Anti-PGR (phospho S190) Antibody

Phosphorylation of the human progesterone receptor (PGR) at serine 190, located within the N-terminal transactivation domain, is a recognized marker of ligand-driven receptor activation and downstream transcriptional signaling. This unconjugated rabbit polyclonal IgG preparation from Antibodies.com is raised against the PGR phospho-S190 epitope and is supplied as a 50 µl aliquot for western blot, immunohistochemistry, and immunofluorescence workflows on human samples.

The antibody detects the activated, phosphorylated form of the receptor rather than total PGR expression, supporting studies that examine progestin-induced signaling, nuclear translocation, and isoform-specific responses in breast cancer cell models and reproductive tissue research. Researchers comparing phospho-S190 status across PR-A and PR-B isoform contexts, or probing ligand-dependent versus ligand-independent activation pathways, can apply the reagent to formalin-fixed paraffin-embedded tissue sections for IHC, to cultured cell lysates for WB, and to fixed cells for IF imaging of receptor localization.

As an unconjugated primary antibody, the reagent pairs with common secondary detection chemistries, including HRP, fluorescent, and biotinylated systems, giving flexibility across experimental designs. Researchers should follow the storage and handling recommendations provided with the vial to preserve phospho-specific binding activity over the working shelf life of the reagent.