The development and investigation of a new affinity proteomics probe and methodology are presented in this dissertation. A trifunctional affinity proteomics probe (TAPP) was envisioned and prepared to serve as a lectin capture reagent. The TAPP consists of a solid support to serve as a handle for captured protein as well as scaffold for multivalency, a saccharide of interest to fish for an unknown or elicit a suspected specific interaction, and a photoactivated cross-linking moiety to covalently capture binding proteins. The perfluorinated phenylazide cross-linker was shown to exhibit better performance relative to the parent phenylazide with respect to sensitivity and selectively for specific and nonspecific interactions. The synthetic strategy included coupling of the saccharide signal as late as possible in the preparation to allow for ease of diversification of the saccharide signal. Such a strategy could be exploited with automated combinatorial chemical synthesis of oligosaccharides to quickly build a diverse series of probes for study. Synthesis of several galactose and galactosamine based monosaccharide donors are presented in this dissertation with the potential to be used to create an array of six oligosaccharides from the nematode Caenorhabditis elegans. Solution phase, automated synthesis was employed to test the building blocks, and to investigate current methods to accomplish the formation of a 3,4,6 glycosidic branching pattern on a singular monosaccharide unit. Results suggest such a glycosylation reaction is, indeed, possible.