EGF Receptor 661-681 is a peptide fragment corresponding to a regulatory region within EGFR's cytoplasmic domain. Acidic and hydrophobic residues shape its role in protein-protein interactions and conformational transitions. Researchers use it to study signaling-motif binding and phosphorylation-dependent regulation. Applications include receptor-mapping studies, peptide-protein docking, and signaling-mechanism research.
CAT No: R2759
Synonyms/Alias:LYS-ARG-GLU-LEU-VAL-GLU-PRO-LEU-THR-PRO-SER-GLY-GLU-ALA-PRO-ASN-GLN-ALA-LEU-LEU-ARG;MAPKINASEPHOSPHORYLATIONSUBSTRATE;KRELVEPLTPSGEAPNQALLR-NH2;H-LYS-ARG-GLU-LEU-VChemicalbookAL-GLU-PRO-LEU-THR-PRO-SER-GLY-GLU-ALA-PRO-ASN-GLN-ALA-LEU-LEU-ARG-NH2;EGFRECEPTOR661-681;EGFRECEPTOR661-681[KRELVEPLTPSGEAPNQALLR-NH2];EGFRECEPTORSEQUENCE(661-681)
EGF Receptor 661-681 is a synthetic peptide fragment corresponding to residues 661 through 681 of the human epidermal growth factor receptor (EGFR). As a segment derived from the intracellular domain of EGFR, this peptide encompasses a region implicated in signal transduction, protein-protein interactions, and post-translational modifications. The sequence is of particular interest to researchers investigating the molecular mechanisms of receptor tyrosine kinases, cellular signaling cascades, and the structural biology of membrane-associated proteins. Its defined length and well-characterized origin make it a valuable tool for dissecting the functional domains of EGFR and exploring the biochemical events that regulate receptor activity in normal and pathological states.
Signal Transduction Studies: The peptide fragment is widely used in the analysis of EGFR-mediated signaling pathways. By serving as a substrate or competitive inhibitor in kinase assays, it enables the detailed examination of phosphorylation events within the receptor's cytoplasmic domain. Researchers utilize this sequence to map specific phosphorylation sites, study the kinetics of tyrosine kinase activity, and elucidate downstream signaling events that are fundamental to cell proliferation and differentiation.
Protein-Protein Interaction Analysis: EGF Receptor 661-681 provides a model system for investigating interactions between EGFR and intracellular adaptor proteins or effectors. Its defined sequence allows for precise mapping of binding motifs involved in the recruitment of signaling partners such as SH2 or PTB domain-containing proteins. Experimental approaches including pull-down assays, surface plasmon resonance, and co-immunoprecipitation often employ this peptide to characterize the selectivity and affinity of protein-protein contacts central to EGFR function.
Phosphorylation Site Characterization: As a representative segment containing potential phosphorylation sites, the peptide is instrumental in studies focused on post-translational modification. Researchers use it to identify and validate tyrosine residues targeted by EGFR's intrinsic kinase activity or by associated kinases. This approach facilitates the development of phospho-specific antibodies and supports mass spectrometry-based proteomic analyses, advancing the understanding of regulatory mechanisms that control receptor activation and signal propagation.
Structural Biology and Modeling: The defined sequence of this EGFR-derived peptide supports structural investigations aimed at elucidating conformational changes upon phosphorylation or binding to regulatory proteins. Through techniques such as NMR spectroscopy, X-ray crystallography, or computational modeling, scientists employ the peptide to resolve atomic-level details that inform on the dynamics and structural determinants of EGFR signaling regions. These insights are crucial for rational drug design and the development of molecular probes targeting EGFR-related pathways.
Peptide-Based Assay Development: The synthetic peptide is also utilized in the development and optimization of biochemical assays for EGFR activity and inhibition. Its application extends to high-throughput screening platforms where it serves as a standard substrate for evaluating kinase inhibitors, validating assay sensitivity, and benchmarking experimental conditions. The reproducible nature and specificity of the peptide sequence make it an essential reagent for assay standardization in both academic research and pharmaceutical development settings.
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