Heat Shock Protein 90, Recombinant, Human (HSP90)

HSP90 has been identified in the cytosol, nucleus and endoplasmic reticulum, and is reported to exist in many tissue types. In several tissues, including smooth muscle, HSP-90 comprises up to 2% of total cellular protein. HSP90 functions as a dimer, assembled as part of heterocomplex. It possesses ATP-binding site and low ATPase activity. HSP90 is able to associate with actin filaments in certain conditions. Another important property of HSP90 is the binding of unoccupied steroid hormone receptors. HSP90 has been characterized as a molecular chaperone able to keep the target protein in a folding-competent state. It has an enhanced chaperone activity in oligomeric form at high temperatures. HSP90 function is sensitive to bivalent cations concentration.\n\nRecombinant HSP-90 produced in \nE. coli is a single non-glycosylated polypeptide chain containing 732 amino acids and having a molecular mass of 86.8kD. Recombinant HSP-90 is expressed with a 20aa His tag at the N-terminus and purified by proprietary chromatographic techniques.\n\nStorage and Stability: \nMay be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add 0.1% HSA or BSA, aliquot and store at -20 degrees C. Aliquots are stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

H1831-57R

Size

10ug

Form

Supplied as a sterile liquid in 20mM Tris-HCl, pH 7.4, 100mM sodium chloride.

Purity

~90% by RP-HPLC and SDS-PAGE

References

1. NMR Backbone Assignment of the N-terminal Domain of Human HSP90. J Biomol NMR 2006 Jul 5; 2. Synthesis of a red-shifted fluorescence polarization probe for Hsp90. Bioorg Med Chem Lett 2006 Jun 21; 3. Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms. BMC Genomics 2006 Jun 17;7(1):156 4. Sustained activation of protein kinase C down-regulates nuclear factor-{kappa}B signaling by dissociation of IKK-{gamma} and Hsp90 complex in human colonic epithelial cells. Carcinogenesis 2006 Jun 14; 5. [Construction of mammalian co-expression plasmid pIRES -LMP1-HSP90 beta and its expression in vitro] Sichuan Da Xue Xue Bao Yi Xue Ban 2006 May;37(3):339-43 6. Hsp90 structure: when two ends meet. Nat Struct Mol Biol 2006 Jun;13(6):478-80