Immunoglobulin heavy chain binding

Molecular chaperone (relative molecular mass 78 K) found in the lumen of the ER. BiP is related to the Hsp70 family of heat-shock proteins and was originally described as immunoglobulin heavy chain binding protein. 

Chaperones. Figure 2 The multiple roles of BiP in the biogenesis of the secretory proteins. BiP, immunoglobulin heavy chain binding protein ER, endoplasmic reticulum ERAD, ER-associated degradation ERj, resident ER protein with J-domain Sec61, core subunit of the protein translocase UPR, unfolded protein response that involves several signal transduction pathways that are activated in order to increase the biosynthetic capacity and decrease the biosynthetic burden of the ER... 

Haas, LG. Meo, T. (1988). cDNA cloning of the immunoglobulin heavy chain binding protein. Proc. Natl, Acad. Sci. USA 85,2250-2254. 

Munro, S and Pelham, H. R. B (1986) An HSP70-like protein in the ER identity with the 78kD glucose-regulated protein and immunoglobulin heavy chain binding protein Cell 46,291-300. 

Witzmann FA, Jarnot BM, Parker DN, Clack JW. Modification of hepatic immunoglobulin heavy chain binding protein (BiP/Grp78) following exposure to structurally diverse peroxisome proliferators. Fundam Appl Toxicol 1994 23 1-8. 

Bole DG, Flendershot LM, Kearney JF (1986) Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in non-secreting and secreting hybri-domas. J Cell Biol 102 1558-1566... 

Haas, 1. G., and Wahl, M, (1983), Immunoglobulin heavy chain binding protein. Nature (London) 306, 387-389. 

Hendershot, L. M., Ting, J., and Lee, A. S. (1988). Identity of the immunoglobulin heavy-chain-binding protein with the 78,000-dalton glucose-regulated protein and the role of posttranslational modifications in its binding function. Mol. Cell. Biol. 8,4250-4256. 

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