Proteins - Purified Proteins, Heat Shock Proteins, Oxidative Cellular Stress

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Product Name: Aha1 (Recombinant, Human, Native sequence)
Catalog #: SPR-300C
Alternative Names: Aha1, SHSA1, HspC322, p38
Type: Recombinant Protein
Accession Number: NM_036243.1
Gene ID: 10598
SwissProt: O95433
Applications: WB control, functional/activity studies
Species: Human
Conjugate/Tag: Native
Form: Multi-step Chromatographically purified.
Storage Buffer: 20mM HEPES buffer p7.2, 80mM NaCl in 10% glyercol
Concentration: 1mg/mL
Certificate of Analysis: This product has been certified >90% pure using SDS PAGE analysis. 2uM SPR-300 generated a 9-fold ATPase activation of 2uM Hsp90 (His-tagged Hsp90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)
Background Info: Molecular weight of approximately 38kD
Package Size: 2x 100ug
Storage Temp: -20°C
Shipping Temp: Dry Ice, Blue Ice or 4°C
Datasheet: SPR 300 Ahsa1 Heat Shock
Research Area: Chaperones, Heat Shock
Price: $515.00 USD Add to Cart

SDS PAGE of native, human Aha1 protein.

Research 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.

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