Kinesin-like protein KIF20A (12-20)

Kinesin-like protein KIF20A (12-20) is a synthetic peptide fragment derived from the motor domain region of the KIF20A protein, a member of the kinesin superfamily involved in microtubule-based intracellular transport and mitotic processes. As a well-defined peptide sequence corresponding to amino acids 12 through 20 of KIF20A, it provides a valuable molecular tool for researchers investigating the structure, function, and regulatory mechanisms of kinesin motor proteins. The specificity and sequence fidelity of this peptide make it highly relevant for studies focused on motor protein interactions, cell division, and the regulation of microtubule dynamics in various cellular contexts.

Epitope Mapping: Researchers frequently use the KIF20A (12-20) peptide for epitope mapping to identify and characterize antibody binding sites within the KIF20A protein. By employing this peptide in immunoassays such as ELISA or western blot, investigators can determine the specificity of monoclonal or polyclonal antibodies against KIF20A, which is essential for the development and validation of immunodetection reagents. This application is particularly valuable in studies aiming to elucidate the immune recognition landscape of kinesin proteins or to generate highly selective research antibodies for use in cell biology and proteomics.

Protein-Protein Interaction Studies: The peptide fragment serves as a model substrate for dissecting protein-protein interactions involving the KIF20A motor domain. Its defined sequence enables in vitro binding assays to investigate how KIF20A interacts with microtubule-associated proteins, regulatory cofactors, or potential inhibitors. By using the peptide in pull-down assays, surface plasmon resonance, or peptide array formats, researchers can map binding interfaces and gain mechanistic insights into the regulation of kinesin-driven processes during mitosis and intracellular transport.

Phosphorylation and Post-Translational Modification Analysis: KIF20A (12-20) can be employed as a substrate in kinase assays to study phosphorylation events within the N-terminal region of the protein. This application is instrumental in delineating kinase-substrate relationships, characterizing the functional impact of site-specific modifications, and exploring how phosphorylation influences kinesin activity or mitotic progression. The use of synthetic peptides in these assays allows for precise control over sequence context and facilitates the identification of modification sites by mass spectrometry.

Peptide-Based Inhibitor Screening: The defined sequence of this KIF20A fragment makes it suitable for use in high-throughput screening platforms aimed at identifying small molecules or peptides that disrupt KIF20A interactions. By incorporating the peptide into competitive binding assays, researchers can evaluate the efficacy of candidate inhibitors in blocking key protein interfaces. Such studies contribute to the development of novel research tools for modulating kinesin function and advancing the understanding of mitotic regulation at a molecular level.

Antigen Design for Immunization: The KIF20A (12-20) peptide is also utilized as an immunogen for generating sequence-specific antibodies in animal models. Its unique sequence allows for the production of antibodies that recognize the native or denatured forms of KIF20A, facilitating subsequent applications in immunoprecipitation, immunofluorescence, or tissue localization studies. The ability to elicit targeted immune responses using synthetic peptides supports the creation of robust detection reagents tailored to the needs of cell division and cytoskeletal research.

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