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Product Details
Citations (4)
Supplemental Products

GDP-Azido-Fucose Summary


Key Benefits

Learn more about Fluorescent Glycan Labeling and Detection

GDP-Azido-Fucose Structure



Molecular Weight

630.35 Da


1 mM Provided in 20 mM Tris, 50 mM NaBorate, pH 9.0


Incorporate or detect fucose without expensive, specialized equipment!


  • For in vitro enzymatic incorporation of azido-sugars into specific, targeted glycans.
  • Detecting the presence or absence of fucosylated glycans.
  • Tagging bio-molecules through fucosylation.
  • Assessing the level of fucosylation on target molecules.

Key Features and Benefits

  • Can assess for the presence of terminal fucosylation (e.g. core fucose) without expensive, specialized equipment.
  • Can be introduced to proteins and lipids that have fucosylation sites via fucosyltransferases.
  • Can be conjugated to desired reporter molecules via click chemistry.
  • Can be detected via Western blot, ELISA, and flow cytometry, depending on the type of reporter molecule.
  • Contains the smallest possible orthogonal functional group.
  • Has minimal side effects on target molecules.
  • User-friendly.

For Details:
Wu, ZL et al., (2015) Carbohydrate Res. 412:1-6.
Wu, ZL. et al., (2020) Glycobiology 30:970.

Related Reagents

Click Chemistry


Enzymes and Detection Reagents for GDP-Azido-Fucose, ES101




Protein O-Fucosyltransferase 1/POFUT1 Adds Fucose to Ser/Thr Important for Notch signaling
Fucosyltransferase 2/FUT2 Adds (terminal) Fucose to Galactose Generates H antigen
Fucosyltransferase 3/FUT3 Adds (terminal) Fucose to GlcNAc Generates Lea, Leb antigens
Fucosyltransferase 5/FUT5 Adds (terminal) Fucose to Galactose Generates sLex antigen

Fucosyltransferase 6/FUT6

  Generates sLex antigen
Fucosyltransferase 7/FUT7 Adds (terminal) Fucose to GlcNAc Generates sLex antigen
Fucosyltransferase 8/FUT8 Adds (non-terminal) Fucose to GlcNAc  

Fucosyltransferase 9/FUT9

  Generates sLex antigen
Fucosyltransferase 11/FUT11 Adds (non-terminal) Fucose to GlcNAc  





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The terminal fucose can be removed using a Fucosidase. Azido-fucose can then be added to open sites with specific fucosyltransferases and detected using Biotinylated Alkyne in a click chemistry reaction.

Sample Data

Detecting Open Fucosylation Sites on the Acceptor Substrate Recombinant Drosophila Notch EGF20
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Detecting Open Fucosylation Sites on the Acceptor Substrate Recombinant Drosophila Notch EGF20. rhPOFUT1 at 0.5 µg of was incubated at 37 °C for one hour with increasing amounts (0.5, 1, 2, 4 µg) of rdNotch EGF20 repeat. The left side is a labeling reaction including GDP-Azido-Fucose. The right side serves as a negative control labeling reaction without GDP-Azido-Fucose.

The results clearly show GDP-Azido-Fucose incorporation into the Notch EGF20 substrate on open sites for POFUT1-mediated fucosylation.

The buffer used contained 25 mM HEPES pH 7.5, 150 mM NaCl, and 10 mM MnCl2 for a total volume of 40 µl. The reactions were then conjugated for one hour with 1 nmol of Biotinylated Alkyne in the prescence of 100 µM CuCl2 and 2 mM Ascorbic Acid for a final volume of 50 µl. All reactions were separated on 12% SDS-PAGE and then detected with Streptavidin-HRP.


Shipping Conditions
The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Store the unopened product at < -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Good for 12 months from date of receipt.

Product Datasheets

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Assay Procedure

Sample Protocol for Core-6 Fucose Labeling

Protocols are guidelines. Parameters need to be optimized by end users.



Assay Procedure

1. Prepare a reaction mixture by combining 5 µg of Protein Sample, 1 µg of rhFUT8 in the presence of 1 nmol GDP-Azido-Fucose in the Assay Buffer with the final volume of 25 µL.


2. Prepare negative controls according to step 1 but omit Protein Sample or rhFUT8 or GDP-Azido-Fucose.


3. Incubate all the reactions and the controls at 37°C for one hour.


4. To each of the samples, add 5 µL of 1 mM CuCl2, 5 µL of 20 mM Ascorbic Acid, and 5 µL of 1 mM Biotinylated Alkyne. Mix with gentle tapping.


5. Incubate all samples at room temperature for 1 hour.


6. Separate the reactions and controls by 12% SDS-PAGE.


7. Blot the gel to a nitrocellulose membrane.


8. Block the blot with 10% fat-free milk for 5 minutes.


9. Thoroughly wash the membrane with TBST buffer by changing buffer three times for a total of 45 minutes.


10. Incubate the blot with 25 ng/mL Streptavidin-HRP in 30 mL TBST buffer for 30 minutes.


11. Thoroughly wash the membrane with TBST buffer by changing buffer three times for a total of 45 minutes.


12. Detect with commercial ECL (Enhanced Chemiluminescence) reagents.

Final Assay Conditions Per Reaction

  • GDP-Azido-Fucose: 1 nmol
  • rhFUT8: 1 µg
  • Protein Sample: 5 µg
  • Reaction volume: 25 µl

Click Chemistry Reaction Conditions Per Reaction

  • CuCl2: 5 nmol
  • Ascorbic Acid: 100 nmol
  • Biotinylated Alkyne: 5 nmol
  • Reaction volume: 40 µl

Citations for GDP-Azido-Fucose

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

4 Citations: Showing 1 - 4
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  1. Mouse WIF1 Is Only Modified with O-Fucose in Its EGF-like Domain III Despite Two Evolutionarily Conserved Consensus Sites
    Authors: F Pennarubia, E Pinault, B Al Jaam, CE Brun, A Maftah, A Germot, S Legardinie
    Biomolecules, 2020-08-28;10(9):.  2020-08-28
  2. Functional Characterization of POFUT1 Variants Associated with Colorectal Cancer
    Authors: M Deschuyter, F Pennarubia, E Pinault, S Legardinie, A Maftah
    Cancers (Basel), 2020-05-31;12(6):.  2020-05-31
  3. Imaging specific cellular glycan structures using glycosyltransferases via click chemistry.
    Authors: Wu Z, Person A, Anderson M, Burroughs B, Tatge T, Khatri K, Zou Y, Wang L, Geders T, Zaia J, Sackstein R
    Glycobiology, 2018-02-01;0(0):.  2018-02-01
  4. Core-6 fucose and the oligomerization of the 1918 pandemic influenza viral neuraminidase.
    Authors: Wu Z, Zhou H, Ethen C, N Reinhold V
    Biochem Biophys Res Commun, 2016-03-21;473(2):524-9.  2016-03-21


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