Glycosylation

Glycoprofile Metabolic Labeling


Highly selective chemical reactions within a cellular environment can be powerful tools for tracking and elucidating biological processes or engineering novel interactions. This chemical transformation permits the novel formation of covalent adducts of biopolymers within cells. Peracetylated unnatural sugars are introduced within glycans by metabolism of the synthetic azidosugar without detrimental side effects. The modified ligation scheme modeled after the widely applied Staudinger reaction results in an amide bond by coupling of the azide and a specifically engineered FLAG®-phosphine conjugate. Both reactive partners are abiotic and bio-orthogonal to native cellular components. Subsequent detection or enrichment is enabled through coupling of the GlycoProfile™ FLAG-phosphine with bound azido complex to various complementary FLAG platform reagents. The tremendous selectivity of the transformation should permit its execution within a cell's interior, offering new possibilities for probing intracellular interactions in model cell systems and even live animals.


  • Selectively targets labeled sugarsDetect and enrich without contamination
  • Fast non-toxic reactionsGet accurate and representative biological observations
  • Choose either or both detection and enrichment - FLAG platform reagents offer high sensitivity and specificity

   View Recent Literature

Product Code
Product Name
Package Qty
Minimum Applications
Sample Input
GPHOS1 GlycoProfile FLAG-Phosphine 1mg, 5x1mg 1, 5 600,000 cells per incubation. Tested with HeLa, Jurkat and CHO lines
A7480 N-Acetyazidogalactosamine, acetylated 1mg, 5mg 1, 5
A7355 A-Acetylazidoglucosamine, acetylated 1mg, 5mg 1, 5
A7605 N-Azidoacetylmannosamine, acetylated 1mg, 5mg 1, 5

Representation of the Staudinger Ligation:

Staudinger Ligation diagram

 

Reference:

  1. Saxon, E. & Bertozzi, C.R. Cell surface engineering by a modified Staudinger reaction. Science 287, 2007–2010
  2. Prescher, J.A. et al. Chemical remodelling of cell surfaces in living animals. Nature 430, 873–877 (2004).
  3. Vocadlo, D. J. & Bertozzi, C.R. A chemical approach for identifying O-GlcNAc-modified proteins in cells. Proc. Natl. Acad. Sciences, 100, 9116-9121 (2004)
  4. Hang, H. C. & Bertozzi, C.R. A metabolic labeling approach toward proteomic analysis of mucin-type O-linked glycosylation. Proc. Natl. Acad. Sci 100, 14846-14851(2004)
  5. Dube, D.H. & Bertozzi, C. R. Proc Natl Acad Sci, 103, 4819-4824 (2006)