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BD Transduction Laboratories™ Purified Mouse Anti-BiP/GRP78
Clone 40/BiP (RUO)
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.
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 Details
BD Transduction Laboratories™
GRP78
Human (QC Testing), Mouse, Rat, Dog (Tested in Development)
Mouse IgG2a
Human BiP/GRP78 aa. 525-628
Western blot (Routinely Tested), Immunofluorescence (Not Recommended)
78 kDa
250 µg/ml
AB_398292
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
RUO
Preparation And Storage
The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.
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.
610978 Rev. 1
Antibody Details
40/BiP
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.
610978 Rev. 1
Format Details
Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
610978 Rev.1
Citations & References
View product citations for antibody "610978" on CiteAb
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
610978 Rev. 1
Please refer to Support Documents for Quality Certificates
Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.