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SPR-313A SPR-312A SPR-313B SPR-312B +2

AHA2 Protein

Stressmarq Biosciences

DESCRIPTION

Human Recombinant AHA2 Protein

DETAILS

  • Nature: Recombinant
  • Purity: >90%
  • Target: AHA2
  • Category: Protein
  • Conjugate: His tag
  • 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.
  • Applications: WB | SDS-PAGE
  • Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
  • Protein Size: ~38 kDa
  • Purification: Affinity Purified
  • Concentration: Lot/batch specific. See included datasheet.
  • Research Areas: Cancer | Heat Shock
  • Storage Buffer: 100mM NaH2PO4 pH4.5, 10mM Tris buffer with 8M urea
  • Alternative Names: ATPase hydrogen-exporting ATPase 2 Protein
  • Cite This Product: Human Recombinant AHA2 Protein (StressMarq Biosciences, Canada, Cat # SPR-312A)
  • Expression System: E. coli
  • Species Full Name: Human
  • Storage Temperature: -20ºC
  • Shipping Temperature: Blue Ice or 4ºC
  • Scientific Background: Aha2 shares 45% sequence homology with Aha1, however, little is known about the functional protein. 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).
  • Certificate of Analysis: This product has been certified >90% pure using SDS - PAGE analysis.