Product Details
Alternative Name: | Progesterone receptor complex p23, Telomerase-binding protein p23 |
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Clone: | JJ3 |
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Host: | Mouse |
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Isotype: | IgG2a |
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Immunogen: | Recombinant human HSP90 Co-chaperone. |
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UniProt ID: | Q15185 |
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Species reactivity: | Human, Mouse Chicken, Guinea pig, Rabbit
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Applications: | ICC, IP, WB
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Recommended Dilutions/Conditions: | Immunoprecipitation (use on free or complexed HSP90 Co-chaperone) Western Blot (1:1,000) Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application. |
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Application Notes: | Detects a band of ~23kDa by Western blot. |
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Formulation: | Liquid. Ascites diluted in PBS containing 0.05% sodium azide. |
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Handling: | Avoid freeze/thaw cycles. |
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Shipping: | Shipped on Blue Ice |
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Long Term Storage: | -20°C |
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Scientific Background: | 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 (HSP70 and HSP90), immunosuppressant binding proteins called immunophilins (the FK506 binding proteins, FKBP52 & FKBP54 and the cyclosporin binding protein, CyP-40) and at least three other proteins termed p23, p60 and p48. p23 along with HSP70, HSP90 and p60, combine with progesterone receptor (PR) as members of a transient intermediate complex. Cloned human p23 encodes a protein of 160 aa 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 HSP90 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. |
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Regulatory Status: | RUO - Research Use Only |
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Product Literature References
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.: K.D. Dittmar & W.B. Pratt; J. Biol. Chem.
272, 13047 (1997),
Abstract;
Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids: J. Hu, et al.; EMBO J.
16, 59 (1997),
Abstract;
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