HSP90 proteins are essential molecular chaperones involved in signal transduction, protein folding, and degradation. They interact with cochaperones to fold newly synthesized or denatured proteins after stress. HSP90, abundant in eukaryotic cells, interacts with diverse proteins, modulating their stability or degradation, thus influencing multiple signaling pathways. Its ATP-driven conformational cycle operates as a dimer. Hsp90 has alpha and beta isoforms; alpha is stress-inducible and overexpressed in cancer cells. Targeting Hsp90 offers potential for intervening in various stages of oncogenic transformation.
This antibody recognizes the epitope EEVHHG within N-terminal part of ubiquitously expressed HSP90 beta.
References: Chen, Bin et al. Genomics vol. 86,6 (2005): 627-37.
Product Overview
Key info about the protein can be found under Product Information > Specifications and Features.
Alternative names: 90-kDa heat shock protein beta
