EGFR Protein Tyrosine Kinase Substrate [ADEYLIPQQ]

Product Name: EGFR Protein Tyrosine Kinase Substrate [ADEYLIPQQ]

Sequence One Letter Code: ADEYLIPQQ

Sequence Three Letter Code: H-Ala-Asp-Glu-Tyr-Leu-Ile-Pro-Gln-Gln-OH

Chemical Formula:C48H73N11O17

Molecular Weight: 1076.2

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Cancer Disease Research

Source / Species: Human, mouse, rat

Conjugation: Unconjugated

Code Nacres: NA.26

Application: EGFR Protein Tyrosine Kinase Substrate is a synthetic peptide with the sequence ADEYLIPQQ, designed for enzymatic analysis of epidermal growth factor receptor (EGFR) activity. The peptide contains a central tyrosine residue that serves as the phosphorylation site specifically recognized by EGFR tyrosine kinase. It is commonly applied in in vitro kinase assays to quantify catalytic activity, determine kinetic parameters, and compare functional differences among EGFR variants. This substrate is also suitable for evaluating the potency and selectivity of small-molecule EGFR inhibitors. Because EGFR signaling regulates cell proliferation, differentiation, survival, and migration, accurate assessment of its kinase activity is critical in cancer biology research. The peptide supports mechanistic investigations into aberrant EGFR activation and therapeutic resistance, providing a reliable biochemical tool for drug discovery programs targeting EGFR-driven malignancies and dysregulated receptor tyrosine kinase signaling pathways.

Current Research: EGFR Protein Tyrosine Kinase Substrate is a synthetic peptide with the sequence ADEYLIPQQ, specifically designed for biochemical evaluation of epidermal growth factor receptor (EGFR) kinase activity. The peptide incorporates a centrally positioned tyrosine residue that serves as the phosphorylation site selectively recognized by the EGFR tyrosine kinase domain. Its defined and minimal structure enables direct, quantitative assessment of catalytic activity in controlled in vitro assay systems. EGFR is a receptor tyrosine kinase that plays a pivotal role in regulating cell proliferation, differentiation, survival, and migration. Upon ligand binding and receptor dimerization, the intracellular kinase domain becomes activated, leading to autophosphorylation and downstream signaling through pathways such as MAPK/ERK, PI3K/AKT, and JAK/STAT. Dysregulated EGFR signaling—through overexpression, mutation, or constitutive activation—is a hallmark of multiple malignancies, including non-small cell lung cancer, colorectal cancer, and glioblastoma. As a result, accurate measurement of EGFR kinase activity remains central to cancer biology research and targeted drug development. The ADEYLIPQQ peptide substrate provides a streamlined platform for enzymatic analysis of EGFR function. In vitro kinase assays utilizing this substrate enable precise quantification of tyrosine phosphorylation, typically through radiometric detection, antibody-based phosphotyrosine recognition, or fluorescence-coupled methods. Because the sequence is short and structurally uncomplicated, phosphorylation reflects intrinsic catalytic efficiency rather than confounding regulatory interactions present in full-length protein substrates. This substrate is widely employed for determination of key kinetic parameters, including Km and Vmax, facilitating detailed enzymatic characterization of wild-type and mutant EGFR variants. Comparative studies using this peptide allow researchers to evaluate how clinically relevant mutations—such as those affecting the ATP-binding pocket or activation loop—alter catalytic turnover and substrate affinity. These analyses are essential for understanding oncogenic activation mechanisms and predicting therapeutic response. In addition to fundamental enzymology, the EGFR Protein Tyrosine Kinase Substrate supports pharmacological profiling of small-molecule inhibitors. Competitive inhibitors targeting the ATP-binding site or allosteric modulators affecting kinase conformation can be evaluated using peptide-based phosphorylation assays. By measuring changes in phosphorylation rates in the presence of candidate compounds, researchers can determine inhibitory potency, mechanism of action, and selectivity profiles. This makes the substrate particularly valuable in preclinical drug discovery programs focused on EGFR-driven tumors. The peptide is also suitable for assessing resistance-associated EGFR mutations that emerge during targeted therapy. Secondary mutations can reduce inhibitor binding while preserving kinase activity, leading to treatment failure. Using a standardized substrate such as ADEYLIPQQ allows direct comparison of inhibitor efficacy across mutant variants under consistent assay conditions, supporting rational design of next-generation therapeutics. Beyond oncology, EGFR signaling contributes to tissue repair, epithelial homeostasis, and inflammatory responses. Quantitative evaluation of EGFR kinase activity using defined peptide substrates enhances mechanistic studies of receptor regulation, signal amplitude control, and pathway cross-talk with other receptor tyrosine kinases. Overall, EGFR Protein Tyrosine Kinase Substrate (ADEYLIPQQ) provides a reliable and efficient biochemical tool for enzymatic analysis of EGFR activity. Its specific phosphorylation site, compatibility with diverse detection platforms, and suitability for kinetic and inhibitor studies make it a foundational reagent in cancer research and targeted therapy development. By enabling precise measurement of EGFR catalytic function, this peptide supports deeper investigation into aberrant receptor signaling and therapeutic intervention strategies.