends on the Bid cleavage sites; generally 11-15 kDa C-truncated cleavage forms are generated. Shorter C-terminal Bid cleavage products may result from protease cleavage that involves both caspases and other proteases. Full length Bid is quite stable, but cleaved/truncated forms may have a short half-life (less than 1.5 h) and degrade rapidly. Therefore, a time course may be useful when detecting Bid cleavage fragments.
Test in a species/application not listed above to receive a full credit towards a future purchase.
Dog, Gerbil, Human, Mouse, Rat Not yet tested in other species.
Alternate Names for BID Antibody
apoptic death agonist
BH3 interacting domain death agonist
BH3-interacting domain death agonist
BID isoform ES(1b)
BID isoform L(2)
BID isoform Si6
desmocollin type 4
Human BID coding sequence
The Bcl-2 family of apoptosis-related genes plays central roles in regulating apoptotic pathways (reviewed in Thomadaki and Scorilas, 2006). Regulation of cell death through apoptosis is critical for the maintenance of homeostasis, defense against infectious agents, and normal development. Bcl-2 family proteins regulate apoptosis primarily through the regulation of mitochondrial outer membrane permeability. In mammals, the family consists of both prosurvival (antiapoptotic) and proapoptotic (prodeath) members. Cellular homeostasis is thought to be dependent on a balance between the actions of prosurvival and proapoptotic proteins. Bcl-2 family proteins can be divided into 3 main subfamilies on the basis of their function and the content of their Bcl-2 homology (BH) domains, for example: 1) Prosurvival: Bcl-2, Bcl-XL, Bcl-W, A1, and Mcl-1 2) Proapoptotic (multidomain): Bax, Bak, and Bok. 3) BH3-only (proapoptotic): Bad, Bcl-XS, Bid, Bik, Bim, Blk, Bmf, Bnip, Noxa, and Puma. Prosurvival members inhibit cells from undergoing apoptosis, whereas proapoptotic and BH3-only subfamily members promote apoptosis. There are 4 BH domains (1-4) conserved among Bcl-2 family proteins. The BH domains are important for function as well as for heterodimerization between family members. Typical prosurvival family members have all four BH domains (1-4), whereas proapoptotic (multidomain) members have BH1, 2 and 3 domains and BH3-only members have only the BH3 domain. Overall, the relative ratio of prosurvival and proapoptotic proteins determines the suseptibility of a cell to various apoptotic stimuli. Many Bcl-2 family proteins are differentially expressed in various malignancies and some are useful prognostic biomarkers. Prosurvival proteins are often elevated in diverse cancers and have the potential to confer resistance to both endogenous cell death stimuli and cancer treatments. Alterations in the ratio or levels of Bcl-2 family proteins have been also associated with nonmalignant diseases including neurodegenerative diseases, autoimmune diseases, AIDs, Down's syndrome, cardiovascular diseases, diabetes, glomerulonephritis, and muscular dystrophy. NB100-56107 recognizes Bid (~19-23 kDa) Bid. It also recognizes cleaved/truncated forms which contain amino acids 1-55. The C-terminal cleaved/truncated form (11-15 kDa), often referred as tBid in the literature, is not predicted to contain amino acids 1-55 (reviewed in Yin, 2006). Howwever, NB100-56107 may recognize tBid in cases where the smaller N-terminal portion (containing amino acids 1-55) of Bid has not separated from the larger C-terminal portion. Please see Applications Notes for more information on the biology of Bid.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.