Kin of IRRE-like protein 3 isoform 2 precursor (402-419)

Kin of IRRE-like protein 3 isoform 2 precursor (402-419) is a synthetic peptide fragment derived from the C-terminal region of the KIRREL3 protein, a member of the immunoglobulin superfamily implicated in cell adhesion and synapse formation. As a defined peptide segment, it embodies a specific sequence motif that is relevant to studies investigating protein-protein interactions, neuronal connectivity, and signaling pathways in developmental neurobiology. Its precise amino acid composition and structural features make it valuable for dissecting the functional domains of KIRREL3, which is known to play a role in synaptic specification and maintenance within the central nervous system.

Peptide interaction mapping: Researchers employ this peptide to elucidate interaction interfaces within the KIRREL3 protein and its binding partners. By using the (402-419) sequence in in vitro binding assays or pull-down experiments, scientists can characterize the molecular determinants underlying KIRREL3-mediated adhesion and signal transduction. This targeted approach enables detailed analysis of how specific sequence motifs contribute to the assembly and stability of protein complexes involved in neural development.

Antibody epitope validation: The defined sequence of this peptide serves as a reliable antigen for generating and validating antibodies that recognize the C-terminal region of KIRREL3 isoform 2. In immunoassays such as Western blotting, ELISA, or immunocytochemistry, the peptide helps confirm antibody specificity and sensitivity, facilitating accurate detection of endogenous or recombinant KIRREL3 in complex biological samples. This application is critical for studies aiming to localize or quantify the protein in various cellular contexts.

Functional domain analysis: The (402-419) fragment is instrumental in functional assays designed to probe the role of discrete KIRREL3 domains in cellular processes. By introducing the peptide into cultured neurons or heterologous expression systems, researchers can assess its influence on cell adhesion, neurite outgrowth, or synaptic assembly. Such experiments provide mechanistic insights into how this region of KIRREL3 contributes to its biological activity and regulatory interactions.

Peptide-based inhibitor design: Due to its sequence specificity, the peptide may be utilized as a template for developing selective inhibitors or mimetics that modulate KIRREL3 function. In structure-activity relationship studies, researchers can systematically modify the peptide to identify key residues essential for binding or activity, informing the rational design of molecules that alter protein-protein interactions in neurobiological pathways. This strategy supports efforts to dissect signaling cascades and understand the functional consequences of KIRREL3 modulation.

Mass spectrometry calibration and assay development: The unique sequence and defined mass of the (402-419) peptide make it suitable as an internal standard or calibration reference in mass spectrometry-based proteomic workflows. By incorporating the peptide into sample preparations, analysts can improve the accuracy and reproducibility of peptide identification and quantification, particularly in targeted assays focused on KIRREL3 or related proteins. This application enhances the reliability of proteomic data and supports high-confidence characterization of neuronal protein networks.

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