Target: AHA1
Nature: Recombinant
Swiss-Prot: O95433
Expression System: E. coli
Amino Acid Sequence: SHMAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
Purification: Affinity Purified
Purity: >90%
Storage Buffer: 20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol
Protein Size: ~38 kDa
Conjugate: His tag
Cellular Localization: Cytoplasm
Scientific Background: 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).
References: 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.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.