Glycans and glycoconjugates are integral to a wide range of biological functions, including energy storage, immune modulation, and molecular recognition. To elucidate the molecular mechanisms underlying these functions, a variety of chemical biology strategies have been developed. For instance, fluorescent probes have been employed to visualize the dynamics and subcellular localization of glycans, while photoaffinity probes have enabled the identification of glycan-binding proteins in complex biological systems. In parallel, C-glycoside analogs—resistant to enzymatic hydrolysis—have been developed as stable mimics of native glycans, preserving both structural features and biological activity. Given that specific functional groups within glycan structures often play decisive roles in their function, approaches that minimize the extent of chemical modification are critical for accurate functional analysis. Guided by this rationale, our group has developed a series of glycan analogs and photoaffinity probes that retain the native structure and physicochemical properties of the parent glycans. This chapter outlines the conceptual basis, development, and applications of these molecular tools in the context of chemical glycobiology.