Hsp90 beta is a constitutively expressed isoform of the heat shock protein 90 (HSP90) family, located in the cytoplasm of cells. Unlike its counterpart Hsp90 alpha, which is induced under stress conditions, Hsp90 beta is consistently present in cells under normal conditions. As a molecular chaperone, Hsp90 beta plays a crucial role in maintaining cellular homeostasis by assisting in the proper folding of proteins, preventing their aggregation, and stabilizing various client proteins that are essential for cell growth, differentiation, and survival. These client proteins include kinases, transcription factors, and steroid hormone receptors, many of which are implicated in cancer progression when overexpressed or mutated. Additionally, Hsp90 beta is involved in regulating cellular processes such as the cell cycle, apoptosis, and signal transduction pathways. Its role in stabilizing oncogenic proteins makes it a target for cancer therapy, as inhibiting Hsp90 beta can lead to the degradation of these proteins, thereby disrupting cancer cell survival and proliferation.