Receptor tyrosine-protein kinase erbB-2 (952-961)

Receptor tyrosine-protein kinase erbB-2 (952-961) is a synthetic peptide fragment derived from the intracellular domain of the human HER2/neu receptor, a member of the epidermal growth factor receptor (EGFR) family. This nonapeptide encompasses amino acid residues 952 to 961, a region implicated in signal transduction and protein-protein interactions within cellular pathways that regulate proliferation and differentiation. As a research tool, this peptide offers valuable insights into HER2-mediated signaling mechanisms, making it a significant resource for studies focused on cancer biology, receptor phosphorylation, and downstream effector pathways.

Signal transduction research: The peptide corresponding to residues 952-961 of erbB-2 is frequently utilized in studies investigating the molecular details of HER2 signaling. By serving as a defined substrate or competitor in kinase assays, it enables researchers to dissect phosphorylation events and to characterize the specificity of kinases or phosphatases that interact with this region. Such studies are fundamental for mapping the functional domains responsible for HER2-driven oncogenic signaling and for identifying regulatory checkpoints within the pathway.

Protein-protein interaction mapping: The 952-961 sequence of HER2 is involved in mediating interactions with various intracellular adaptor proteins and signaling effectors. Synthetic peptides representing this region are employed in pull-down assays, surface plasmon resonance studies, and other biochemical binding experiments to elucidate the binding partners and interaction affinities of the HER2 cytoplasmic tail. These applications are critical for understanding the assembly of signaling complexes and for identifying novel modulators of HER2 function.

Antibody epitope characterization: Researchers use the erbB-2 (952-961) peptide as a defined antigenic target to map antibody binding sites and to evaluate the specificity of monoclonal or polyclonal antibodies directed against HER2 intracellular domains. Such applications are essential for the development and validation of immunoassays, as well as for the quality control of antibody reagents used in research and diagnostic settings.

Peptide-based assay development: The defined sequence of this peptide lends itself to the development of various in vitro assays, including enzyme-linked immunosorbent assays (ELISAs) and mass spectrometry-based detection platforms. By incorporating the peptide as a calibrator, standard, or capture reagent, assay developers can achieve precise quantitation of HER2-related activity or presence in complex biological samples, thereby enhancing the reliability and reproducibility of experimental results.

Phosphorylation site analysis: The erbB-2 (952-961) peptide serves as a model substrate for characterizing phosphorylation patterns mediated by HER2 or associated kinases. By employing this peptide in in vitro phosphorylation reactions, researchers can pinpoint specific residues subject to post-translational modification and assess the impact of sequence context on kinase activity. This application is fundamental for delineating the functional consequences of HER2 phosphorylation and for guiding the design of targeted inhibitors or modulators in signal transduction research.

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