Heat Shock Protein 90, Co-chaperone p23 (HSP90, Telomerase-Binding Protein p23, Progesterone Receptor Complex p23)

Steroid receptors are ligand-dependent intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate hormone. Prior to activation, steroid receptors associate with a number of different proteins in both a stable and transient fashion. Steroid receptor complex proteins include heat shock proteins (HSP 70 and HSP 90), immunosuppressant binding proteins called immunophilins (the FK 506 binding proteins, FKBP 52 & FKBP 54 and the cyclosporin binding protein, CyP-40) and at least three other proteins termed p23, p60 and p48. p23 along with HSP 70, HSP 90 and p60, combine with progesterone receptor (PR) as members of a transient intermediate complex. Cloned human p23 encodes a protein of 160 amino acids that is highly conserved between species and shows no homology to previously identified proteins. p23 is a highly acidic phosphoprotein with an aspartic acid-rich C-terminal domain and multiple potential phosphorylation sites. In vitro studies have suggested that p23 binds to HSP90 and is necessary for the binding of HSP 90 and CyP-40 to PR. While neither its exact function nor mechanism of action have been identified, p23 appears to be an important factor in PR function.\n\nApplications: \nSuitable for use in Immunofluorescence, Western Blot and Immunoprecipitation. 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. For long-term storage and to avoid repeated freezing and thawing, aliquot Store at -20 degrees C. Aliquots are stable for at least 12 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.\n\nSold under license from Geron

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SPECIFICATIONS

Catalog Number

H1834-60H

Size

100ul

Applications

IF, IP, WB

Hosts

Mouse

Reactivities

Hum, Mouse, Ch/Bird, GP, Rabbit

Form

Supplied as a liquid in PBS, pH 7.2, 0.05% sodium azide.

P Type

Mab

Purity

Ascites

Isotype

IgG1

References

This product has been used in:Hu J et al. Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids. EMBO J 16:59-68 (1997). <PUBMED:9009268>Dittmar KD & Pratt WB Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation. J Biol Chem 272:13047-54 (1997). <PUBMED:9148915>Hutchison KA et al. The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90. J Biol Chem 270:18841-7 (1995). <PUBMED:7642537>Johnson JL & Toft DO Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol Endocrinol 9:670-8 (1995). <PUBMED:8592513>Johnson JL et al. Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes. Mol Cell Biol 14:1956-63 (1994). <PUBMED:8114727>Johnson JL & Toft DO A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23. J Biol Chem 269:24989-93 (1994). <PUBMED:7929183>

Additional Info

Species Crossreactivity: Crossreacts with Human, Rabbit, Mouse, Guinea pig and Chicken. Not yet tested in other species.