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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.
BD Transduction Laboratories™ Purified Mouse Anti-BiP/GRP78
Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml.
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
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.
Development References (5)
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Han JM, Kim Y, Lee JS. Localization of phospholipase D1 to caveolin-enriched membrane via palmitoylation: implications for epidermal growth factor signaling. Mol Biol Cell. 2002; 13(11):3976-3988. (Clone-specific: Western blot). View Reference
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Morishima N, Nakanishi K, Takenouchi H, Shibata T, Yasuhiko Y. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem. 2002; 277(37):34287-34294. (Clone-specific: Western blot). View Reference
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Ting J, Lee AS.. Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA. 1988; 7(4):275-286. (Biology). View Reference
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Waelter S, Boeddrich A, Lurz R. Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol Biol Cell. 2001; 12(5):1393-1407. (Clone-specific: Immunofluorescence). View Reference
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Yamazaki T, Chang TY, Haass C, Ihara Y. Accumulation and aggregation of amyloid beta-protein in late endosomes of Niemann-pick type C cells. J Biol Chem. 2001; 276(6):4454-4460. (Clone-specific: Western blot). View Reference
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