Core 1 O-Glycan

The core 1 glycan consists of galactose linked β-3 to GalNAc. Core 1 is the most common O-linked glycan found in nature. It is antigenic, also known as the T antigen. It forms the core structure of other O-linked glycans, most often containing sialic acids, extended from the terminal beta-linked galactose or the serine/thronine-linked GlcNAc. Extension of larger O-linked glycans also includes galactose, GlcNAc, GalNAc, or fucose. Other core 1 O-linked glycans we supply include sialylated core 1 glycan and disialylated core 1 glycan.

Description Core 1 O-glycan (C1).

Form Dry. Dried by centrifugal evaporation from an aqueous solution.

Purity >90% pure as assessed by a combination of CE and HPLC.

HILIC HPLC profile of 2AB labelled C1 glycan (see method conditions below) (Cat. #: CAB-C1-01, Batch B412- 07).

Storage Keep at -20°C both before and after dissolution. This product is stable for at least 5 years as supplied.

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. Minimize exposure to elevated temperatures or extremes of pH.

Safety This product is non-hazardous and has been purified from synthetic sources certified to be free of all hazardous material including pathogenic biological agents.

Core 1 Glycan References

Brockhausen I, Schachter H, Stanley P. O-GalNAc Glycans. In: Varki A, Cummings RD, Esko JD, et al., editors. Essentials of Glycobiology. 2nd edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2009. Chapter 9.

Marcelo F, Garcia-Martin F, Matsushita T, Sardinha J, Coelho H, Oude-Vrielink A, Koller C, André S, Cabrita EJ, Gabius HJ, Nishimura S, Jiménez-Barbero J, Cañada FJ. Delineating binding modes of Gal/GalNAc and structural elements of the molecular recognition of tumor-associated mucin glycopeptides by the human macrophage galactose-type lectin. Chemistry. 2014 Dec 1;20(49):16147-55. doi: 10.1002/chem.201404566. Epub 2014 Oct 16.

Edwinson A, Widmer G, McEvoy J. Glycoproteins and Gal-GalNAc cause Cryptosporidium to switch from an invasive sporozoite to a replicative trophozoite. Int J Parasitol. 2016 Jan;46(1):67-74. doi: 10.1016/j.ijpara.2015.09.001. Epub 2015 Sep 30.