EGF-R (1138-1147)

EGF-R (1138-1147) is a synthetic peptide corresponding to amino acids 1138 to 1147 of the human Epidermal Growth Factor Receptor (EGFR) protein. This decapeptide segment is derived from the intracellular domain of EGFR, a transmembrane receptor tyrosine kinase that plays a pivotal role in cell signaling pathways regulating proliferation, differentiation, and survival. The EGF-R (1138-1147) peptide is of considerable interest in biochemical and molecular biology research, particularly in studies focused on receptor phosphorylation, protein-protein interactions, and signal transduction mechanisms. Its well-defined sequence and structural relevance make it a valuable tool for dissecting the functional aspects of EGFR-mediated cellular processes.

Phosphorylation studies: The EGF-R (1138-1147) peptide serves as a model substrate for investigating EGFR kinase activity and site-specific phosphorylation events. Researchers utilize this peptide in in vitro kinase assays to characterize the enzymatic properties of EGFR and related tyrosine kinases, enabling detailed analysis of phosphorylation kinetics, substrate specificity, and the effects of modulators or inhibitors. Such studies provide insight into the regulatory mechanisms governing EGFR signaling and its dysregulation in various biological contexts.

Protein interaction mapping: As a representative segment of the EGFR intracellular tail, this peptide is instrumental in mapping binding sites for SH2 domain-containing proteins and other downstream signaling effectors. By employing the peptide in binding assays, pull-down experiments, or surface plasmon resonance analyses, scientists can elucidate the molecular interactions that mediate signal propagation from activated EGFR, thereby advancing understanding of complex signaling networks and identifying potential regulatory nodes.

Antibody characterization: The defined sequence of EGF-R (1138-1147) is frequently used as an immunogen or as a standard in antibody validation protocols. Researchers rely on this peptide to assess the specificity and binding affinity of antibodies directed against the C-terminal region of EGFR, facilitating the development and quality control of research-grade antibodies. Accurate antibody characterization is essential for reliable detection and quantification of EGFR in biochemical assays, immunoblotting, or immunoprecipitation applications.

Peptide-based inhibitor screening: The EGF-R (1138-1147) peptide provides a strategic template for the rational design and screening of small molecule or peptide-based inhibitors targeting EGFR signaling. By incorporating this sequence into competitive binding or enzymatic inhibition assays, researchers can evaluate the efficacy of candidate compounds in modulating receptor activity or disrupting critical protein-protein interactions. This approach supports the identification of new chemical probes for basic research into EGFR function and regulation.

Analytical method development: The peptide is also utilized as a calibration standard or reference material in mass spectrometry-based proteomics and analytical chemistry workflows. Its defined molecular weight and sequence facilitate the optimization of peptide detection, quantification, and fragmentation protocols, contributing to the robustness and reproducibility of analytical methods used in protein characterization and post-translational modification studies.

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3. The spatiotemporal control of signalling and trafficking of the GLP-1R

4. The effect of sex on immune responses to a homocitrullinated peptide in the DR4-transgenic mouse model of Rheumatoid Arthritis

5. Tachykinin-related peptides modulate immune-gene expression in the mealworm beetle Tenebrio molitor L