New Reagent Resources Available for Glycobiologists

NEW REAGENT RESOURCES FOR GLYCOBIOLOGISTS!!
Challenges in mammalian glycobiology research:
  • Most mammalian glycosyltransferases, glycosidases, and glycan modifying enzymes are difficult to express in bacteria
  • Many require post-translational modifications, disulfide bonds, chaperones for folding and function
  • Few are available in large quantities for enzymatic glycan synthesis, biochemical or structural studies on specificity or mechanisms
  • Most investigators in the field have their own favorite expression platforms for a small number of coding regions
  • Universal platforms for truncation design and eukaryotic expression are not generally available
To overcome these roadblocks we are introducing the “Repository of Glyco-Enzyme Expression Constructs” 
Expression constructs encoding ~80% of human glycosyltransferases, glycosidases, sulfotransferases, glycan modifying enzymes
  • Coding regions captured as truncated catalytic domains when possible
  • Transferred into Gateway® donor vectors for transfer into custom expression vectors
  • Expression vector constructs prepared for baculovirus, mammalian and bacterial expression
  • Eukaryotic expression constructs are generally designed to generate secreted products containing N- or C-terminal fusion protein tags
  • Constructs containing alternative fusion protein tag strategies are available for many expression products
  • All constructs are available from the NIH Protein Structure Initiative Materials Repository (DNASU)
  • Construct designs, expression protocols, and full annotation information is available at: glycoenzymes.ccrc.uga.edu
  • Tutorials are available to navigate the website and identify relevant genes, expression constructs, annotation information, clone IDs, and links to order information at DNASU
This is an NIH funded “Repository of Glyco-Enzyme Expression Constructs” with goals to:
  • Create expression reagents and protocols to to produce human glycosylation enzymes for biochemical, enzymatic, and structural studies.
  • Provide enzyme catalysts to complement glycan chemical synthesis: chemoenzymatic synthesis of glycan standards, recombinant glycoprotein remodeling, synthesis of rare unique glycans
  • Advance our understanding of mammalian glycosylation enzymes and synthesis of glycan structures.
For more information please go to: glycoenzymes.ccrc.uga.edu