Heat Shock Protein 90kDa Beta (GRP94), also known as HSP90B1, is a molecular chaperone that plays a critical role in the folding, assembly, and stabilization of a wide range of proteins. It is a member of the HSP90 family and is predominantly found in the endoplasmic reticulum (ER). GRP94 is also referred to as endoplasmin, gp96, or ERp99 .
GRP94 is an ATP-binding protein that assists in the proper folding of newly synthesized proteins and the refolding of misfolded proteins within the ER. It is involved in the processing and transport of secreted proteins and is essential for the proper functioning of the immune system. GRP94 interacts with Toll-like receptors (TLRs) and integrins, playing a crucial role in both innate and adaptive immunity .
GRP94 is implicated in various cellular processes, including:
Monoclonal antibodies against GRP94, such as those produced in mice, are valuable tools in research and diagnostics. These antibodies are used to detect and quantify GRP94 in various biological samples. They are also employed in studying the role of GRP94 in different diseases and in the development of therapeutic interventions .
The mouse anti-human GRP94 antibody has several applications, including: