H10, Biotinylated carries a functional peptide motif covalently linked to biotin, enabling high-affinity capture on streptavidin matrices. The construct permits controlled orientation in pull-down, ELISA, or imaging assays. Researchers exploit the tag to study protein-peptide interactions and complex formation. Applications include affinity purification, interaction screening, and biosensor development.
CAT No: R2744
H10, biotinylated, is a specialized carbohydrate compound that features a biotin moiety conjugated to the H10 oligosaccharide backbone. This unique molecular design enables both high-affinity binding to streptavidin or avidin and the preservation of the carbohydrate's native recognition properties, making it highly versatile for research and analytical applications. The biotinylation of H10 enhances its utility in a range of biochemical assays, allowing for robust and specific immobilization, detection, or purification strategies. Its water solubility, chemical stability, and compatibility with various biological matrices further expand its potential uses in both routine and advanced laboratory workflows. Researchers value biotinylated H10 for its capacity to bridge carbohydrate chemistry with biotin-avidin technology, thereby facilitating precise molecular interactions and downstream analyses.
Glycan microarray construction: In glycomics research, H10, biotinylated, serves as an essential building block for constructing glycan microarrays. By leveraging the strong biotin-streptavidin interaction, the compound can be immobilized efficiently onto streptavidin-coated surfaces, enabling high-density and spatially controlled presentation of the carbohydrate. This immobilization strategy allows scientists to systematically probe carbohydrate-protein interactions, screen for glycan-binding proteins, and elucidate binding specificities with high sensitivity and reproducibility. The use of biotinylated H10 in microarrays significantly accelerates the discovery of novel glycan ligands and the mapping of glycan recognition patterns, which are fundamental to understanding cell signaling, pathogen recognition, and immune responses.
Affinity purification: Biotinylated H10 is employed as a selective affinity ligand for the purification of carbohydrate-binding proteins or antibodies. By attaching the biotinylated carbohydrate to streptavidin- or avidin-coated beads, researchers can create highly specific affinity matrices that capture target molecules from complex biological samples. This approach minimizes non-specific interactions and enhances the purity of the isolated proteins, making it particularly valuable for downstream proteomic analyses, enzyme characterization, or antibody validation. The reversible nature of the biotin-streptavidin binding also allows for gentle elution conditions, preserving the functional integrity of the captured molecules.
Cell surface labeling and tracking: The biotin tag on H10 facilitates its use in cell surface labeling experiments, where it can be used to probe cell surface glycan expression or to monitor glycan-mediated cellular processes. By incubating cells with the biotinylated carbohydrate, followed by detection with fluorescently labeled streptavidin, researchers can visualize and quantify glycan distribution on live or fixed cells using flow cytometry or fluorescence microscopy. This application is instrumental in studies of cell differentiation, immune cell activation, or pathogen-host interactions, as it enables precise mapping of glycan signatures in diverse cellular contexts.
Enzyme substrate for glycosyltransferase studies: In enzymology, H10, biotinylated, functions as a defined substrate for glycosyltransferase assays. The biotinylated structure allows for straightforward detection and quantification of enzymatic modifications using streptavidin-based detection systems. Researchers can monitor the incorporation of additional sugar residues, assess enzyme specificity, and compare catalytic efficiencies under various conditions. This application is critical for the characterization of glycosyltransferase enzymes, which play key roles in glycan biosynthesis and remodeling pathways.
Immunoassay development: The incorporation of biotinylated H10 into immunoassay platforms, such as ELISA or lateral flow assays, enhances both sensitivity and specificity in the detection of glycan-binding antibodies or lectins. By immobilizing the biotinylated carbohydrate onto streptavidin-coated plates or membranes, assay developers achieve consistent and oriented presentation of the glycan epitope, resulting in improved assay performance and reproducibility. This strategy is widely adopted in the development of diagnostic reagents, research tools for immune profiling, and high-throughput screening of glycan-binding molecules.
Lectin interaction studies: Biotinylated H10 is a valuable probe in the investigation of lectin-carbohydrate interactions, providing a robust platform for kinetic and binding studies. By immobilizing the biotinylated carbohydrate on sensor chips or beads, researchers can perform surface plasmon resonance, biolayer interferometry, or pull-down assays to characterize lectin specificity, affinity, and binding kinetics. These studies yield critical insights into the molecular basis of glycan recognition, informing the design of glycan-based inhibitors, vaccines, or therapeutic agents. The versatility of H10, biotinylated, in such applications underscores its importance in advancing glycoscience research and expanding the toolkit available for carbohydrate-focused investigations.
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