GRP78 antikoerper, BiP antikoerper, GRP-78 antikoerper, grp78 antikoerper, hspa5a antikoerper, BIP antikoerper, MIF2 antikoerper, AL022860 antikoerper, AU019543 antikoerper, Bip antikoerper, D2Wsu141e antikoerper, D2Wsu17e antikoerper, Grp78 antikoerper, Hsce70 antikoerper, SEZ-7 antikoerper, Sez7 antikoerper, baffled antikoerper, mBiP antikoerper, cb865 antikoerper, fb60h09 antikoerper, fi36d04 antikoerper, wu:fb60h09 antikoerper, wu:fi36d04 antikoerper, zgc:55994 antikoerper, zgc:77606 antikoerper, 78 kDa glucose-regulated protein antikoerper, heat shock protein family A (Hsp70) member 5 antikoerper, BiP/GRP78 antikoerper, glucose-regulated protein 78 antikoerper, putative glucose-regulated protein 78 antikoerper, Hsp70 family ATPase KAR2 antikoerper, heat shock protein family A (Hsp70) member 5 S homeolog antikoerper, heat shock 70 kDa protein 5a antikoerper, heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa) antikoerper, heat shock protein 5 antikoerper, heat shock protein family A member 5 antikoerper, CpipJ_CPIJ003550 antikoerper, HSPA5 antikoerper, grp78 antikoerper, LOC100533358 antikoerper, BiP/grp78 antikoerper, Tc00.1047053506585.40 antikoerper, Tb11.02.5450 antikoerper, Tb11.02.5500 antikoerper, LMJF_28_1200 antikoerper, KAR2 antikoerper, LOC100135840 antikoerper, hspa5.S antikoerper, hspa5 antikoerper, Hspa5 antikoerper
Hintergrund
The immunoglobulin heavy chain binding protein BiP (Binding Protein) is a member of the hsp70 family of heat shock proteins, and is identical to the glucose regulated protein grp78.2 While BiP was originally described for its function in B cells, it is now known to be distributed in a variety of tissues, if not ubiquitous. The highly conserved hsp 70 proteins have an essential physiological role in stress responses and as molecular chaperones, which are responsible for a variety of functions such as protein transport, prevention of protein toxicity and direction of protein folding.1-5 With regard to its immunological role, BiP is a component of the endoplasmic reticulum and binds free intracellular heavy chains in nonsecreting pre-B cell lines (+,L-) or incompletely assembled Ig precursors in H+L+ secreting hybridomas and myelomas. In the absence of light chain synthesis, heavy chains remain associated with BiP and are not secreted. BiP is an ATP binding protein and the dissociation of the BiP-heavy chain complex is probably driven by the ATPase activity attributed to BiP.7