EDDR1 (867-876)

EDDR1 (867-876) is a synthetic peptide corresponding to amino acid residues 867 to 876 of the Epithelial Discoidin Domain Receptor 1 (EDDR1) protein sequence. As a peptide fragment derived from the intracellular region of EDDR1, it serves as a valuable molecular tool for dissecting the structure-function relationships of this receptor tyrosine kinase, which is implicated in cell adhesion, migration, and extracellular matrix interactions. Its defined sequence and biochemical stability make it particularly relevant for researchers investigating receptor signaling, protein-protein interactions, and downstream effector pathways associated with EDDR1 activity.

Peptide mapping: EDDR1 (867-876) is commonly employed as a reference standard in peptide mapping experiments aimed at characterizing the post-translational modifications and sequence integrity of EDDR1 and related proteins. By serving as a well-defined sequence fragment, it enables mass spectrometry-based identification and quantification of specific receptor domains, supporting high-resolution proteomic analyses and facilitating the validation of protein expression or modification states in cell-based or in vitro systems.

Protein-protein interaction studies: As a synthetic peptide mimicking a specific segment of EDDR1, this compound is instrumental in probing the molecular determinants of receptor interactions with intracellular partners. Researchers utilize it in binding assays, pull-down experiments, and competition studies to elucidate the binding preferences and affinities of EDDR1 for downstream signaling molecules, adaptor proteins, or regulatory factors, thereby advancing the mechanistic understanding of receptor-mediated signal transduction.

Antibody production and epitope mapping: The defined sequence of EDDR1 (867-876) makes it an ideal immunogen or epitope for generating sequence-specific antibodies against the C-terminal region of EDDR1. These antibodies are valuable for use in immunoblotting, immunoprecipitation, and immunofluorescence assays aimed at detecting endogenous or recombinant EDDR1, as well as for mapping antibody binding sites to support the development of novel research reagents or diagnostic tools.

Kinase substrate assays: The peptide's origin from a receptor tyrosine kinase domain positions it as a suitable substrate in in vitro kinase assays. Researchers can employ EDDR1 (867-876) to assess the phosphorylation activity of EDDR1 or related kinases, enabling the investigation of kinase specificity, inhibitor screening, and the functional consequences of phosphorylation events within this critical signaling region.

Structural and functional peptide studies: The defined length and sequence of EDDR1 (867-876) facilitate its use in structural biology applications, including nuclear magnetic resonance (NMR) spectroscopy and circular dichroism (CD) analysis. These studies provide insights into the conformational properties of EDDR1's intracellular domains and their potential roles in mediating receptor function, interaction dynamics, and cellular localization, supporting the rational design of peptide-based modulators or structural mimetics for advanced research applications.

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