HSP90 alpha ELISA Kit

Heat Shock Protein 90 (HSP90) is a highly conserved molecular chaperone that plays a critical role in maintaining protein homeostasis within the cell. It assists in the proper folding, stabilization, and activation of a wide range of client proteins, many of which are involved in essential cellular processes such as signal transduction, cell cycle regulation, and stress responses. HSP90 expression is typically upregulated during cellular stress conditions—including heat, oxidative stress, and infection—to protect proteins from misfolding and degradation. This elevated expression is also commonly observed in rapidly dividing or stressed cells, such as cancer cells.
In research settings, HSP90 is widely studied as a key regulator of protein stability and as a central player in the cellular stress response. Its interaction with numerous oncogenic client proteins (e.g., HER2, AKT, RAF) has made it a valuable target for cancer biology research, drug discovery, and mechanistic studies of tumor progression. HSP90 inhibitors, such as geldanamycin derivatives, are commonly used tools to probe protein stability, test dependency of cancer cells on chaperone networks, and explore therapeutic vulnerabilities.
Clinically, HSP90 is of interest both as a biomarker and as a therapeutic target. Elevated HSP90 levels in biological fluids or tissues may reflect cellular stress, tumor burden, or inflammatory activity. Several clinical trials have evaluated HSP90 inhibitors as potential treatments for cancer, neurodegenerative diseases, and inflammatory conditions due to the protein’s central role in maintaining pathogenic protein states. Although no HSP90 inhibitor has yet achieved broad clinical approval, ongoing research continues to explore its utility in diagnostics, prognostics, and targeted therapy development.

This product is manufactured in Canada by StressMarq.