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A New Enzyme for Remove Sialic Acids on Glycoproteins
A New Enzyme for Remove Sialic Acids on Glycoproteins
Origin of place United States
Model
Supplier Profacgen
Price
Hits 472
Updated 8/23/2023
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Glycosylation plays a crucial role in protein folding, trafficking, stability, and cellular activities such as receptor binding, cell signaling, immune recognition, inflammation, and pathogenesis. N-glycosylation and O-glycosylation are the two primary forms of glycosylation modification. N-linked glycans are linked to the amide side chains of asparagine (Asn) residues on the protein with a core; in contrast, O-linked glycans have a disaccharide core of Core 1 or Core 3 attached to the hydroxyl side chains of Ser or Thr residues.

https://www.profacgen.com/a-new-enzyme-for-remove-sialic-acids-on-glycoproteins.htm

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