Platelet Factor 4 (58-70), human, a peptide based on the amino acid sequence corresponding to residues 58-70 of platelet factor-4 (PF-4), contains the major heparin-binding domain, which is not sufficient for full antiangiogenic activity.
CAT No: R1621
CAS No:82989-21-7
Synonyms/Alias:82989-21-7;Platelet Factor 4 (58-70), human;IPF-4305-V;Platelet Factor-4 (Human, 58-70);DA-56923;Pro-Leu-Tyr-Lys-Lys-Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser;
Platelet Factor 4 (58-70), human is a synthetic peptide fragment corresponding to amino acids 58 through 70 of the human Platelet Factor 4 protein. As a cationic, chemokine-derived peptide, it has garnered significant interest in biochemical and biomedical research due to its involvement in modulating various cellular processes, including coagulation, inflammation, and immune cell signaling. The sequence-specific characteristics of this peptide fragment make it a valuable tool for dissecting structure-activity relationships within the broader context of platelet-derived chemokines, as well as for investigating the functional domains critical to Platelet Factor 4's biological activity.
Peptide structure-function analysis: Researchers frequently employ this peptide to study the structure-function relationships of Platelet Factor 4 and its derived fragments. By isolating the 58-70 region, scientists can examine the contribution of this specific sequence to the protein's overall bioactivity, receptor binding, and interactions with glycosaminoglycans. Such investigations are essential for mapping the domains responsible for chemokine activity, enabling a deeper understanding of how subtle sequence variations influence biological function.
Protein-protein interaction studies: The 58-70 fragment is widely used in assays designed to elucidate the molecular mechanisms underlying Platelet Factor 4's interactions with other proteins, including those involved in coagulation and immune modulation. Its defined sequence allows for precise mapping of binding interfaces and competitive inhibition experiments, which are instrumental in characterizing the specificity and affinity of interactions with target molecules such as heparin, chondroitin sulfate, or cell surface receptors.
Antibody epitope mapping: The synthetic peptide is a valuable reagent for identifying and characterizing antibody binding sites within the Platelet Factor 4 molecule. By serving as an antigenic determinant, it enables the development and validation of immunoassays, as well as the generation of sequence-specific antibodies. These applications are particularly relevant in the context of heparin-induced thrombocytopenia research, where understanding epitope specificity is crucial for both basic and applied studies.
Cell signaling and chemotaxis research: The defined region represented by this peptide fragment is implicated in modulating cell signaling pathways and chemotactic responses. Researchers utilize it to probe the signaling cascades activated by Platelet Factor 4, particularly in studies involving endothelial cells, leukocytes, and other immune cell populations. Such work advances the understanding of how specific chemokine domains contribute to inflammatory processes and cellular migration, supporting the development of targeted experimental models.
Peptide-based assay development: The unique biochemical properties of the 58-70 fragment make it a useful standard or control in a variety of in vitro assays. Its application extends to the calibration of analytical techniques, such as mass spectrometry, high-performance liquid chromatography, and immunodetection platforms, where it provides a reliable reference for quantifying peptide-protein interactions, post-translational modifications, or degradation kinetics. This versatility underpins its value in both fundamental research and the optimization of assay methodologies targeting chemokine activity.
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