Abcam, ab111143, Recombinant mouse AHA1 protein

Size: 50µg
Recombinant mouse AHA1 protein is a Mouse Full Length protein, in the 1 to 338 aa range, expressed in Escherichia coli, with >90%, suitable for WB, FuncS.
Key facts
Purity:>90% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:WB, FuncSSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:2uM ab111143 generated a 9-fold ATPase activation of 2uM Hsp90 (His-tagged Hsp90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees celcius (this is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm).,
Accession:Q8BK64,
Animal free:No,
Carrier free:No,
Species:Mouse,
Storage buffer:Constituents: 50% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.378% Tris HCl, 0.002% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Stable for 12 months at -20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
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.
Biological function summary
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.
Pathways
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.