Phospho-Insulin Receptor β (Tyr1150/1151) Recombinant Rabbit mAb (S-4079-65)

Phospho-Insulin Receptor β (Tyr1150/1151) refers to the activated form of the insulin receptor beta subunit that has been specifically phosphorylated at tyrosine residues 1150 and 1151 within the kinase domain's activation loop, a critical post-translational modification that serves as a definitive biomarker for insulin receptor catalytic activity and downstream signal transduction. Upon insulin binding to the extracellular alpha subunits, the intrinsic tyrosine kinase activity of the beta subunit is triggered, leading to autophosphorylation at these specific sites which induces a conformational change that fully activates the kinase, thereby enabling the recruitment and phosphorylation of insulin receptor substrates (IRS) and initiating the PI3K-Akt and MAPK signaling cascades essential for glucose uptake, glycogen synthesis, and cell growth. Detection of this specific phospho-epitope using site-specific antibodies is widely utilized in biomedical research and drug discovery to assess insulin sensitivity, evaluate the efficacy of insulin mimetics or kinase inhibitors, and investigate the molecular pathophysiology of metabolic disorders such as type 2 diabetes and insulin resistance syndromes where impaired phosphorylation at Tyr1150/1151 directly correlates with defective insulin signaling.