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Surface plasmon resonance (SPR) is an optical biosensing technique that monitors biomolecular interactions in real time by detecting changes in the refractive index at a metal film surface. When polarized light illuminates the metal layer, it generates evanescent waves that resonate with surface plasmon waves produced by free electrons at a specific angle or wavelength, causing a sharp dip in reflected light intensity; binding events between ligands (such as immobilized glycans) and analytes (such as antibodies) alter the local refractive index, shifting the resonance angle and thereby enabling label-free quantification of binding specificity, affinity, kinetics, and concentration. Leveraging this principle, SPR has proven exceptionally effective for glycan-targeting antibody screening and analysis: diverse glycan architectures, derived from chemical synthesis or biological sources, either purified or blended, can be immobilized on biosensor chips in defined geometric patterns to create plasmonic glycan arrays. These platforms support exhaustive antibody profiling, pathological biomarker discovery, and standardized large-scale analysis of dynamic binding parameters and immunoglobulin concentrations.