The Phospho-Progesterone Receptor (Ser190) antibody is a specialized tool used to detect the progesterone receptor (PR) when phosphorylated at serine residue 190. PR, a member of the nuclear receptor superfamily, exists as two isoforms (PRA and PRB) and mediates progesterone’s effects in reproductive tissues, mammary glands, and the central nervous system. Phosphorylation is a key post-translational modification regulating PR activity, influencing ligand binding, nuclear localization, and transcriptional activation. Ser190 phosphorylation, located in the PR’s N-terminal domain, is associated with receptor activation and downstream signaling. Studies suggest this modification enhances PR interaction with co-regulators and promotes target gene expression, impacting processes like cell proliferation, differentiation, and apoptosis.
The antibody is widely used in research to investigate PR signaling dynamics in hormone-responsive cancers, such as breast and endometrial cancers, where dysregulated PR phosphorylation may contribute to disease progression or therapy resistance. It enables detection of phosphorylated PR in techniques like Western blotting, immunohistochemistry, and immunofluorescence, aiding in the study of hormonal regulation, drug responses, and biomarker discovery. Understanding PR phosphorylation at Ser190 provides insights into progesterone signaling mechanisms and potential therapeutic targets, particularly in contexts of endocrine resistance or reproductive disorders. Proper validation, including knockout controls and peptide competition assays, ensures specificity in experimental models.