Western blot using HSP90AA1 polyclonal antibody (Cat # PAB10218) shows detection of a band at ~90 KDa corresponding to HSP90AA1 in various lysate preparations (arrowhead). COS-7 transfected with mutant K294R HSP90AA1 (left two lanes), COS-7 transfected with wild type HSP90AA1 (middle two lanes) and empty vector CSO-7 cells (right two lanes) were either treated with Trichostatin A (an HDAC inhibitor) or mock treated with DMSO only, as indicated. Transfected cells express either mutant or wt HSP90AA1 coupled to Flag™tag. Anti-Flag™ immunoprecipitation was performed prior to immunoblotting with HSP90AA1 polyclonal antibody. Personal Communication, Brad Scroggins, Urologic Oncology Branch, CCR, NCI, Rockville, MD.
HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1, an inducible form, and HSP90AB1 (MIM 140572), a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM
heat shock 90kD protein 1, alpha,heat shock 90kD protein 1, alpha-like 4,heat shock 90kD protein, alpha-like 4,heat shock 90kDa protein 1, alpha