Western blot using HSP90AA1 polyclonal antibody (Cat # PAB10219) shows detection of a band at ~90 KDa corresponding to HSP90AA1 in an SK-BR-3 cell lysate (arrowhead) after treatment with Trichostatin A (an HDAC inhibitor). Western blotting results do not definitively demonstrate the acetyl K294 specificity of this reagent because similar staining is seen in the control lane (no treatment with TSA). Immuno-precipitation with HSP90AA1 polyclonal antibody was performed prior to immunoblotting with anti-HSP90AA1 acetyl K294.
Immunohistochemistry of HSP90AA1 polyclonal antibody (Cat # PAB10219) was used at 20 ug/mL to detect signal in a variety of tissues including multi-human, multi-brain and multi-cancer slides. This image shows moderate nuclear and granular cytoplasmic positive staining in human prostate carcinoma at 40X. Tissue was formalin-fixed and paraffin embedded. The image shows localization of the antibody as the precipitated red signal, with a hematoxylin purple nuclear counter stain. Personal Communi-cation, Tina Roush, Life Span Biosciences, Seattle, WA.
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