N-acetyl-D-mannosamine-[2-13C]

N-acetyl-D-mannosamine-[2-13C], an isotopically labeled compound essential for metabolic and biochemical research, finds diverse applications in the scientific domain. Here are the key applications:

Glycan Biosynthesis Studies: Central to the exploration of glycan biosynthesis, N-acetyl-D-mannosamine-[2-13C] plays a pivotal role. By integrating this isotope-laden sugar into cell culture media, researchers can meticulously monitor its integration into glycan structures. This process aids in unraveling the intricacies of glycosylation pathways, deciphering glycan structure-function correlations, and investigating the repercussions of glycosylation alterations on cellular functions.

Metabolic Flux Analysis: Embedded in metabolic investigations, N-acetyl-D-mannosamine-[2-13C] serves as a valuable tool for scrutinizing metabolic fluxes within cellular systems. Through the incorporation of this labeled sugar into metabolic pathways, scientists can trace its transformation into diverse metabolites using advanced techniques like NMR or mass spectrometry. This method enables the precise quantification of metabolic fluxes, offering profound insights into metabolic regulation and the dynamic nature of pathways.

Pathway Tracing in Disease Models: In the realm of disease modeling, N-acetyl-D-mannosamine-[2-13C] emerges as a critical element for tracing perturbed metabolic pathways linked to ailments like cancer and congenital glycosylation disorders. By analyzing alterations in metabolite labeling patterns, researchers can pinpoint dysregulated pathways and potential targets for therapeutic intervention. This approach contributes significantly to unraveling disease mechanisms and fostering the development of diagnostic strategies driven by biomarkers.

Protein Glycosylation Research: Delving into the realm of protein glycosylation, N-acetyl-D-mannosamine-[2-13C] serves as a valuable resource for investigating the intricate processes governing protein glycosylation within cells. Through the incorporation of this labeled sugar into glycoproteins, scientists can explore its impact on protein stability, folding, and functionality. This research is pivotal for comprehending how glycosylation influences protein interactions, signaling cascades, and the design of therapeutic glycoproteins tailored for medical applications.