vimentin (177-185)

Vimentin (177-185) is a synthetic peptide fragment corresponding to amino acid residues 177 through 185 of the human vimentin protein, an intermediate filament protein critical for maintaining cellular integrity and cytoskeletal organization. As a short, well-defined segment of the vimentin sequence, this peptide serves as a precise molecular tool for probing protein-protein interactions, post-translational modifications, and the structural dynamics of intermediate filaments. Its biochemical relevance extends to studies of cytoskeletal regulation, cellular signaling, and the mechanisms underlying cell migration and morphology. The unique sequence of vimentin (177-185) enables researchers to investigate specific regions of the vimentin molecule, providing insight into its functional domains and their roles in cellular physiology.

Epitope mapping: The 177-185 fragment of vimentin is frequently utilized in epitope mapping experiments to identify and characterize antibody binding sites within the vimentin protein. By presenting this defined peptide segment, researchers can assess the specificity and affinity of monoclonal or polyclonal antibodies directed against vimentin, facilitating the development of reliable immunoassays. Such mapping is essential for the generation of diagnostic reagents, the validation of antibody-based detection methods, and the elucidation of immune recognition patterns in fundamental and applied research contexts.

Protein interaction studies: As a representative sequence from the central rod domain of vimentin, the peptide is instrumental in dissecting protein-protein interactions involved in cytoskeletal assembly and dynamics. It can be employed as a molecular probe in pull-down assays, surface plasmon resonance, or other biophysical techniques to investigate binding partners and regulatory proteins that associate with vimentin's rod domain. These studies contribute to a deeper understanding of cytoskeletal organization and the modulation of intermediate filament networks under physiological and stress conditions.

Phosphorylation and post-translational modification analysis: The vimentin (177-185) peptide is a valuable substrate for examining site-specific phosphorylation and other post-translational modifications. By serving as a model peptide in kinase assays or mass spectrometry-based studies, it enables researchers to pinpoint modification sites, analyze enzyme specificity, and assess the functional consequences of such modifications on filament assembly and cellular signaling pathways. This approach supports the broader investigation of cytoskeletal regulation through reversible protein modification.

Peptide-based inhibitor development: The defined sequence of vimentin (177-185) allows for its application in the design and screening of peptide-based inhibitors targeting vimentin-mediated interactions. By mimicking a functional domain of the full-length protein, the peptide can competitively interfere with endogenous protein interactions, providing a platform for evaluating the potential of peptide analogs as modulators of cytoskeletal dynamics in cell-based or in vitro assays. Such studies are important for advancing the understanding of vimentin's role in cellular processes and for the rational design of research tools.

Analytical assay calibration: The synthetic peptide is also employed as a standard or calibrator in analytical assays, including quantitative mass spectrometry and immunodetection techniques. Its defined composition and sequence specificity make it suitable for method development, assay validation, and quantitative analysis of vimentin-related peptides in complex biological samples. This application enhances the reliability and reproducibility of experimental results in proteomics and cell biology research.

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