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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Progesterone receptor (PGR) is a ligand-activated nuclear hormone receptor encoded by the PGR gene and functions as a transcription factor that mediates cellular responses to progesterone signaling. PR Antibody for WB recognizes this steroid hormone receptor, which belongs to the nuclear receptor subfamily 3 group C member 3 (NR3C3) family of ligand-regulated transcription factors. The receptor is predominantly localized in the nucleus where it regulates gene transcription in response to progesterone binding, influencing reproductive biology, cellular differentiation, and hormone-dependent signaling pathways.
The PR Antibody for WB (clone RM357) is designed for western blot detection of Progesterone receptor protein in cell and tissue lysates. Western blot analysis is commonly used to evaluate Progesterone receptor expression levels and to distinguish the major receptor isoforms produced from the PGR gene. The two best characterized isoforms are PR-A and PR-B, which arise from alternative transcription start sites and differ in their N-terminal regulatory domains. These isoforms have distinct biological activities and often appear as separate bands in western blot experiments, making western blot analysis particularly valuable for studying progesterone receptor biology.
Progesterone receptor signaling plays an essential role in reproductive tissues such as uterus, ovary, and mammary gland, where hormone-dependent transcriptional regulation drives processes including ovulation, implantation, and mammary gland development. Because of this central role in hormone signaling, Progesterone receptor expression is frequently analyzed in breast cancer and other hormone-responsive tumors. Western blot detection of PGR protein provides a useful method for examining receptor expression levels, evaluating receptor isoform patterns, and monitoring signaling pathway changes in hormone-responsive cell models.
Western blot experiments targeting Progesterone receptor typically detect multiple protein species corresponding to the PR-A and PR-B isoforms, which differ in size due to the presence or absence of an N-terminal activation domain. In many experimental systems, the receptor may also appear as slightly shifted bands due to phosphorylation events that occur following hormone stimulation. These phosphorylation-dependent mobility changes are commonly observed in western blot analysis and reflect activation of the receptor and downstream transcriptional signaling.
Because Progesterone receptor functions as a transcriptional regulator, its expression and stability are tightly controlled by hormone signaling pathways, receptor turnover, and ligand-dependent activation. Western blot analysis therefore provides a valuable approach for monitoring receptor abundance, assessing hormone-dependent regulation, and evaluating receptor degradation or stabilization following pharmacological treatments. PR Antibody for WB is useful for detecting Progesterone receptor expression in research studies investigating steroid hormone signaling, endocrine regulation, and hormone-responsive cancer biology.
The stated application concentrations are suggested starting points. Titration of the PR Antibody for WB may be required due to differences in protocols and secondary/substrate sensitivity.
A peptide corresponding to C-terminus of human Progesterone Receptor was used as the immunogen for the PR Antibody for WB.
Store the PR/Progesterone Receptor antibody at -20oC.
Progesterone receptor antibody, PGR antibody, NR3C3 antibody, Progesterone receptor A antibody, Progesterone receptor B antibody
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