Insulin Receptor (1142-1153), pTyr1150

Product Name: Insulin Receptor (1142-1153), pTyr1150

Sequence One Letter Code: TRDIYETD-pY-YRK

Sequence Three Letter Code: H-Thr-Arg-Asp-Ile-Tyr-Glu-Thr-Asp-pTyr-Tyr-Arg-Lys-OH

Chemical Formula:C72H108N19O27P

Molecular Weight: 1702.8

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Diabetes and Metabolic Syndrome

Source / Species: Human, zebrafish, drosophila, mouse, rat, bovine

Conjugation: Unconjugated

Code Nacres: NA.26

Application: Insulin Receptor (1142–1153), pTyr1150 is a synthetic phosphotyrosine-containing peptide derived from the activation loop of the human insulin receptor β-subunit. Phosphorylation at Tyr1150 is critical for full tyrosine kinase activation and amplification of downstream insulin signaling cascades, including IRS recruitment and metabolic pathway regulation. This peptide serves as a defined substrate and reference standard in insulin receptor kinase assays, phosphotyrosine detection systems, and inhibitor screening platforms. It is particularly valuable for investigating insulin receptor autophosphorylation mechanisms, kinase activity quantification, and signaling dysfunction associated with insulin resistance and metabolic disease. The sequence supports reproducible biochemical studies focused on diabetes research, metabolic signaling pathways, and therapeutic target validation.

Current Research: Phosphorylation within the activation loop of the insulin receptor (IR) tyrosine kinase domain is a decisive molecular event governing receptor activation and downstream metabolic signaling. Tyr1150, together with Tyr1146 and Tyr1151, forms part of the tri-tyrosine regulatory cluster that stabilizes the catalytically competent conformation of the kinase. Structural and biochemical studies demonstrate that phosphorylation at Tyr1150 enhances ATP binding, promotes substrate access, and facilitates recruitment of adaptor proteins such as insulin receptor substrates (IRS-1/2), thereby amplifying PI3K–AKT and MAPK pathway activation. Current research continues to refine the understanding of stepwise IR autophosphorylation. Evidence indicates that activation loop phosphorylation occurs through ordered intermolecular and intramolecular events, with Tyr1150 playing a key role in relieving steric constraints that suppress kinase activity in the basal state. Defined phosphopeptides corresponding to individual activation loop residues, including IR (1142–1153), pTyr1150, are widely used to calibrate phosphotyrosine-specific antibodies, validate site-selective detection methods, and standardize quantitative kinase assays. These reagents enable precise dissection of residue-specific phosphorylation dynamics under physiological and pathophysiological conditions. In metabolic disease research, impaired insulin receptor autophosphorylation is strongly associated with insulin resistance in skeletal muscle, liver, and adipose tissue. Reduced phosphorylation at Tyr1150 has been observed in models of obesity, chronic inflammation, and lipotoxic stress, correlating with diminished IRS engagement and attenuated AKT activation. Synthetic activation loop phosphopeptides provide reproducible standards for comparing kinase activity in insulin-sensitive versus insulin-resistant states and for evaluating how genetic variants or post-translational modifications influence receptor function. Beyond metabolic regulation, dysregulated insulin and IGF-1 receptor signaling has emerged as a contributor to oncogenic growth and therapeutic resistance. As a structurally defined phosphomotif, the pTyr1150-containing peptide supports screening of small-molecule inhibitors targeting the kinase domain and characterization of SH2 domain–containing adaptor protein interactions. Competitive binding assays and in vitro kinase platforms frequently employ activation loop phosphopeptides to assess inhibitor potency, selectivity, and mechanism of action. Advances in phosphoproteomics and targeted mass spectrometry further highlight the need for well-characterized phosphopeptide standards. Site-specific peptides such as IR (1142–1153), pTyr1150 facilitate optimization of LC–MS/MS workflows, validation of phosphosite-specific antibodies, and development of quantitative assays for translational research. These approaches are increasingly applied to identify proximal signaling defects in prediabetes, type 2 diabetes, and metabolic syndrome. Collectively, current research underscores Tyr1150 phosphorylation as a critical determinant of insulin receptor catalytic activation and metabolic signal propagation. Insulin Receptor (1142–1153), pTyr1150 serves as a robust tool for mechanistic kinase studies, assay validation, inhibitor discovery, and detailed investigation of signaling alterations underlying insulin resistance and related metabolic disorders.