Receptor tyrosine-protein kinase erbB-2 (391-399)

Receptor tyrosine-protein kinase erbB-2 (391-399) is a synthetic peptide corresponding to amino acids 391 through 399 of the human HER2/neu (erbB-2) protein sequence. As a defined fragment of the extracellular domain of this receptor tyrosine kinase, it holds significant value in molecular and cellular research focused on signal transduction, protein-protein interactions, and the pathological roles of HER2/neu in various biological systems. The peptide's sequence specificity and structural fidelity make it a versatile tool for dissecting the functional properties of the erbB-2 receptor, facilitating advanced studies in oncology, immunology, and biochemical signaling pathways.

Epitope mapping: Researchers utilize this peptide fragment to precisely identify and characterize antibody binding sites within the HER2/neu extracellular domain. By serving as a defined epitope, the peptide enables the screening and validation of monoclonal and polyclonal antibodies, supporting the development of highly specific immunodetection reagents. This application is particularly valuable in studies aiming to elucidate the molecular determinants of antibody recognition and to optimize reagents for immunoassays or diagnostic platforms.

Peptide-based assay development: The erbB-2 (391-399) peptide is frequently incorporated into various in vitro assay systems, such as enzyme-linked immunosorbent assays (ELISA) and surface plasmon resonance (SPR) studies. Its defined sequence allows for the quantitative assessment of protein-ligand interactions, including the detection of autoantibodies or the evaluation of peptide affinity for candidate binding partners. These assays contribute to a deeper understanding of receptor-ligand dynamics and support the screening of potential modulators of HER2/neu function.

T-cell epitope studies: As a well-characterized fragment of the HER2/neu protein, this peptide is instrumental in immunological research investigating T-cell responses to tumor-associated antigens. It serves as a model antigen in studies of antigen processing and presentation, enabling the evaluation of MHC binding affinity and T-cell activation profiles. Such investigations are essential for elucidating mechanisms of immune recognition relevant to cancer immunology and vaccine research.

Protein interaction analysis: The defined sequence of the erbB-2 (391-399) peptide makes it a practical tool for mapping interaction domains within the HER2/neu receptor and its associated signaling partners. By using the peptide in pull-down assays, crosslinking experiments, or competitive binding studies, researchers can delineate the molecular interfaces that govern receptor dimerization, downstream signaling, or regulatory protein recruitment. This facilitates the identification of novel interaction motifs and enhances the mechanistic understanding of HER2/neu-mediated cellular processes.

Peptide synthesis and modification research: The erbB-2 (391-399) fragment also serves as a model substrate in peptide chemistry, supporting studies on synthetic strategies, post-translational modifications, and structure-activity relationships. Its well-defined sequence is particularly amenable to site-specific modifications, such as phosphorylation or conjugation, enabling the systematic evaluation of structural changes on biological activity or recognition by binding partners. This contributes to the optimization of peptide-based reagents and the development of novel research tools for molecular biology and biochemistry.

1. TMEM16F and dynamins control expansive plasma membrane reservoirs

2. Quantitative Analysis of Ligands Effects on Bioefficacy of Nanoemulsion encapsulating Depigmenting Active

3. Characterization of Novel P-Selectin Targeted Complement Inhibitors in Murine Models of Hindlimb Injury and Transplantation

4. Uncarboxylated osteocalcin decreases insulin-stimulated glucose uptake without affecting insulin signaling and regulators of mitochondrial biogenesis in myotubes

5. Relatedness of antibodies to peptides containing homocitrulline or citrulline in patients with rheumatoid arthritis