BOC Sciences provides the synthesis of high-quality glycosylated amino acids, with specifications ranging from milligrams to kilograms. We also provide an amino acid quality inspection report together with the target product to ensure that the product meets the requirements.
Glycosylation of proteins refers to the process in which proteins are linked to sugar chains under the action of enzymes. N-glycosylation is the most widely and deeply studied type of modification in glycosylation, which refers to the connection of sugar chains with the free amino groups of asparagine in proteins. N-glycosylation modification plays an important role in the correct folding, functional localization, and intracellular transport of proteins, and can improve protein stability. N-glycosylation can affect various important life activities such as cell recognition, differentiation and development, signal transduction, and immune response. For mammals, N-glycosylation plays an important role in regulating embryonic development, cancer development and immune defense. For plants, N-glycosylation plays an important role in many physiological processes such as cell wall formation, reproductive development, and resistance to pathogen invasion.
Glycosylated amino acids refer to compounds with amino and carboxyl functional groups attached to the carbon atoms of the 2,5- or 2,6-sugar ring backbone, which can be used as building blocks for the preparation of various glycoconjugates. The step-by-step synthesis of glycopeptide compounds from glycosylated amino acids is highly reliable, accurate, and easy to control. It provides a new research method for the design and research of glycopeptide compounds, which is of great significance. We provide customized amino acid N-glycosylation modification services, and the resulting products include N-glycosyl modified asparagine, aspartic acid and their derivatives.
With accumulated rich experience, we have been focusing on the custom synthesis of amino acids. We can synthesize glycosylated amino acids of different specifications and purity levels according to different requirements of customers, and attach an analysis report to ensure the high-quality and efficient completion of the project.
We react different amino acids with amino sugars to prepare N-glycosylated amino acid compounds. The synthetic route has mild reaction and high yield. All compounds were confirmed by elemental analysis, IR, NMR and MS.
N-potential glycosylation sites are predicted by online software.
Glycosylation site analysis helps to further reveal the biological characteristics of glycoproteins and plays an important role in product quality control. Proteins modified by N-glycosylation have a basic amino acid structural backbone. The N-glycosidic bond formed during the N-glycosylation modification has special requirements on the amino acid sequence, and only binds to the amino group of asparagine in the specific amino acid sequence. N-glycosylation site analysis uses specific endoglycosidase or protease to enzymatically hydrolyze glycoproteins into peptides, then enriches glycopeptides, and performs desugaring reactions in 16O and 18O aqueous solutions, combined with mass spectrometry analysis and identification N-glycosylation site.
N-glycosylation analysis is to analyze the structure and type of N-type sugar chains and confirm the amino acid sites where N-glycosylation occurs.