P23 Antibody (G-7): sc-376725

P23 Antibody (G-7) is a mouse monoclonal IgG1 antibody that detects P23 in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). P23, also known as PTGES3 (prostaglandin E synthase 3) or TEBP (telomerase-binding protein p23), is a ubiquitously expressed protein that serves as a cochaperone within the HSP 90-based molecular chaperone complex, playing a crucial role in signal transduction. P23 is primarily located in the cytoplasm, where P23 interacts with various steroid hormone receptors, including the glucocorticoid receptor (GR) and estrogen receptor alpha (ERα). P23 interaction with these receptors is vital, as P23 facilitates the proper folding and maturation of these proteins, thereby influencing their transcriptional activity. By promoting the disassembly of transcriptional regulatory complexes, P23 can inhibit GR-dependent transcription, which is essential for regulating cellular responses to hormonal signals. P23 involvement in these pathways highlights P23 significance in cellular processes and potential role in cancer biology, as P23 upregulation has been associated with increased invasion and metastasis in various cancer types. Anti-P23 antibody (G-7) is an invaluable tool for researchers studying the intricate mechanisms of hormone signaling and P23 implications in disease states.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

P23 Antibody (G-7) References:

1. The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies.  |  Freeman, BC., et al. 2000. Genes Dev. 14: 422-34. PMID: 10691735
2. Localization of sites of interaction between p23 and Hsp90 in solution.  |  Martinez-Yamout, MA., et al. 2006. J Biol Chem. 281: 14457-64. PMID: 16565516
3. cPGES/p23 is required for glucocorticoid receptor function and embryonic growth but not prostaglandin E2 synthesis.  |  Lovgren, AK., et al. 2007. Mol Cell Biol. 27: 4416-30. PMID: 17438133
4. p23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity.  |  Forafonov, F., et al. 2008. Mol Cell Biol. 28: 3446-56. PMID: 18362168
5. A truncated form of p23 down-regulates telomerase activity via disruption of Hsp90 function.  |  Woo, SH., et al. 2009. J Biol Chem. 284: 30871-80. PMID: 19740745
6. Global functional map of the p23 molecular chaperone reveals an extensive cellular network.  |  Echtenkamp, FJ., et al. 2011. Mol Cell. 43: 229-41. PMID: 21777812
7. miRNA mediated up-regulation of cochaperone p23 acts as an anti-apoptotic factor in childhood acute lymphoblastic leukemia.  |  Liu, X., et al. 2012. Leuk Res. 36: 1098-104. PMID: 22677230
8. Lettuce chlorosis virus P23 Suppresses RNA Silencing and Induces Local Necrosis with Increased Severity at Raised Temperatures.  |  Kubota, K. and Ng, JC. 2016. Phytopathology. 106: 653-62. PMID: 26828232
9. Hsp90 and p23 Molecular Chaperones Control Chromatin Architecture by Maintaining the Functional Pool of the RSC Chromatin Remodeler.  |  Echtenkamp, FJ., et al. 2016. Mol Cell. 64: 888-899. PMID: 27818141
10. Down-Regulation of p23 in Normal Lung Epithelial Cells Reduces Toxicities From Exposure to Benzo[a]pyrene and Cigarette Smoke Condensate via an Aryl Hydrocarbon Receptor-Dependent Mechanism.  |  Chen, J., et al. 2019. Toxicol Sci. 167: 239-248. PMID: 30204910

The preferred P23 antibody is P23 Antibody (JJ6): sc-101496.