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HSP90 Co-chaperone monoclonal antibody (JJ3)

ALX-804-023-R100 100 µl 590.00 USD
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Product Specification

Alternative Name:Progesterone receptor complex p23, Telomerase-binding protein p23
Immunogen:Recombinant human HSP90 Co-chaperone.
UniProt ID:Q15185
Species reactivity:Human, Mouse
Chicken, Guinea pig, Rabbit
Applications:ICC, IP, WB
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.
Application Notes:Detects a band of ~23kDa by Western blot.
Formulation:Liquid. Ascites diluted in PBS containing 0.05% sodium azide.
Handling:Avoid freeze/thaw cycles.
Shipping:Shipped on Blue Ice
Long Term Storage:-20°C
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.

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; Full Text

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