The Phospho-Glucocorticoid Receptor (Ser226) antibody is a specialized tool used to detect glucocorticoid receptor (GR) phosphorylated at serine residue 226. a post-translational modification critical for regulating GR activity. The glucocorticoid receptor, a member of the nuclear receptor superfamily, mediates the effects of glucocorticoid hormones, influencing metabolism, immune response, and stress adaptation. Upon ligand binding, GR translocates to the nucleus, where it modulates gene expression by binding glucocorticoid response elements or interacting with transcription factors. Phosphorylation at specific residues, including Ser226. fine-tunes GR transcriptional activity, cellular localization, and protein-protein interactions. Ser226 phosphorylation has been linked to altered receptor function, including reduced transactivation potential and changes in nuclear-cytoplasmic shuttling. This antibody enables researchers to study GR activation dynamics in conditions like inflammation, cancer, or metabolic disorders, where dysregulated glucocorticoid signaling is implicated. It is commonly employed in techniques such as Western blotting, immunofluorescence, or immunoprecipitation to investigate cell signaling pathways, receptor trafficking, or drug effects. Understanding Ser226 phosphorylation provides insights into GR regulatory mechanisms and their pathological or therapeutic relevance.