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Activator of 90kD Heat Shock Protein ATPase Homolog 1, Recombinant Human (Activator of Heat Shock 90kDa Protein ATPase Homolog 1, AHA1, AHSA1, C14orf3, HSPC322, p38) (Azide Free)

Cat no: A0855-78B

Activator of 90kD Heat Shock Protein ATPase Homolog 1, Recombinant Human (Activator of Heat Shock 90kDa Protein ATPase Homolog 1, AHA1, AHSA1, C14orf3, HSPC322, p38) (Azide Free)

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 \nsensitivity to HSP inhibitors (4). \n \nSource:\nHuman cDNA; Swiss/Prot: O95433 \n\nApplications:\nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

A0855-78B

Size

50ug

Applications

WB

Form

20mM HEPES buffer p7.2, 80mM sodium chloride in 10% glyercol.

Purity

~90%

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.

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