HOP, Recombinant, Human (HSP70 HSP90 Organizing Protein)

Hop (Hsp70/Hsp90 Organizing Protein), or Stress-induced Phosphoprotein 1 (STI1) as it is also known, is a 60kDa protein that belongs to the large group of co-chaperones which regulate and assist the major chaperones. It is located in diverse cellular regions and can move between the cytoplasm and the nucleus. It functions to reversibly link together the protein chaperones Hsp70 and Hsp90. HOP contains three tetratricopeptide repeat (TPR) domains, TPR1, TPR2a and TPR2b. Hsp70 binding has been localized to TRP1 and sp90 binding have been localized to TPR2a (1). It has also been found to modulate the chaperone activities of the linked proteins and possible interacts with other chaperones and proteins. It has also been found to participate in other complexes besides the Hsp70/Hsp90 one (2). HOP is closely related to human 63kDa protein that is sensitive to simian virus SV40 transformation, and is related to the yeast heat-shock- responsive STI1 gene product (3, 4). \n \nSource:\nProtein, his-tagged, human CDNA; SwissProt: P31948 \n\nApplications:\nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20 degrees C. Aliquots are stable for at least 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

H6700-03

Size

50ug

Applications

WB

Form

Supplied as a liquid in 20mM HEPES buffer p7.2, 80mM sodium chloride in10% glyercol.

Purity

~90%

References

1. Flom G., Behal R.H., Rosen L., Cole D.G., Johnson J.L. (2007) Biochem J. 404(1):159-167. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387(pt3):789-796. 3. Honore B.H., et al. (1992) J Biol Chem. 267:8485-8491. 4. Nicolet C.M., et al. (1989) Mol Cell Bio. 9:3638-3646.