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 (MIM 140571), an inducible form, and HSP90AB1, a constitutive form.

Western

Western blot analysis of Hsp90 beta in Jurkat (1), A431 (2), Hela (3), A549 (4), HEK293 (5), K562 (6), NIH/3T3 (7), PC-12 (8) and Cos7 (9) cell lysate using Hsp90 beta antibody.

Immunocytochemistry

Immunocytochemistry analysis of Hsp90 beta in Hela cells using Hsp90 beta antibody (green),and DAPI(blue). Red: Actin filaments have been labeled with Alexa Fluor- 555 phalloidin.