Technical Data

B1770
Clone Type
Monoclonal
Host
Rabbit
Source
Human
Isotype
IgG
Clone Number
7H9(C50B12)
Grade
Purified
Applications
FC IHC WB
Crossreactivity
Hu Mo
Gene ID
3309
Shipping Temp
Blue Ice
Storage Temp
-20°C
Rabbit Anti-BiP

Secretory and transmembrane proteins are synthesized on polysomes and translocated into the endoplasmic reticulum (ER). Inside the ER, these proteins are often modified by disulfide bond formation, amino-linked glycosylation and folding. To help proteins fold properly, the ER contains a pool of molecular chaperones including BiP. BiP was identified as an immunoglobulin heavy chain binding protein in pre-B cells. It was also found to be induced at the protein level by glucose starvation. When protein folding is disturbed inside ER, BiP synthesis is increased. Subsequently, BiP binds to misfolded proteins to prevent them from forming aggregates and assists them to refold properly.

Applications
Suitable for use in Western Blot, Immunohistochemistry and Flow Cytometry. Other applications not tested.
Recommended Dilutions
Western Blot: 1:1000. Incubate membrane with diluted antibody in TBS, 5% BSA, 0.1% Tween-20 at 4°C with gentle shaking, overnight. Immunohistochemistry (Paraffin):1:200 (Antigen retrieval: Citrate/TBST-5% NGS) Immunohistochemistry (Frozen): 1:200 (10% neutral buffered formalin) Flow Cytometry: 1:200 Optimal dilutions to be determined by the researcher.
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Synthetic peptide corresponding to residues surrounding Gly584 of human BiP.
Form
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, <0.02% sodium azide, 50% glycerol
Purity
Purified
Specificity
Recognizes endogenous levels of total human BiP protein at ~78kD. Species Crossreactivity: mouse

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
US Biological reference:|1. Berthe A., et al. Protein N-glycosylation alteration and glycolysis inhibition both contribute to the antiproliferative action of 2-deoxyglucose in breast cancer cells. 2018. Breast Cancer Res Treat. https://doi.org/10.1007/s10549-018-4874-z.||1. Wabl, M. and Steinberg, C. (1982) Proc. Natl. Acad. Sci. USA 79, 6976-6978. 2. Haas, I.G. and Wabl, M. Nature 306, 387-389. 3. Munro, S. and Pelham, H.R. (1986) Cell 46, 291-300. 4. Kohno, K. et al. (1993) Mol. Cell Biol. 13, 877-890.
USBio References
1. Colin-Cassin C, Yao X, Cerella C, Chbicheb S, Kuntz S, Mazerbourg S, Boisbrun M, Chapleur Y, Diederich M, Flament S, Grillier-Vuissoz I. PPARγ-inactive Δ2-troglitazone independently triggers ER stress and apoptosis in breast cancer cells. Mol Carcinog. 2013 Nov 30. doi: 10.1002/mc.22109. |2. Berthe A., et al. Protein N-glycosylation alteration and glycolysis inhibition both contribute to the antiproliferative action of 2-deoxyglucose in breast cancer cells. 2018. Breast Cancer Res Treat. https://doi.org/10.1007/s10549-018-4874-z..
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