Insulin Receptor (1142-1153), pTyr1146

TRDI-pY-ETDYYRK corresponds to residues 1142-1153 of the insulin receptor beta-subunit kinase domain with phosphorylation installed at Tyr1146. This regulatory segment contains the clustered activation-loop tyrosines of the insulin receptor. The singly phosphorylated peptide is useful as a defined phosphotyrosine standard and as a substrate for phosphatase studies, including analytical workflows that distinguish different phosphorylation states of the insulin-receptor activation loop.

• phosphotyrosine peptide standards
• insulin-receptor signaling studies
• protein tyrosine phosphatase assays
• LC-MS phosphopeptide method development

This material already contains phosphotyrosine at Tyr1146. It should therefore be positioned as a defined phosphorylation-state reference or phosphatase substrate rather than as an unphosphorylated kinase phosphate-acceptor peptide.

1. Direct MALDI-MS/MS of Phosphopeptides Affinity-Bound to Immobilized Metal Ion Affinity Chromatography Beads
2. Evaluation of Quantitative Performance of Sequential Immobilized Metal Affinity Chromatographic Enrichment for Phosphopeptides