Bacterial cell surface glycans mediate pathogenic and symbiotic interactions with hosts and other organisms. The implications of bacterial glycans in human health have made them attractive targets in drug design for antibiotics, antibacterial vaccines, and even in new therapeutics for treating diseases. Despite this appeal, there are a lack of specific glycan- interacting tools to isolate, detect, and target bacterial glycans. This is partly due to the incredible diversity of bacterial glycans, which includes rare monosaccharide building blocks as well as complex branching and linkages. However, many bacterial polysaccharides are composed of oligosaccharide repeat units, and these repeat units are built on a common isoprenoid scaffold called bactoprenyl phosphate (BP). While we have used this knowledge for a generalized route for studying bacterial glycans, there is a need for more efficient ways to isolate glycans such as polysaccharides and a need for methods to develop glycan-interacting tools for a diverse set of bacterial glycans.The work in this thesis followed a general scheme for developing new bacterial glycan- interacting partners (GIPs), which included: glycan isolation and glycan immobilization onto a magnetic bead (MB) platform for GIP analysis. This study utilized a model bacterial glycan system with the well-studied capsular polysaccharide A (CPSA) from Bacteroides fragilis and the isoprenoid-linked tetrasaccharide CPSA repeat unit. Using these two glycans, this study investigated two glycan immobilization strategies, which may be applied to other bacterial glycans. A new isolation technique and noncovalent immobilization method were established for the isoprenoid-linked oligosaccharide, and a preliminary covalent immobilization method was investigated for the polysaccharide.