BiP (AA 525-628) antibody

Details for Product No. ABIN968290
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

 
Antigen
Synonyms AL022860, AU019543, Bip, D2Wsu141e, D2Wsu17e, Grp78, Hsce70, SEZ-7, Sez7, baffled, mBiP
Epitope
AA 525-628
(1)
Reactivity
Human
(7), (5), (5), (2), (2), (2), (1), (1), (1)
Host
Mouse
(6), (2), (1), (1)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(1)
Application
Western Blotting (WB)
(10), (4), (3), (3), (1), (1)
Pubmed 5 references available
Catalog no. ABIN968290
Quantity 50 µg
Price
Contact our Customer Service for availability and price in your country.
Options
Shipping to United States (Change)
Add to Basket

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Immunogen Human BiP/GRP78
Clone DG10
Isotype IgG2a
Cross-Reactivity Dog (Canine), Rat (Rattus), Mouse (Murine)
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 Purified from tissue culture supernatant or ascites by affinity chromatography.
Purity Purified
Background Synthesis of nascent proteins occurs at sites on the endoplasmic reticulum (ER) called translocons. Translocon proteins form a pore in the membrane that allow passage of the newly synthesized protein from the ribosome into the ER lumen. As the nascent protein enters the lumen, it is bound by BiP (binding protein), the major chaperone of the ER. This protein is identical to the 78kDa glucose regulated protein, GRP78. BiP binds short hydrophobic sequences of the emerging peptide and prevents denaturation or nonspecific aggregation. Hydrolysis of ATP by BiP results in the release of the nascent protein which quickly assumes its proper conformation. However, if folding is incorrect, BiP again binds the protein and prevents its exit from the ER. In addition, BiP binding is thought to enhance the movement of secretory polypeptides across the ER membrane, but it is not required for protein translocation. It is 60% identical to Hsp70 and is similarly increased by conditions that produce incorrectly folded proteins. Thus, BiP is a chaperone of the ER lumen that binds misfolded or unassembled secretory proteins and ensures proper movement of proteins from the ER to the Golgi apparatus.
Molecular Weight 78 kDa
Comment

Related Products: ABIN968587, ABIN967389
Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Storage -20 °C
Supplier Images
anti-BiP (AA 525-628) antibody Western blot analysis of BiP on HepG2 cell lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of anti-BiP antibody.
Product cited in: Ting, Lee: "Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation." in: DNA (Mary Ann Liebert, Inc.), Vol. 7, Issue 4, pp. 275-86, 1988 (PubMed).

Yamazaki, Chang, Haass et al.: "Accumulation and aggregation of amyloid beta-protein in late endosomes of Niemann-pick type C cells." in: The Journal of biological chemistry, Vol. 276, Issue 6, pp. 4454-60, 2001 (PubMed).

Waelter, Boeddrich, Lurz et al.: "Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation." in: Molecular biology of the cell, Vol. 12, Issue 5, pp. 1393-407, 2001 (PubMed).

Morishima, Nakanishi, Takenouchi et al.: "An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12." in: The Journal of biological chemistry, Vol. 277, Issue 37, pp. 34287-94, 2002 (PubMed).

Han, Kim, Lee et al.: "Localization of phospholipase D1 to caveolin-enriched membrane via palmitoylation: implications for epidermal growth factor signaling." in: Molecular biology of the cell, Vol. 13, Issue 11, pp. 3976-88, 2002 (PubMed).

Hosts (6), (2), (1), (1)
Reactivities (7), (5), (5), (2), (2), (2), (1), (1), (1)
Applications (10), (4), (3), (3), (1), (1)
Conjugates (1)
Epitopes (1)
back to top