AHA1 Antibody, Clone 25F2.D9: Streptavidin

Activator of HSP90 ATPase Homolog 1 (AHA1) is a critical member of the HSP90 co-chaperone family, known for its role in regulating protein folding and stability. AHA1 enhances the ATPase activity of HSP90, a central molecular chaperone, by competitively displacing other co-chaperones such as p23, thereby accelerating the chaperone cycle and influencing client protein maturation. AHA1 is implicated in endoplasmic reticulum (ER) to Golgi trafficking, a process essential for proper protein sorting and cellular homeostasis. It also interacts with HSP90 (HSPCA) and the cytoplasmic tail of vesicular stomatitis virus glycoproteins (VSV G), suggesting a broader role in viral pathogenesis and intracellular transport mechanisms. Importantly, AHA1 is widely expressed across multiple tissues, including the brain, heart, skeletal muscle, and kidney, with lower expression levels observed in the liver and placenta. Its presence in the central nervous system highlights its potential relevance in neurodegenerative disease pathways, where protein misfolding and aggregation are hallmark features. Emerging evidence suggests that targeting AHA1 may enhance the efficacy of HSP90 inhibitors, positioning it as a promising therapeutic co-target in diseases characterized by proteostasis imbalance, such as Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease.

1 µg/ml of SMC-172 was sufficient for detection of Aha1 in 10 µg of rat tissue lysate by colorimetric immunoblot analysis using Goat anti-rat IgG:HRP as the secondary antibody.

1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.

1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3) : 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121 (pt.5) : 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68 (4) : 1188-1197.