Chemical conjugation of polysaccharides to protein carriers has become essential in carbohydrate vaccine development to enhance the poor immunogenicity of glycans. Neutral and uncharged carbohydrates induce T-cell independent responses, failing to produce robust IgG antibodies or sustained T-cell memory and conjugating native or synthetic glycans with carrier proteins such as the Cross-Reactive-Material-197 (CRM197) diphtheria toxin mutant, tetanus toxoid, or protein D of H. influenzae eliciting T-cell-dependent immune responses and class switching that produces high-affinity antibodies. This chapter describes the most commonly used synthetic glycoconjugates preparation strategy involving a spacer and a linker carrying a functional group, mostly amine, that couples the synthetic glycan to the carrier protein through its primary amine side chains of lysine residues and N-terminus. Our detailed protocol aims to advance the development of carbohydrate-binding antibodies that target tumor-associated carbohydrate antigens and expand our toolbox in the war against cancer.