Vimentin (402-413)

Vimentin (402-413) is a synthetic peptide fragment derived from the intermediate filament protein vimentin, specifically encompassing amino acid residues 402 to 413. As a highly conserved cytoskeletal component, vimentin plays a pivotal role in maintaining cellular integrity, supporting organelle positioning, and regulating cell signaling pathways. The 402-413 sequence is of particular interest due to its involvement in protein-protein interactions and potential post-translational modification sites, making it a valuable tool for dissecting vimentin's structural and functional properties in various cellular contexts. Researchers utilize this peptide to explore fundamental aspects of cell biology, cytoskeletal dynamics, and signal transduction, providing insights into the broader roles of intermediate filaments in physiological and pathological processes.

Peptide mapping: The 402-413 fragment serves as a critical tool for peptide mapping studies aimed at elucidating the structural organization and domain-specific functions of vimentin. By employing this sequence in mass spectrometry-based proteomics or immunological assays, scientists can identify and characterize specific interaction sites, post-translational modifications, or cleavage events within the vimentin molecule. Such investigations contribute to a detailed understanding of how structural motifs within intermediate filaments govern their assembly, stability, and cellular localization.

Antibody epitope characterization: The defined sequence of vimentin (402-413) provides a unique epitope for the generation and validation of sequence-specific antibodies. Researchers use the synthetic peptide to immunize animals or screen pre-existing antibodies, thereby producing reagents capable of selectively detecting vimentin or its fragments in diverse biological samples. These antibodies are instrumental in immunoblotting, immunofluorescence, and immunoprecipitation experiments designed to monitor vimentin expression, distribution, and post-translational modifications under various experimental conditions.

Protein interaction studies: The 402-413 peptide is frequently employed in binding assays to investigate direct and competitive interactions between vimentin and its cellular partners. By introducing this fragment in vitro, researchers can assess its capacity to disrupt or mimic native protein-protein interactions, advancing the mechanistic understanding of how vimentin participates in signaling pathways, cytoskeletal remodeling, and cellular response to stress. Such studies are essential for unraveling the molecular basis of intermediate filament dynamics and their integration with other cytoskeletal systems.

Phosphorylation analysis: The amino acid sequence encompassed by residues 402 to 413 of vimentin contains potential phosphorylation sites that are known to regulate filament assembly and disassembly. Synthetic peptides corresponding to this region are widely used as substrates in kinase assays or as reference standards in phosphoproteomic analyses. These applications enable the detailed examination of kinase specificity, phosphorylation kinetics, and the functional consequences of site-specific modification on vimentin's structural and regulatory roles within the cell.

Cell signaling research: By leveraging the defined sequence and biochemical properties of the 402-413 peptide, researchers can probe the involvement of vimentin in intracellular signaling cascades. The fragment can be utilized in cellular models to study its effects on downstream effector pathways, cytoskeletal organization, and cellular adaptation to environmental stimuli. Such investigations provide valuable insights into the broader impact of intermediate filament proteins on cell physiology, migration, and response to external cues, supporting a range of fundamental and applied research initiatives.

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