Pure and full-length recombinant enzyme
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HOP (human recombinant)

Item No. 22733

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Hsp70/Hsp90 Organizing Protein
  • Stress-Induced Phosphoprotein
Purity
≥95% as estimated by SDS-PAGE
Source
N-terminally Histidine-tagged human HOP protein (full length) purified from E. coli
Amino Acids
2-543 (full length)
MW
65 kDa
Formulation (Request formulation change)
50 mM HEPES, pH 8.0, with 150 mM sodium chloride
UniProt Accession №
P31948
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    50 µg

    $267

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    Product Description

    HOP (Hsp70/Hsp90 Organizing Protein), also known as Stress-Induced Phosphoprotein 1 (STI1 or STIP1), acts as a co-chaperone to reversibly form a complex with Hsp70 and Hsp90 to assist in transfer of proteins between Hsp70 and Hsp90. The three tetratricopeptide repeat domains (TPR1, TPR2a, and TPR2b) act as binding regions, with TPR1 and TPR2B binding to Hsp70 and TPR2A binding to Hsp90. 1 Highly conserved in Eukaryotes, it is closely related to the yeast STI1. HOP is both a nuclear and cytoplasmic protein, capable of travel between both. 2 HOP has also been found to interact with several other proteins/complexes, including but not limited to: Hsc70, Hsp90α, Hsp90β, PACRG, METTL21B, FLCN, FNIP1, and FNIP2. 3,4,5,6,7

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Flom, G., Behal, R.H., Rosen, L., et al. Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions. Biochem J. 404(1), 159-167 (2007).

    2. Schmid, A.B., Lagleder, S., Gräwert, M.A., et al. The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. EMBO J. 31(6), 1506-1517 (2012).

    3. Harst, A., Lin, H., and Obermann, W.M. Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation. Biochem J. 387(Pt. 3), 789-796 (2005).

    4. Imai, Y., Soda, M., Murakami, T., et al. A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death. The Journal of Biological Chemisty 278(51), 51901-51910 (2003).

    5. Cloutier, P., Lavallée-Adam, M., Faubert, D., et al. A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9(1), 1-13 (2013).

    6. Silverstein, A.M., Galigniana, M.D., Chen, M.S., et al. Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin. The Journal of Biological Chemisty 272(26), 16224-16230 (1997).

    7. Woodford, M.R., Dunn, D.M., Blanden, A.R., et al. The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding. Nat. Commun. 7, 12037 (2016).