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HAF018). A specific band was detected for p23/PTGES3 at approximately 23 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1." class="big_lightbox" target="_blank">
VC001). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents." class="big_lightbox" target="_blank">
NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm." class="big_lightbox" target="_blank">
Species: Hu, Mu Applications: WB, IHC, ICC/IF Host: Mouse Monoclonal
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.