|Other Names||Endoplasmin, 94 kDa glucose-regulated protein, GRP-94, Heat shock protein 90 kDa beta member 1, Tumor rejection antigen 1, gp96 homolog, HSP90B1, GRP94, TRA1|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity.|
|Cellular Location||Endoplasmic reticulum lumen. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
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Provided below are standard protocols that you may find useful for product applications.
HSP90 proteins are highly conserved molecular chaperonesthat have key roles in signal transduction, protein folding,protein degradation, and morphologic evolution. HSP90 proteinsnormally associate with other cochaperones and play important rolesin folding newly synthesized proteins or stabilizing and refoldingdenatured proteins after stress. HSP90B1 is an endoplasmicreticulum HSP90 protein. Other HSP90 proteins are found in cytosol(see HSP90AA1; MIM 140571) and mitochondria (TRAP1; MIM 606219)(Chen et al., 2005 [PubMed 16269234]).
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Suzuki, S., et al. Biochem. Biophys. Res. Commun. 398(3):525-531(2010)Bloor, S., et al. Proc. Natl. Acad. Sci. U.S.A. 107(15):6970-6975(2010)Davila, S., et al. Genes Immun. 11(3):232-238(2010)Wang, X., et al. Clin. Dev. Immunol. 2010, 212537 (2010) :
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