Kinesin-like protein KIF20A
Kinesin-like protein KIF20A (284-293) is a synthetic peptide fragment derived from the motor domain of the KIF20A protein, a member of the kinesin superfamily involved in intracellular transport and mitotic processes. This defined peptide sequence represents a key region of the protein that is frequently studied for its role in microtubule-based motility and cell division. As a research tool, the peptide offers a focused approach to dissecting the molecular mechanisms underlying kinesin-mediated transport, mitotic spindle dynamics, and protein-protein interactions central to cell cycle regulation. Its specificity and well-characterized sequence make it a valuable reagent for probing the functional domains of KIF20A and related cellular pathways in biochemical and cell biology research.
Protein-protein interaction studies: Researchers utilize the KIF20A (284-293) peptide to investigate the interaction interfaces between kinesin motor proteins and their binding partners. By providing a discrete and accessible segment of the KIF20A protein, the peptide enables mapping of interaction sites through in vitro assays such as pull-down experiments, surface plasmon resonance, or co-immunoprecipitation. These studies contribute to a deeper understanding of how KIF20A associates with regulatory proteins, adaptors, or components of the mitotic apparatus, informing broader insights into mitotic progression and intracellular transport mechanisms.
Antibody production and epitope mapping: The defined sequence of this peptide makes it an ideal immunogen for generating sequence-specific antibodies against KIF20A. Polyclonal or monoclonal antibodies raised using the peptide as an antigen can be used for applications such as Western blotting, immunoprecipitation, or immunofluorescence, facilitating the detection and localization of endogenous KIF20A in various cell types. In addition, the peptide supports epitope mapping efforts, allowing researchers to pinpoint antibody binding sites and validate antibody specificity in functional studies.
Phosphorylation and post-translational modification analysis: As KIF20A is subject to regulatory phosphorylation during the cell cycle, the peptide corresponding to residues 284-293 serves as a substrate for in vitro kinase assays. Investigators can use the peptide to assess the activity of candidate kinases, identify modification sites, and characterize the functional consequences of phosphorylation within this region. Such studies are instrumental in elucidating the regulatory networks that control kinesin activity and mitotic fidelity.
Peptide-based inhibitor screening: The KIF20A (284-293) peptide is employed in assays designed to screen for small molecules or peptides that disrupt protein-protein interactions involving KIF20A. By mimicking a critical interaction motif, the peptide can be used as a competitive inhibitor or as a probe in high-throughput screening platforms to identify compounds that modulate kinesin function. This approach supports the discovery of novel modulators of mitotic kinesins, with potential applications in basic research and chemical biology.
Structural and biophysical studies: The defined nature of the peptide allows for detailed structural analysis using techniques such as NMR spectroscopy, X-ray crystallography, or circular dichroism. These studies provide insight into the conformational properties of the KIF20A motor domain segment and its interaction with binding partners or regulatory molecules. By elucidating the structural determinants of kinesin function, the peptide aids in advancing the molecular understanding of microtubule-based transport and mitotic regulation.
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