Western blot analysis of cell lysates of HeLa (each 20 ug) was resolved by SDS - PAGE , transferred to PVDF membrane and probed with HSP90AA1 monoclonal antibody , clone 4F10 (1 : 1000) (Cat # MAB1092). Proteins were visualized using a goat anti - mouse secondary antibody conjugated to HRP and an ECL detection system.
Paraffin embedded sections of human urothelium were incubated with HSP90AA1 monoclonal antibody, clone 4F10 (Cat # MAB1092) (1:100) for 2 hours at room temperature. Antigen retrieval was performed in 0.1M sodium citrate buffer and detected using Diaminobenzidine (DAB).
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