HS fraction I mol. wt. approx. 40kDa

GAG-HS I

eparan Sulphate - Guidance notes

Heparan sulphate (HS) is widely recognised as the major glycosaminoglycan on cell surfaces; it is an essential 

co-receptor for many growth factors, morphogenic proteins and signalling structural elements in the extracellular 

matrix such as fibronectin and various types of collagen. It has a distinctive molecular organisation in which

 sulphated domains are spaced along the polymer chain separated by regions that are largely devoid of sulphate 

groups. Despite sharing a common design the HS fine structure is often typical of the cell of origin due to variability 

of sulphation patterns in the sulphated regions. This variability probably underpins specific protein binding activities 

at cell surfaces.

Kjellen, L. and Lindahl, U. (2018) Specificity of glycosaminoglycan-protein interactions. Current Opinion in Structural 

Biology 50:101–108

Gallagher J. (2015) Fell-Muir Lecture: Heparan Sulphate and the art of cell regulation: a polymer chain conducts the 

protein orchestra. Int J Exp Pathol. 96:203-231.

Xu D. and  Esko JD: (2014) Demystifying heparan sulfate-protein interactions. Annu Rev Biochem . 83:129-157.

To assist investigations of this most intriguing of glycosaminoglycans we offer several preparations of Heparan 

Sulphates that vary in molecular size and sulphation including a unique set of selectively-desulphated Heparan 

Sulphates. Please also see our heparin oligosaccharides that mimic some of the sulphation variability seen in HS.

Heparan Sulphate Polymer Fractions

1. Heparan Sulphate fraction I: Mol wt approx. 40kDa

Relatively low in Sulphation (when compared to parent GAG-HS01)/High Molecular Weight HS.

40 N-sulphate groups per 100 disaccharides 35 O-sulphate groups per 100 disaccharides *Polymer sulphation 

(N- and O-sulphate groups) is 75 per 100 disaccharides. The domain structure of this preparation is broadly 

similar to the most common form of heparan sulphate present on cell surfaces