Recombinant Human HSP90 alpha Protein, CF
Recombinant Human HSP90 alpha Protein, CF Summary
HSP90 alpha /HSP90AA1 is a molecular chaperone that assists in the folding of nascent polypeptides and the refolding of denatured proteins. Reaction conditions will need to be optimized for each specific application. IMPORTANT: HSP90 alpha /HSP90AA1 works in conjunction with the co-chaperones such as p23/PTGES3--both proteins are typically required for enzymatic activity. For in vitro use we recommend an initial co-chaperone concentration of 2-3 μM, with an equimolar (or greater) concentration of HSP90 alpha /HSP90AA1.
Accession # P07900
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
X mg/ml (X μM) in 50 mM HEPES pH 7.5, 50 mM KCl, 1 mM TCEP.
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: HSP90 alpha
Members of the HSP90 family are essential chaperones found in all organisms from bacteria to humans. HSP90 complexes often interact with proteins in their native conformation and help to maintain/stabilize ligand-bound states. In this capacity, HSP90 plays a central role in function and turnover of many proteins involved in processes such as signal transduction, cell cycle control and apoptosis. HSP70 family members and HSP90 complexes frequently act in tandem, with the former participating in the folding of the client proteins and HSP90 stabilizing them in a way favorable for interaction with ligands. HSP90 forms complexes with an array of co-chaperones that both regulate its interaction with client proteins and stimulate its ATPase activity. By binding to different co-chaperones HSP90 acquires specificity for different families of client proteins. Many of the HSP90-client proteins are involved in tumor cell growth and HSP90 inhibitors are important as potential anticancer drugs. Inhibition of HSP90 also prevents the formation of protein aggregates in models of Parkinson disease, Huntington disease, and others. This recombinant protein may be used in conjunction with p23 (AP-170) in various in vitro protein refolding assays.
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- Jackson S. E. (2013) Topics Curr. Chem. 328: 155-240.
- Pratt W.B., et al. (2008) J Biol Chem. 283: 22885-22889.
- Pratt W.B., et al. (2010) Exp. Biol. and Med. 235: 278-289.
- Waza M., et al. (2005) Nat. Med. 11: 1088-95.
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