Phospho-Estrogen Receptor α (Ser118) Rabbit mAb

Phospho-Estrogen Receptor α (Ser118) Rabbit mAb detects endogenous levels of estrogen receptor α only when phosphorylated at serine 118.

Phospho-Estrogen Receptor α (Ser118)  (ERα) is a ligand-activated nuclear hormone receptor that mediates estrogen signaling by regulating transcription of estrogen-responsive genes. Structurally, ERα comprises a modular architecture with an intrinsically disordered N-terminal domain (NTD) containing Ser118, a central DNA-binding domain, and a C-terminal ligand-binding domain. It is abundantly expressed in estrogen-responsive tissues, particularly in breast epithelium and many breast cancers. Phosphorylation at Ser118—triggered by estrogen (E2), growth factors (via MAPK), or selective modulators—induces conformational changes in the NTD that modulate protein-protein and DNA interactions. This site-specific phosphorylation is critical for gene-specific recruitment of ERα and transcriptional coregulators, thereby determining differential gene expression outcomes and highlighting its essential role in fine-tuning estrogen-mediated transcriptional responses.