Kinesin family member 27, isoform CRA_b (84-103)

Kinesin family member 27, isoform CRA_b (84-103) is a synthetic peptide fragment derived from the motor protein KIF27, representing residues 84 to 103 of the CRA_b isoform. As a segment of a larger kinesin superfamily protein, this peptide encompasses a region potentially involved in microtubule-based transport and intracellular trafficking. Kinesins are critical for cellular processes such as mitosis, organelle movement, and signal transduction, making specific fragments like this one valuable for dissecting protein structure-function relationships and mechanistic studies. The defined sequence and origin of this peptide provide a precise tool for researchers investigating the molecular dynamics of kinesin family member 27 and its associated pathways.

Peptide mapping: The peptide corresponding to amino acids 84 to 103 of KIF27 is frequently utilized in peptide mapping studies, where it serves as a reference standard for mass spectrometric identification or validation of protein expression. By incorporating this sequence into analytical workflows, researchers can confirm the presence and integrity of the KIF27 protein in complex biological samples. Such mapping is essential for characterizing post-translational modifications, detecting isoform-specific expression, and supporting proteomic profiling efforts focused on motor protein families.

Antibody generation: Synthetic peptides from defined regions of target proteins are widely employed as immunogens to raise polyclonal or monoclonal antibodies. The KIF27 (84-103) fragment offers a unique antigenic epitope for generating antibodies that specifically recognize the CRA_b isoform or its conserved motifs. These antibodies are instrumental in immunoblotting, immunoprecipitation, and immunofluorescence assays, enabling researchers to interrogate the spatial and temporal distribution of KIF27 within various cellular compartments and experimental conditions.

Protein-protein interaction studies: The defined sequence of the KIF27 (84-103) peptide provides a valuable probe for investigating direct or competitive binding interactions with other proteins or regulatory factors. In vitro binding assays, such as surface plasmon resonance or pull-down experiments, can utilize this fragment to elucidate the interaction partners of KIF27, map binding domains, or assess the effects of sequence modifications on affinity and specificity. These studies contribute to a deeper understanding of the molecular mechanisms governing microtubule dynamics and intracellular transport.

Epitope mapping: Researchers often employ synthetic peptides to delineate the precise epitopes recognized by antibodies or interacting proteins. The KIF27 (84-103) sequence can be used to map antibody binding sites, identify immunodominant regions within the kinesin protein, or validate the specificity of reagents developed for basic research applications. Such epitope mapping is essential for optimizing antibody-based assays and for the development of high-fidelity detection tools targeting KIF27 isoforms.

Functional assays: Incorporation of the KIF27 (84-103) peptide into cell-based or biochemical assays supports functional studies aimed at dissecting the regulatory roles of the kinesin protein. By introducing this fragment as a competitive inhibitor or substrate mimic, researchers can probe the contribution of the corresponding region to motor activity, cargo recognition, or microtubule association. These functional analyses facilitate the identification of key motifs required for kinesin-mediated processes and may reveal novel regulatory mechanisms within the broader context of cytoskeletal dynamics.

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