Technical Data
B1770
BiP
Description:
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 (1,2). It was also found to be induced at the protein level by glucose starvation (3). 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 (4).

Applications:
Suitable for use in ELISA, Western Blot and Immunohistochemistry. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000
Immunohistochemistry (Paraffin):1:200 (Antigen retrieval: Citrate/TBST-5%NGS)
Immunohistochemistry (Frozen): 1:200 (10% neutral buffered formalin)
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. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
MabIgG7H9Supernatant
SizeStorageShippingSourceHost
100ul-20°CBlue IceHumanRabbit
Concentration:
Not Determined
Immunogen:
Synthetic peptide corresponding to residues surrounding Gly584 of human BiP.
Purity:
Supernatant
Form
Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.
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.
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.