Vimentin (226-234)

Vimentin (226-234) is a synthetic peptide fragment corresponding to amino acid residues 226 through 234 of the intermediate filament protein vimentin. As a highly conserved cytoskeletal component, vimentin plays a crucial role in maintaining cellular architecture, supporting organelle positioning, and facilitating various dynamic processes such as migration and division in mesenchymal cells. The 226-234 region represents a functionally significant epitope within the vimentin molecule, making this peptide a valuable tool for research into cytoskeletal dynamics, protein-protein interactions, and post-translational modifications. Its defined sequence and biochemical properties enable precise interrogation of vimentin's structural and regulatory roles in cellular systems.

Epitope mapping: The vimentin (226-234) peptide is widely utilized in epitope mapping studies to identify antibody binding sites and characterize immune recognition patterns. By serving as a defined antigenic determinant, this peptide allows researchers to dissect the specificity of monoclonal and polyclonal antibodies raised against vimentin. Such investigations are essential for developing reliable immunodetection assays, generating high-affinity reagents for cell biology, and advancing our understanding of autoimmune responses where vimentin is implicated as an autoantigen.

Protein-protein interaction analysis: As a segment of the vimentin rod domain, the 226-234 peptide can be employed to investigate binding interactions with regulatory proteins, small molecules, or cytoskeletal partners. In vitro binding assays and pull-down experiments using this peptide facilitate the identification of interaction motifs and the elucidation of mechanisms underlying vimentin's role in signaling pathways, cytoskeletal reorganization, and cellular stress responses. These studies contribute to a deeper mechanistic understanding of intermediate filament dynamics in both physiological and pathological contexts.

Phosphorylation and post-translational modification studies: The defined amino acid sequence of vimentin (226-234) provides an ideal substrate for examining phosphorylation events and other post-translational modifications that modulate vimentin function. Researchers can use the peptide in kinase assays to assess site-specific phosphorylation, screen for modifying enzymes, or develop phospho-specific antibodies. Such applications are critical for unraveling how post-translational changes influence vimentin assembly, disassembly, and its integration into broader cellular signaling networks.

Peptide-based assay development: The vimentin (226-234) fragment serves as a standard or competitor in a variety of peptide-based biochemical assays. Its application spans ELISA, competitive binding assays, and mass spectrometry calibration, where it enables the quantification of vimentin or vimentin-derived peptides in complex samples. This functionality supports the development of robust analytical platforms for studying cytoskeletal protein expression, turnover, and fragmentation under different experimental conditions.

Cell signaling research: The 226-234 peptide is also utilized as a molecular probe to interrogate cell signaling pathways in which vimentin is a key mediator. By introducing the peptide into cultured cells or cell-free systems, researchers can assess its impact on filament assembly, intracellular localization, or downstream effector activation. These experiments provide valuable insights into how specific vimentin domains contribute to cellular adaptation, migration, and response to environmental cues, furthering our understanding of the cytoskeleton's regulatory landscape.

1. Peptides as Active Ingredients: A Challenge for Cosmeceutical Industry

2. A possible role of tachykinin-related peptide on an immune system activity of mealworm beetle, Tenebrio molitor L

3. Genetic, cellular, and structural characterization of the membrane potential-dependent cell-penetrating peptide translocation pore

4. The effect of sex on immune responses to a homocitrullinated peptide in the DR4-transgenic mouse model of Rheumatoid Arthritis

5. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs