G0F Glycan (NGA2F) Synonyms NGA2F N-linked oligosaccharide, F(6)A2
The G0F glycan is on of the four most common glycans found on monoclonal antibodies, along with the two G1F isomers, and G2F. A mixture of these glycans have been combined in our MAb4 Antibody Reference Panel.
These glycans are known to affect stability and solubility of antibodies within the body, as well as affecting ADCC and CDC activity. Due to the biological functions of these glycans found on monoclonal antibodies, the micro-heterogeneity of these oligosaccharides must be characterized during drug development and lot-to-lot variability in approved biological drug products.
Description: G0F: Asialo-, agalacto-, core-fucosylated bi-antennary complex-type N-glycan (oligosaccharide). NGA2F is the agalacto- substructure of NA2F (G2F) glycan.
Sources: The G0F glycan is found on many mammalian glycoproteins including human IgG and is a substructure of bi-antennary N-linked oligosaccharides such as A2F, A1F, and NA2F which are widely found on glycoproteins. This product is typically purified from the oligosaccharide pool released from porcine thyroglobulin by hydrazinolysis using a combination of HPLC and glycosidase digestion.
Form: Dry. Dried by centrifugal evaporation from an aqueous solution. No salts.
Molecular Weight: 1463
Purity: > 90% pure as assessed by a combination of 1 H-NMR and HPLC.
Storage: -20˚C both before and after dissolution. This product is stable for at least 5 years as supplied.
View Certificate of Stabilty
Shipping: The product can be shipped at ambient when dry. After dissolution, ship on dry ice.
Handling: Allow the unopened vial to reach ambient temperature and tap unopened on a solid surface to ensure that most of the lyophilized material is at the bottom of the vial. Gently remove the cap, add the desired volume of reconstitution medium, re-cap and mix thoroughly to bring all the oligosaccharide into solution. For maximal recovery of oligosaccharide, ensure that the cap lining is also rinsed and centrifuge the reconstituted vial briefly before use. Ensure that any glass, plasticware or solvents used are free of glycosidases and environmental carbohydrates. Minimise exposure to elevated temperatures or extremes of pH. High temperatures and low pH will cause desialylation. High pH will cause epimerisation of the reducing terminus GlcNAc.
Safety: This product is non-hazardous and has been purified from natural sources certified to be free of all hazardous material including pathogenic biological agents.
Download Non-hazardous MSDS
HPLC Analysis of the G0F Glycan (NGA2F)
LudgerPure and LudgerTag labeled glycan mixtures may be separated and analysed by a variety of HPLC (high pressure liquid chromatography) methods using LudgerSep HPLC columns.
The LudgerSep columns are are available for the following applications:
Separation of charged and neutral glycans via anion exchange columns:
LS-C3-7.5×75 LudgerSep C3 – 7.5x75mm
LS-C2-4.6×50 LudgerSep C2 – 4.6x50mm
Profile analysis of neutral and charged glycans via normal phase columns:
LS-N2-2.0×250 LudgerSep N2 – 2.00x250mm
LS-N2-4.6×250 LudgerSep N2 – 4.6x250mm
LS-N1-4.6×250 LudgerSep N1 – 4.6x250mm
The LudgerSep N2 columns are an especially powerful tool for the purification and analysis of LudgerTag labeled oligosaccharides from complex glycan mixtures. Please contact us for advise regarding your particular application.
Mass Spectrometry and Electrophoresis
LudgerPure and LudgerTag labeled glycans may also be analysed by mass spectrometry, electrophoresis, and various types of spectroscopy. Please call us for advise on the dyes and analysis conditions most suitable for your intended analyses.
– Huhn C, Selman MH, Ruhaak LR, Deelder AM, Wuhrer M. IgG glycosylation analysis. Proteomics 9(4):882-913. (2009)
-Liu L. Antibody glycosylation and its impact on the pharmacokinetics and pharmacodynamics of monoclonal antibodies and Fc-fusion proteins. J Pharm Sci. Jun;104(6):1866-1884. (2015).
Reusch D, Haberger M, Maier B, Maier M, Kloseck R, Zimmermann B, Hook M, Szabo Z, Tep S, et al. Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles–part 1: separation-based methods. MAbs. 7(1):167-79. (2015)