anticorps GRP78, anticorps BiP, anticorps GRP-78, anticorps grp78, anticorps hspa5a, anticorps BIP, anticorps MIF2, anticorps AL022860, anticorps AU019543, anticorps Bip, anticorps D2Wsu141e, anticorps D2Wsu17e, anticorps Grp78, anticorps Hsce70, anticorps SEZ-7, anticorps Sez7, anticorps baffled, anticorps mBiP, anticorps cb865, anticorps fb60h09, anticorps fi36d04, anticorps wu:fb60h09, anticorps wu:fi36d04, anticorps zgc:55994, anticorps zgc:77606, anticorps 78 kDa glucose-regulated protein, anticorps heat shock protein family A (Hsp70) member 5, anticorps BiP/GRP78, anticorps glucose-regulated protein 78, anticorps putative glucose-regulated protein 78, anticorps Hsp70 family ATPase KAR2, anticorps heat shock protein family A (Hsp70) member 5 S homeolog, anticorps heat shock 70 kDa protein 5a, anticorps heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa), anticorps heat shock protein 5, anticorps heat shock protein family A member 5, anticorps CpipJ_CPIJ003550, anticorps HSPA5, anticorps grp78, anticorps LOC100533358, anticorps BiP/grp78, anticorps Tc00.1047053506585.40, anticorps Tb11.02.5450, anticorps Tb11.02.5500, anticorps LMJF_28_1200, anticorps KAR2, anticorps LOC100135840, anticorps hspa5.S, anticorps hspa5, anticorps Hspa5
Sujet
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