rat monoclonal IgG; GRP 78 Antibody (76-E6) is an IgG rat monoclonal GRP 78 antibody (also designated GRP78 antibody, HSPA5 antibody or BIP antibody) that detects the GRP 78 protein of mouse, rat and human origin by WB and IP. GRP 78 Antibody (76-E6) is available as both the non-conjugated anti-GRP 78 antibody form, as well as multiple conjugated forms of anti-GRP 78 antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. The HSP 70 family is composed of four highly conserved proteins: HSP 70, HSC 70, GRP 75 and GRP 78. These proteins serve a variety of roles: they act as molecular chaperones facilitating the assembly of multi-protein complexes, participate in the translocation of polypeptides across cell membranes and to the nucleus, and aid in the proper folding of nascent polypeptide chains. All members of the family, except HSP 70, are constitutively expressed in primate cells. HSP 70 expression is strongly induced in response to heat stress. HSP 70 and HSC 70 play key roles in the cytosolic endoplasmic reticulum and mitochondrial import machinery and are found in both the cytosol and nucleus of mammalian cells. Both HSP 70 and HSC 70 are involved in the chaperoning of nascent polypeptide chains and in protecting cells against the accumulation of improperly folded proteins. GRP 78 is localized in the endoplasmic reticulum, where it receives imported secretory proteins and is involved in the folding and translocation of nascent peptide chains. GRP 75 expression is restricted to the mitochondrial matrix and aids in the translocation and folding of nascent polypeptide chains of both nuclear and mitochondrial origin.