The Activator of HSP90 ATPase-1 (AHSA1), also known as p38, C14orf3, or ACA1, is a co-chaperone protein that plays a crucial role in the regulation of the heat shock protein 90 (HSP90) ATPase activity . This protein is essential for the proper functioning of HSP90, a molecular chaperone involved in the folding, stabilization, and activation of a wide range of client proteins, many of which are involved in signal transduction, cell cycle control, and stress responses .
AHSA1 binds to the middle domain of HSP90 (amino acids 272-627) and functions as an ATPase-activating protein . By stimulating the ATPase activity of HSP90, AHSA1 enhances the chaperone’s ability to assist in the proper folding and activation of its client proteins . This interaction is competitive, as AHSA1 competes with other co-chaperones, such as p23, for binding to HSP90 .
The activation of HSP90 by AHSA1 is critical for various cellular processes, including the endoplasmic reticulum to Golgi trafficking . AHSA1’s role in enhancing HSP90’s chaperone activity is particularly important in the context of cellular stress, where the demand for protein folding and stabilization is increased . Additionally, AHSA1 has been implicated in several diseases, including Parkinson’s disease and stomatitis, highlighting its significance in maintaining cellular homeostasis .
The Mouse Anti Human AHSA1 Antibody is a monoclonal antibody derived from the hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human AHSA1 protein . This antibody is used in various laboratory applications, including ELISA, Western blot analysis, immunocytochemistry, and immunofluorescence, to detect and study the AHSA1 protein .
The antibody has been tested to ensure specificity and reactivity, with recommended starting dilutions for Western blot analysis being 1:1000 . For optimal storage, the antibody should be kept at 4°C for up to one month or at -20°C for longer periods, avoiding freeze-thaw cycles to maintain stability .