Heat Shock Cognate Protein 70, Recombinant, Rat (Hsc70-interacting protein, Hip, HSC70, Heat Shock Protein 73, HSP73)

Hsc70-interacting protein (Hip) is a cytosolic protein that exists as a homo-oligomer and participates in the regulation of the heat shock protein Hsc70 in eukaryotic cells (1). Hip \ninteracts with the ATPase domain of Hsc70 molecules through the tetratricopeptide repeats and flanking charged a-helices of Hip (2). This binding reaction is dependent on Hsp40 in the presence of ATP and becomes Hsp40-independent if Hsc70 is preincubated with ADP (2). Upon binding to Hsc70, Hip stabilizes the ADP-bound state of Hsc70, a conformation that \nhas a high affinity for unfolded substrate proteins. Hip by itself binds unfolded polypeptides, suggesting that it may possess chaperone activity (2,3). Together with Hsp40, Hip may regulate the chaperone activity of Hsc70 by stabilizing the chaperone-substrate complex. \n\nRat Hip has a carboxyl terminal addition of residues GSEQKLISEEDL, which represents glycine and serine residues followed by amino acids 410-419 of human c-myc protein. This protein is produced recombinantly in E. coli. It has an apparent molecular mass of ~54kD when fractionated on SDS-PAGE (1). \n\nHip is a member of a multi-protein complex involved in the assembly of progesterone receptor in vitro (4, 5). It serves as a cochaperone in the hsp70/hsp40-dependent protein refolding \ncycle of progesterone receptor in vitro. \n\nStorage and Stability:\nFor long-term storage, aliquot to avoid repeated freezing and thawing and freeze at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 12 months.

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SPECIFICATIONS

Catalog Number

H1830-25C

Size

100ug

Form

Supplied as a liquid in 20mM MOPS pH 7.2, 50mM KCl, 2mM MgCl2.

Purity

(same/more than) 85% as determined by SDS-PAGE analysis.

References

1. Hohfeld, J., Minami, Y., and Hartl, F.-U. (1995) Cell 83: 589-598. \n2. Irmer, H. and Hohfeld, J. (1997) J. Biol. Chem. 272: 2230-2235. \n3. Bruce, B.D. and Churchich, J. (1997) Eur. J. Biochem. 245: 738-744. \n4. Prapapanich, V., Chen, S., Toran, E.J., Rimerman, R.A. and Smith, D.F. (1996) Mol. Cell Biol. 16: 6200-6207. \n5. Prapapanich, V., Chen, S. and Smith, D.F. (1998) Mol. Cell Biol. 18: 944-952. \n