Recombinant mouse AHA1 protein is a Mouse Full Length protein, in the 1 to 338 aa range, expressed in Escherichia coli, with >90% purity and suitable for WB, FuncS.
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155).
Activator of 90 kDa heat shock protein ATPase homolog 1, AHA1, Ahsa1
Recombinant mouse AHA1 protein is a Mouse Full Length protein, in the 1 to 338 aa range, expressed in Escherichia coli, with >90% purity and suitable for WB, FuncS.
Constituents: 50% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.378% Tris HCl, 0.002% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155).
Belongs to the AHA1 family.
Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
AHA1 also known as activator of heat shock 90kDa protein ATPase homolog 1 is a co-chaperone protein that plays a role in the regulation of HSP90 ATPase activity. This protein has a molecular weight of approximately 38 kDa. AHA1 expression occurs in various tissues with higher amounts seen in metabolically active tissues. It interacts directly with HSP90 enhancing the chaperone's ability to fold client proteins correctly by stimulating its ATPase activity.
AHA1 modulates the function of the HSP90 chaperone complex. This complex is important for the stabilization and activation of many client proteins such as steroid hormone receptors and kinases. AHA1 binds to the middle domain of HSP90 contributing to conformational changes necessary for efficient ATP hydrolysis. By influencing these molecular processes AHA1 plays a role in maintaining cellular protein homeostasis under stress conditions.
The HSP90-AHA1 interaction is significant in the signaling pathway of cellular stress responses and protein folding. AHA1's upregulating effect on HSP90 ATPase activity facilitates the correct folding and function of client proteins involved in the MAPK/ERK and PI3K/AKT pathways. These pathways commonly involve interactions with proteins such as RAF and PI3K which are important in cell proliferation and survival processes.
AHA1 influences the progression of cancer and neurodegenerative diseases. Altered expression or function of AHA1 is linked to the development and progression of cancer as it affects the stability of oncoproteins through its interaction with HSP90. The protein is also connected to neurodegenerative diseases with disruptions in its function or expression impacting the folding and maintenance of neuronal proteins. In these diseases the AHA1-HSP90 interaction remains a critical component of pathogenic pathways affecting disease manifestation and progression.
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