AHA1 Human
Description
Product Specs
GWQRYYFEGI KQTFGYGARL.
Product Science Overview
The Activator of HSP90 ATPase-1, also known as AHA1, is a co-chaperone protein that plays a crucial role in the regulation of the heat shock protein 90 (HSP90) ATPase activity. HSP90 is a molecular chaperone involved in the folding, stabilization, and activation of a wide range of client proteins, many of which are essential for cell survival and proliferation. AHA1 enhances the ATPase activity of HSP90, thereby facilitating its chaperone function.
AHA1 binds to the middle domain of HSP90, specifically between amino acids 272 and 627 . This binding stimulates the ATPase activity of HSP90, which is essential for the chaperone cycle. The activation of HSP90 by AHA1 is a critical step in the maturation and activation of client proteins, including steroid hormone receptors, kinases, and other signaling molecules .
Recombinant AHA1 is typically produced using bacterial expression systems. The gene encoding human AHA1 is cloned into an expression vector, which is then introduced into a suitable bacterial host, such as Escherichia coli. The bacteria are cultured, and the expression of AHA1 is induced. The recombinant protein is then purified using affinity chromatography techniques to achieve a high level of purity, often greater than 95% as determined by SDS-PAGE .
AHA1 affects a step in the endoplasmic reticulum to Golgi trafficking, which is crucial for the proper functioning of the secretory pathway . The interaction between AHA1 and HSP90 can be studied using various biochemical and biophysical techniques, including:
- Surface Plasmon Resonance (SPR): This technique can be used to measure the binding affinity between AHA1 and HSP90.
- Isothermal Titration Calorimetry (ITC): ITC can be employed to study the thermodynamics of the interaction between AHA1 and HSP90.
- X-ray Crystallography: This method can provide detailed structural information about the AHA1-HSP90 complex.
The study of AHA1 and its interaction with HSP90 has significant implications for understanding the molecular mechanisms underlying protein folding and stabilization. Additionally, AHA1 is of interest in the context of cancer research, as many HSP90 client proteins are involved in oncogenic signaling pathways. Inhibitors targeting the AHA1-HSP90 interaction are being explored as potential therapeutic agents for cancer treatment.
