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New Products for Investigating the Protein-Binding Properties of Heparin, Heparan Sulfate (HS) and Other Glycosaminoglycans (GAGS)

AMSBIO
18 Jul 2011
bridget bridget
Laboratory Director

Product news

AMSBIO has announced a suite of exciting new products for investigating the protein-binding properties of Heparin, Heparan Sulfate (HS) and other glycosaminoglycans (GAGS).

Such investigations have traditionally been constrained by the need for chemical modification prior to attachment to inert or derivatized surfaces. The AMSBIO Heparin/GAG Binding Plate offers a simple solution to this problem - the specially-prepared plate surface adsorbs GAGS without modification whilst maintaining their protein-binding characteristics.

The versatility of the Heparin/GAG Binding Plate will find many applications including elucidation of optimum GAG sequences and sulfation patterns for binding to proteins of interest, analyses of sulfotransferases and endosulfatases and detection of inhibitors or enhancers of protein-GAG recognition. The new plate can also be used for studying receptor binding to growth factors or chemokines bound to surface-immobilized GAGS. The ELISA-type format of the Heparin/GAG Binding Plate is economical on the use of valuable protein reagents and is compatible with automated laboratory systems.

AMSBIO has also introduced new high performance arrays designed for use with their Heparin/GAG Binding Plate.

AMSBIO GAG Arrays can be used to gain information on the importance of the heparin and dermatan backbone structure and the position and density of sulfate groups for protein binding. The Heparin Oligosaccharide Array can be used to determine the length of oligosaccharide required for optimum binding to a protein of interest. The Heparin / HS Array was developed to find which of AMSBIO's naturally-occurring heparins and heparan sulfates (HS) is most effective at binding proteins of interest.

AMSBIO's K5 Polysaccharide Arrays offer a distinctive set of GAGs that contain novel sulfation motifs on N-acetylated or N-sulfated backbones. They offer exciting prospects for refining knowledge of the molecular basis of GAG-protein recognition and for discovering new activating or antatonistic sequences for growth factors, chemokines and many other proteins that are regulated by HS or heparin.

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