HSC70-Interacting Protein (HIP)

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 interacts with the ATPase domain of Hsc70 molecules through its tetratricopeptide repeats and flanking charged alpha-helices (2). Hip and BAG-1 proteins have been shown to compete in binding to the ATPase domain (4). 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 has 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 and BAG-1, Hip may regulate the chaperone activity of Hsc70 by stabilizing the chaperone-substrate complex.\n\nApplications:\nWestern Blot (Colorimetric): 1:5,000 (mouse, rat)\nWestern Blot (Colorimetric): 1:1,000 (human, bovine)\nOptimal dilutions to be determined by researcher.\nPositive Controls\nRecombinant Rat Hip Protein

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SPECIFICATIONS

Catalog Number

H7651

Size

25ul

Applications

WB

Hosts

Rabbit

Reactivities

Hum, Mouse, Rat, Bov

Form

Serum

P Type

Pab

Purity

Serum

Isotype

IgG

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. Hohfeld, J. and Jentsch, S. (1997) EMBO J. 16: 6209-6216.\n

Additional Info

Detects a ~58kD protein, corresponding to the apparent molecular mass of Hip on SDS-PAGE immunoblots, in samples from human, mouse, rat and bovine. The antibody detects both recombinant rat Hip as well as native Hip protein in tissue extracts. Whilst reactivity with human and bovine Hip protein is detected, this reactivity is much weaker than that observed with samples from rat or mouse origin.