Kinesin-like protein KIF20A
Kinesin-like protein KIF20A (809-817) is a synthetic peptide fragment derived from the motor protein KIF20A, a member of the kinesin superfamily involved in intracellular transport and mitotic spindle dynamics. As a well-characterized segment corresponding to amino acid residues 809 through 817, this peptide serves as a valuable tool for researchers investigating the molecular mechanisms of kinesin-mediated processes, protein-protein interactions, and cell division regulation. Its defined sequence enables precise interrogation of KIF20A's functional domains and their roles in cellular physiology, making it a critical reagent for studies focused on mitotic progression, motor protein biochemistry, and peptide-based assay development.
Epitope mapping: The KIF20A (809-817) peptide is widely utilized in epitope mapping experiments to identify antibody binding sites within the KIF20A protein. By providing a defined linear epitope, this peptide facilitates the characterization of monoclonal and polyclonal antibody specificity, supporting the development of research-grade antibodies for applications such as immunoblotting, immunoprecipitation, and immunofluorescence. Researchers can use it as a positive control or as a competitive inhibitor to validate antibody recognition, thereby enhancing the reliability of immunological assays targeting KIF20A.
Protein interaction studies: As a representative segment of KIF20A's functional region, the peptide is instrumental in probing protein-protein interactions that modulate kinesin activity. Synthetic peptides corresponding to specific motifs allow for in vitro binding assays, such as pull-down experiments or surface plasmon resonance, to elucidate the molecular partners and regulatory proteins that interact with KIF20A. Such studies contribute to a deeper understanding of the mechanisms governing mitotic spindle assembly, chromosome segregation, and intracellular transport dynamics.
Phosphorylation analysis: The defined sequence of the KIF20A (809-817) peptide can be employed as a substrate in kinase assays to investigate post-translational modifications, particularly phosphorylation events that regulate KIF20A function during cell cycle progression. By serving as a model substrate, the peptide enables detailed studies of site-specific phosphorylation by mitotic kinases, facilitating the identification of regulatory pathways and potential modulation points within the kinesin family. This approach aids in dissecting the signal transduction networks that control cell division and motor protein activity.
Peptide-based assay development: The KIF20A (809-817) fragment is a versatile component for the design and optimization of peptide-based assays, including enzyme-linked immunosorbent assays (ELISAs) and competitive binding assays. Its well-defined structure and sequence specificity allow for the establishment of quantitative and reproducible assays to monitor peptide-antibody or peptide-protein interactions. These assay systems are essential for high-throughput screening, antibody validation, and the quantitative assessment of molecular dynamics related to KIF20A.
Functional domain mapping: By employing this peptide in structure-function studies, researchers can dissect the contribution of the 809-817 region to the overall activity and regulation of KIF20A. Synthetic peptides corresponding to discrete protein segments enable systematic mutational analyses and functional mapping, revealing critical residues involved in motor activity, cargo recognition, or regulatory protein binding. Such insights are foundational for advancing the mechanistic understanding of kinesin superfamily members and their roles in cellular organization and division.
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