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Hsp90α (human recombinant)

Cayman Chemical Item Number 10202

Hsp86; Heat Shock Protein 90α

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Description

Source: active recombinant N-terminal His-tagged protein, expressed in E. coli · Mr: 87 kDa · Heat shock proteins (Hsps) are molecular chaperones that can account for upwards of 1-2% of all cellular protein.1 The Hsp90 gene family consists of Hsp90A, Hsp90B, and TRAP subfamilies. The Hsp90A family is localized in the cytoplasm and can be further sub-divided into Hsp90AA (inducible) and Hsp90AB (constitutively expressed), yielding Hsp90α and Hsp90β proteins respectively. Hsp90B codes for the ER-localized protein Grp94, while TRAP, producing TRAP1, is a mitochondrial chaperone.2 Hsp90 acts as a dimer, which can be homo or heterodimers of the α and β isoforms, and functions to bind protein substrates that are unfolded and/or misfolded to assist in folding and prevent aggregation.3 C-terminus dimerization of Hsp90, coupled with the ATPase molecular clamp activity cause a conformational change in the N-terminal nucleotide binding domain thus facilitating substrate binding.4 Hsp90 associates with many co-chaperones including p23/Sba1, which help in recruiting substrates to the Hsp90 complex.5 Hsp90 works on many different substrates, however its activity seems to be more specific for protein kinases involved in signal transduction, steroid receptors, and cytoskeletal proteins.1

1 Csermely, P., Schnaider, T., Soti, C., et al. The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review. Pharmacol Ther 79(2) 129-168 (1998).

2 Chen, B., Piel, W.H., Gui, L., et al. The HSP90 family of genes in the human genome: Insights into their divergence and evolution. Genomics 86 627-637 (2005).

3 Fink, A.L. Chaperone-mediated protein folding. Physiol Rev 79(2) 425-449 (1999).

4 Prodromou, C., Panaretou, B., Chohan, S., et al. The ATPase cycle of Hsp90 drives a molecular “clamp” via transient dimerization of the N-terminal domains. EMBO J 19(16) 4383-4392 (2000).

5 Ali, M.M.U., Roe, S.M., Vaughan, C.K., et al. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440 1013-1017 (2006).

Synonyms
  • Hsp86
  • Heat Shock Protein 90α
Formulation 50 mM sodium phosphate, pH 7.2, containing 100 mM sodium chloride, 5 mM MgCl2, 1 mM DTT, and 20% glycerol
Purity ≥80%
Stability 6 months
Storage -80°C
Shipping Dry ice in continental US; may vary elsewhere

Background Reading

Fink, A.L. Chaperone-mediated protein folding. Physiol Rev 79(2) 425-449 (1999).

Prodromou, C., Panaretou, B., Chohan, S., et al. The ATPase cycle of Hsp90 drives a molecular “clamp” via transient dimerization of the N-terminal domains. EMBO J 19(16) 4383-4392 (2000).

Ali, M.M.U., Roe, S.M., Vaughan, C.K., et al. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440 1013-1017 (2006).

Csermely, P., Schnaider, T., Soti, C., et al. The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review. Pharmacol Ther 79(2) 129-168 (1998).

Chen, B., Piel, W.H., Gui, L., et al. The HSP90 family of genes in the human genome: Insights into their divergence and evolution. Genomics 86 627-637 (2005).

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Size Price Quantity Subtotal
25 µg $52.00 $0.00
50 µg $99.00 $0.00
100 µg $187.00 $0.00
Bulk Contact
Cart Total $0.00

This product is available in custom sizes and/or larger quantities.

Please contact our Sales Department for a quote or to purchase.

Pricing updated 2012-05-26. Prices are subject to change without notice.

To ask for assistance with one of our products please contact a Technical Support Scientist.

Warning This product is not for human or veterinary use.

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