CD24/Siglec-10 Blocking Peptide (CSBP) contains a sequence engineered to disrupt CD24-Siglec-10 binding interfaces. Charged and aromatic residues provide targeted recognition of protein surfaces. Researchers study its binding kinetics, conformational dynamics, and specificity. Applications include receptor-ligand mapping, PPI inhibition modeling, and structural-motif exploration.
CAT No: R2842
Synonyms/Alias:CD24/Siglec-10 blocking peptide, CSBP; HY-P10091; CS-0906803
CD24/Siglec-10 blocking peptide, CSBP, is a synthetic peptide designed to disrupt the interaction between the cell surface protein CD24 and the inhibitory receptor Siglec-10. This peptide targets a key immune checkpoint pathway that modulates phagocytosis and immune tolerance, making it an important molecular tool for dissecting immune regulation mechanisms. Its sequence and structural features are optimized to competitively inhibit the CD24-Siglec-10 axis, providing researchers with a precise approach to study cell signaling, immune evasion, and related cellular processes in vitro. As a specialized peptide reagent, CSBP serves as a valuable resource in immunology, cell biology, and translational research focused on immune checkpoint modulation.
Immune checkpoint research: As a selective inhibitor of the CD24-Siglec-10 interaction, CSBP is widely used to investigate the molecular basis of immune checkpoint pathways. By blocking this specific ligand-receptor pair, researchers can delineate the role of CD24-mediated signaling in the suppression of immune cell activity, particularly in the context of innate immune responses such as macrophage-mediated phagocytosis. This application provides critical insights into how cells evade immune surveillance and how immune checkpoints contribute to tissue homeostasis and disease progression.
Cellular signaling pathway analysis: The peptide is instrumental in dissecting downstream signaling events triggered by the CD24-Siglec-10 axis. By interfering with this interaction, scientists can analyze changes in intracellular signaling cascades, such as the recruitment of SHP-1/2 phosphatases and alterations in phosphorylation patterns. This enables a detailed study of how inhibitory signals are transduced within immune cells, facilitating the identification of novel regulatory nodes and potential targets for immunomodulation in experimental systems.
Functional studies in phagocytosis assays: CSBP is frequently employed in in vitro phagocytosis assays to evaluate the impact of CD24-Siglec-10 blockade on the engulfment of target cells by macrophages or other phagocytes. By preventing the inhibitory signaling that normally dampens phagocytic activity, the peptide allows for quantification of changes in effector cell function. These studies are particularly relevant for elucidating the mechanisms by which cells, such as cancer or apoptotic cells, evade clearance by the immune system.
Development of immune modulation strategies: The blocking peptide serves as a prototype molecule for the design and screening of novel agents aimed at modulating the CD24-Siglec-10 pathway. Its use in structure-activity relationship studies, competitive binding assays, and high-throughput screening platforms supports the identification and optimization of next-generation immune checkpoint inhibitors. This application is of significant interest to researchers developing new molecular tools for immune intervention in preclinical models.
Validation of target specificity: CSBP is an essential control in experiments designed to confirm the specificity of antibodies, small molecules, or other biological agents targeting the CD24-Siglec-10 interaction. By including the peptide in competitive binding or functional inhibition assays, scientists can distinguish between on-target and off-target effects, ensuring the reliability and interpretability of their experimental results. This approach enhances the rigor of studies investigating the biological significance of this immune checkpoint pathway.
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