The co-chaperone Aha1 (Activator of HSP90 ATPase-1) binds the middle domain of Hsp90 (aa272-627) and is proposed to function as an ATPase-activating protein that competes with p23 and other co-chaperones for Hsp90 binding.
Source:Recombinant human, AHA1, full length, with C-terminal HIS tag, expressed in E. coli.
Molecular Weight: 38kD
Specific Activity:The addition of AHA1 increased ATPase activity of hsp90-alpha from 0.18 to 0.94pmol/min/ug.
Assay conditions:50ul reaction mix (100mM TrisHCl pH7.4, 20mM KCl, 6mM MgCl2, 200uM ATP, and 5ug Hsp90a) was incubated with Aha1 (0-10g) for 3 hrs at 37°C. To stop the reaction, 100ul of the malachite green reagent was added to each well. Absorbance at 620nm was measured.
Applications:Suitable for use as ATPase activity assay for Hsp90-alpha. Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:Aliquot to avoid repeated freezing and thawing and store at -70°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 6 months.
仕様
Size：200ug
Source Antigen：Recombinant, E. coli
Grade：Purified
Purity：≥90%
Form：Supplied as a liquid in 25mM Tris-HCl, pH 8.0, 100mM NaCl, 0.05% Tween 20, 3 mM DTT, 50% glycerol.
