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HSP90 Co-chaperone monoclonal antibody (JJ3)

 
ALX-804-023-R100 100 µl 607.00 USD
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Product Specification

Alternative Name:Progesterone receptor complex p23, Telomerase-binding protein p23
 
Clone:JJ3
 
Host:Mouse
 
Isotype:IgG2a
 
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.
 
Regulatory Status:RUO - Research Use Only
 

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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