Aha1 antibody

Antigen: Aha1

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human, Mouse (Murine), Rat (Rattus)

Application: Western Blotting (WB), ELISA, Immunoprecipitation (IP), Immunohistochemistry (IHC), Immunocytochemistry (ICC)

Catalog no.: ABIN361853

Additional Information

Immunogen: Mouse Aha1

Format: Antiserum

Description: Aha1 is a member of the Hsp90 cochaperone family, and is thought to stimulate Hsp90 ATPase activity by competing with p23 and other co-chaperones for Hsp90 binding (1, 2). It may affect a step in the endoplasmic reticulum to Golgi trafficking. Aha1 also interacts with HSPCA/Hsp90 and with the cytoplasmic tail of the vesicular stomatistis virus glycoproteins (VSV G) (3). Aha1 is expressed in numerous tissues, including the brain, heart, skeletal muscle, and kidney, and at low levels, the liver and placenta. Aha1 might be a potential therapeutic strategy to increase sensitivity to HSP inhibitors (4).

Specificity: ~ 38kDa. Species cross-reactivity: Human, mouse, rat, other species not yet tested.

Application Details

Application Notes: Working Dilution 0.5-1:1000 for WB, IHC (1 in 10,000 using Antibody Amplifier)

Buffer: Rabbit antiserum

Storage: -20°C, 1 year+, shipped on cold packs or ambient

Restrictions: For Research Use only

Images

Aha1, human cell lines

Publications

Publications: Harst, Lin, Obermann: "Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation." in: The Biochemical journal, Vol. 387, Issue Pt 3, pp. 789-96, 2005 (PubMed).

Lotz, Brychzy, Heinz et al.: "A novel HSP90 chaperone complex regulates intracellular vesicle transport." in: Journal of cell science, Vol. 121, Issue Pt 5, pp. 717-23, 2008 (PubMed).

Holmes, Sharp, Hobbs et al.: "Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin." in: Cancer research, Vol. 68, Issue 4, pp. 1188-97, 2008 (PubMed).

Hainzl, Lapina, Buchner et al.: "The charged linker region is an important regulator of Hsp90 function." in: The Journal of biological chemistry, Vol. 284, Issue 34, pp. 22559-67, 2009 (PubMed).