BID Antibody

Western Blot: BID Antibody [NB100-56108] - Used at 1:2000 and detected in vitro translated Bid, but not in vitro translated Bcl-2, Bcl-xL, Bax, or Bad. These results show that this antibody is specific for Bid and does not crossreact with other Bcl-2 family members.

Immunohistochemistry-Paraffin: BID Antibody [NB100-56108] - Bid Antibody [NB100-56108] - Used at 1:2000 to stain Mouse Embryos. A) Intrauterine embryo at E.95 dpc (days post conception). B) 10.5-11 dpc Embryo isolated from the yolk sac. Hematoxylin-eosin counterstain.

Immunohistochemistry-Paraffin: BID Antibody [NB100-56108] - Bid Antibody [NB100-56108] - Used at 1:2000 to stain Human tissue sections. A) and Adult Pancreas B) Adult mesencephalon (midbrain). A1 and B1 are higher magnifications of A and B, respectively. Hematoxylin-eosin counterstain

Product Discontinued

BID Antibody Summary

• Immunogen: A synthetic peptide corresponding to amino acids 28-50 (CSDNSFRRELDALGHELPVLAPQ) of human Bid (also known as Bid, isoform 2) was used as immunogen; GenBank no. NP_001187.1. Human Bid is a 195 amino acid protein.
• Specificity: 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.
• Isotype: IgG
• Clonality: Polyclonal
• Host: Rabbit
• Gene: BID
• Purity: Unpurified

Applications/Dilutions

• Dilutions:
  • Immunohistochemistry
  • Immunohistochemistry-Paraffin 1:1000-1:5000
  • Immunoprecipitation 1:50-1:200
  • Western Blot 1:1000-1:2000

Reactivity Notes

Mouse, Canine, Rat reactivity reported in scientific literature (PMID: 15380478).

Packaging, Storage & Formulations

• Storage: Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
• Buffer: Whole antisera
• Preservative: 0.05% Sodium Azide
• Purity: Unpurified

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
• BID
• desmocollin type 4
• FP497
• Human BID coding sequence
• MGC15319
• MGC42355
• p22 BID
• tbid

Background

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 antiapoptotic (prosurvival) and proapoptotic (prodeath) members. Cellular homeostasis is thought to be dependent on a balance between the actions of antiapoptotic 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) Antiapoptotic: 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. Antiapoptotic 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 antiapoptotic 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 antiapoptotic and proapoptotic proteins determines the susceptibility of a cell to various apoptotic stimuli. Many Bcl-2 family proteins are differentially expressed in various malignancies and some are useful prognostic biomarkers. Antiapoptotic 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 syndrome, cardiovascular diseases, diabetes, glomerulonephritis, and muscular dystrophy. Recognizes Bid (approx. 19-23 kDa) Bid. It also recognizes cleaved/truncated forms which contain amino acids 28-55. The C-terminal cleaved/truncated form (11-15 kDa), often referred as tBid in the literature, is not predicted to contain amino acids 28-55 (reviewed in Yin, 2006). However, 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.

Limitations

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.

Publications for BID Antibody (NB100-56108)(1)

Publication using NB100-56108

• Krajewska M, Rosenthal RE, Mikolajczyk J et al. Early processing of Bid and caspase-6, -8, -10, -14 in the canine brain during cardiac arrest and resuscitation. Exp Neurol. 2004-10-01 [PMID: 15380478] (IHC-P, WB, Canine, Mouse, Rat)
  
  Details:
  Antibodies cited: 1. Caspase-9 (Active/Cleaved), IMG-5705: WB: Fig 1A (recombinant human caspase-9), Fig 4A (recombinant human caspase-9, rat brain), Fig 4B-F (isolated mitochondria from rat liver or heart). Fig 5 (PC12 cells) IHC (P): Fig 2d-k (rat kidne

Bioinformatics

• Gene Symbol: BID
• Entrez:
  • 637(Human)
  • 12122(Mouse)
  • 64625(Rat)