Keratin 18 (272-283)

Keratin 18 (272-283) is a synthetic peptide fragment derived from the intermediate filament protein Keratin 18, specifically corresponding to amino acid residues 272 through 283 of the parent sequence. As a member of the type I cytokeratin family, Keratin 18 is predominantly expressed in simple epithelial tissues and plays a vital role in maintaining cytoskeletal integrity and cellular architecture. The 272-283 peptide segment is of particular interest due to its involvement in the structural and functional domains of the protein, making it a valuable tool for researchers investigating cytoskeletal organization, cell signaling, and epithelial cell biology. Its defined sequence and biochemical properties enable precise experimental manipulation, supporting a wide range of studies in molecular and cellular research.

Epitope mapping: The 272-283 region of Keratin 18 is frequently utilized in epitope mapping studies to characterize antibody specificity and binding affinity. By employing this synthetic peptide in immunoassays, researchers can identify and validate monoclonal or polyclonal antibodies targeting Keratin 18, facilitating the development of reliable detection tools for basic research or diagnostic assay design. The defined sequence allows for controlled assessment of antibody-peptide interactions, supporting the optimization of immunological reagents.

Cell signaling research: This peptide segment serves as a model substrate in studies exploring post-translational modifications, such as phosphorylation or proteolytic cleavage, that regulate Keratin 18 function. By incorporating the 272-283 fragment in kinase assays or protease activity screens, investigators can dissect specific signaling pathways that modulate cytoskeletal dynamics in epithelial cells. The peptide's defined length and composition enable detailed mechanistic analysis of modification sites and their functional consequences.

Protein-protein interaction analysis: The Keratin 18 (272-283) peptide is a valuable probe for examining protein-protein interactions involving the intermediate filament network. It can be applied in pull-down assays, surface plasmon resonance, or other biophysical methods to investigate binding partners that recognize or interact with this specific region. Such studies provide insights into the molecular mechanisms underlying cytoskeletal organization, cell junction formation, and epithelial tissue stability.

Peptide-based assay development: The defined sequence and biochemical stability of this peptide make it suitable for the development and validation of peptide-based assays. It can be incorporated into ELISA platforms, competitive binding assays, or biosensor applications to quantitatively measure antibody responses, enzymatic activity, or small molecule interactions. The use of synthetic peptides such as this one enables high specificity and reproducibility in assay design, supporting both basic and applied research objectives.

Structural and functional studies: The 272-283 segment of Keratin 18 is often employed in structural biology to elucidate the conformational properties of intermediate filament proteins. Researchers may use the peptide in spectroscopic analyses or crystallographic experiments to investigate secondary structure elements, folding patterns, or molecular recognition motifs. These insights contribute to a deeper understanding of cytoskeletal protein architecture and the determinants of filament assembly and stability in epithelial cells.

1. Emerging applications of nanotechnology for diagnosis and therapy of disease: a review

2. Investigating Potential Interactions Between Neurohypophyseal Peptides, their Drug Analogs, and Coagulation Factor VIII

3. Spatiotemporal delivery of nanoformulated liraglutide for cardiac regeneration after myocardial infarction

4. Implications of ligand-receptor binding kinetics on GLP-1R signalling

5. Odorant binding protein based biomimetic sensors for detection of alcohols associated with Salmonella contamination in packaged beef