Ftisadtsk is a short peptide rich in polar and charged residues that contribute to flexible secondary-structure formation. Researchers employ it to evaluate phosphorylation motifs, residue-specific effects, and solvent-dependent conformational shifts. The sequence supports analysis of peptide-protein interfaces and hydrogen-bonding behavior. Its compact structure provides high analytical versatility.
CAT No: R2268
CAS No:1431957-73-1
Synonyms/Alias:FTISADTSK;1431957-73-1;HY-P3146;AKOS040756800;CS-0149482;(2S)-6-amino-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S,3R)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-3-hydroxybutanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]propanoyl]amino]-3-carboxypropanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]hexanoic acid;
Ftisadtsk is a synthetic peptide compound characterized by its specific amino acid sequence, which confers unique biochemical properties and functional relevance in peptide research. As a custom-designed peptide, it serves as a valuable tool for probing protein interactions, studying structure-activity relationships, and supporting the development of novel biochemical assays. Its defined sequence allows for precise manipulation in experimental systems, making it particularly suitable for applications in molecular biology, biochemistry, and related life science disciplines. The versatility and specificity of this peptide enable its integration into a wide range of research workflows where controlled peptide interactions and modifications are required.
Peptide-protein interaction studies: In molecular and cellular research, synthetic peptides like Ftisadtsk are frequently employed to investigate the binding affinities and interaction dynamics between peptides and target proteins. By incorporating this sequence into binding assays, researchers can elucidate the molecular determinants that govern recognition, specificity, and complex formation. Such studies are fundamental for mapping protein interaction networks, validating potential drug targets, and understanding the structural basis of biological processes at the molecular level.
Enzyme substrate characterization: The defined structure of this peptide makes it an excellent substrate candidate for enzymatic assays, particularly for proteases or peptidases with specificity for certain residues or motifs. By serving as a model substrate, it facilitates the assessment of enzyme activity, kinetic parameters, and substrate preferences. These insights are crucial for enzyme mechanism studies, inhibitor screening, and the development of high-throughput biochemical assays aimed at characterizing enzyme specificity.
Epitope mapping and antibody validation: The unique sequence of Ftisadtsk enables its use in immunological assays for epitope mapping and antibody specificity testing. By synthesizing this peptide and incorporating it into ELISA, western blot, or immunoprecipitation formats, researchers can precisely identify antibody binding sites and validate antibody selectivity. This application is especially valuable in the development and quality control of monoclonal antibodies, as well as in the refinement of diagnostic reagents.
Peptide modification and conjugation research: Due to its well-defined sequence, this compound serves as an ideal scaffold for chemical modification studies, including the introduction of functional groups, fluorescent labels, or affinity tags. Such modifications enable the exploration of structure-function relationships, facilitate detection or purification workflows, and support the creation of multifunctional peptide conjugates. These approaches are instrumental in advancing chemical biology, drug discovery, and bioanalytical method development.
Cell signaling and functional assays: The synthetic peptide can be utilized in cell-based assays to probe signaling pathways, receptor activation, or cellular uptake mechanisms. By applying the peptide to cultured cells or in vitro systems, researchers can monitor downstream effects, assess bioactivity, and dissect the molecular mechanisms underlying peptide-mediated responses. This application supports the elucidation of cellular signaling networks and the identification of novel modulators within complex biological systems.
4. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
5. Myotropic activity of allatostatins in tenebrionid beetles
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