
Thermo Fisher Scientific P23 Polyclonal Antibody
Rabbit polyclonal antibody against human p23 protein, suitable for WB, IHC, and IP applications. Recognizes residues 110–160 of the human progesterone receptor complex p23. Predicted to cross-react with rat, chicken, bovine, and orangutan. Supplied as ...
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Applications
| Application | Tested Dilution |
|---|---|
| Western Blot (WB) | 1:2,000–1:10,000 |
| Immunohistochemistry (IHC) | 1:2,000–1:10,000 |
| Immunohistochemistry (Paraffin) (IHC (P)) | 1:2,000–1:10,000 |
| Immunoprecipitation (IP) | 2–10 µg/mg lysate |
Product Specifications
| Property | Description |
|---|---|
| Host / Isotype | Rabbit / IgG |
| Class | Polyclonal |
| Type | Antibody |
| Immunogen | Region between residue 110–160 of human Progesterone Receptor Complex p23 (UniProt ID: Q15185-1) |
| Conjugate | Unconjugated |
| Form | Liquid |
| Concentration | 1 mg/mL |
| Storage Conditions | 4°C |
| Shipping Conditions | Wet ice |
Product Specific Information
- Recommended shelf life: 1 year from date of receipt
- For IHC, epitope retrieval with citrate buffer pH 6.0 is recommended for FFPE tissue sections
- Based on 100% sequence identity, this antibody is predicted to react with Rat, Chicken, Bovine, and Orangutan
Target Information
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 various proteins in both stable and transient complexes. These include heat shock proteins (HSP70, HSP90), immunophilins (FKBP52, FKBP54, CyP-40), and other proteins termed p23, p60, and p48.
p23, together with HSP70, HSP90, and p60, forms part of a transient intermediate complex with the progesterone receptor (PR). The cloned human p23 encodes a 160-amino-acid protein, highly conserved across species, with no homology to previously identified proteins. It is a highly acidic phosphoprotein containing an aspartic acid-rich C-terminal domain and multiple potential phosphorylation sites.
In vitro studies suggest that p23 binds to HSP90 and is necessary for the binding of HSP90 and CyP-40 to PR. Although its exact function and mechanism remain unclear, p23 appears to play an important role in PR function.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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