Heat Shock Protein 90kDa Beta (GRP94) Member 1, also known as HSP90B1, is a molecular chaperone that plays a crucial role in the folding and stabilization of other proteins. It is a member of the heat shock protein 90 (HSP90) family and is predominantly found in the endoplasmic reticulum (ER). This protein is also referred to as endoplasmin, gp96, or ERp99 .
HSP90B1 is an ATP-metabolizing molecular chaperone that assists in the proper folding of secreted and membrane-bound proteins. It has ATPase activity, which is essential for its chaperone function. The protein is involved in the endoplasmic reticulum-associated degradation (ERAD) pathway, where it helps in the degradation of misfolded proteins .
HSP90B1 is also known to participate in the unfolding of cytosolic leaderless cargos, such as interleukin 1 (IL-1), to facilitate their translocation into the ER-Golgi intermediate compartment (ERGIC) and subsequent secretion. This translocation process is mediated by the cargo receptor TMED10 .
HSP90B1 plays a critical role in various biological processes, including:
The expression of HSP90B1 is associated with various pathogenic states, including tumor formation. It has been implicated in cancer progression and is considered a potential target for cancer therapy. Additionally, mutations in the HSP90B1 gene have been linked to diseases such as Pelizaeus-Merzbacher-Like Disease and Nemaline Myopathy 9 .
Mouse anti-human HSP90B1 antibodies are commonly used in research to study the protein’s function and its role in various diseases. These antibodies are generated by immunizing mice with human HSP90B1 protein, leading to the production of antibodies that specifically recognize and bind to the human version of the protein. These antibodies are valuable tools for detecting HSP90B1 in various experimental settings, including Western blotting, immunohistochemistry, and immunoprecipitation .