Patent application number | Description | Published |
20080199905 | Catalytic Domains Of Beta(1,4)-Galactosyltransferase I Having Altered Metal Ion Specificity - Disclosed are mutants of galactosyltransferases that can catalyze formation of oligosaccharides in the presence of magnesium; mutants of galactosyltransferases having altered donor and acceptor specificity which can catalyze formation of oligosaccharides in the presence of magnesium; methods and compositions that can be used to synthesize oligosaccharides; methods for increasing the immunogenicity of an antigen; and methods to stabilize platelets. | 08-21-2008 |
20090233345 | Catalytic domains of beta(1,4)-galactosyl transferase i having altered donor and acceptor specificities, domains that promote in vitro protein folding, and methods for their use - Disclosed are methods and compositions that can be used to synthesize oligosaccharides; mutants of galactosyltransferases having altered donor and acceptor specificity; methods for increasing the immunogenicity of an antigen; and polypeptide stem regions that can be used to promote in vitro folding of polypeptides, such as the catalytic domain from a galactosyltransferase. | 09-17-2009 |
20110064663 | BETA 1,4-GALACTOSYLTRANSFERASES WITH ALTERED DONOR AND ACCEPTOR SPECIFICITIES, COMPOSITIONS AND METHODS OF USE - The invention relates generally to beta (1,4)-galactosyltransferase I mutants having altered donor and acceptor specificities, and methods of use thereof. In addition, the invention relates to methods for synthesizing oligosaccharides using the beta (1,4)-galactosyltransferase I mutants and to using the beta (1,4)-galactosyltransferase I mutants to conjugate agents, such as therapeutic agents or diagnostic agents, to acceptor molecules. | 03-17-2011 |
20110217235 | ALPHA 1-3 N-GALACTOSYLTRANSFERASE WITH ALTERED DONOR SPECIFICITIES - The invention generally features compositions and methods based on the structure-based design of alpha 1-3 N-Acetylgalactosaminyltransferase (alpha 3 GaINAc-T) enzymes from alpha 1-3 galactosyltransferase (a3Gal-T) that can transfer 2′-modified galactose from the corresponding UDP-derivatives due to substitutions that broaden the alpha 3Gal-T donor specificity and make the enzyme a3 GaINAc-T. | 09-08-2011 |
20130243690 | ALPHA 1-3 N-GALACTOSYLSTRANSFERASE WITH ALTERED DONOR SPECIFICITIES, COMPOSITIONS AND METHODS OF USE - The invention generally features compositions and methods based on the structure-based design of alpha 1-3 N-Acetylgalactosaminyltransferase (alpha 3 GalNAc-T) enzymes from alpha 1-3galactosyltransferase (a3Gal-T) that can transfer 2′-modified galactose from the corresponding UDP-derivatives due to substitutions that broaden the alpha 3Gal-T donor specificity and make the enzyme a3 GalNAc-T. | 09-19-2013 |
20140178985 | BETA 1,4-GALACTOSYLTRANSFERASES WITH ALTERED DONOR AND ACCEPTOR SPECIFICITIES, COMPOSITIONS AND METHODS OF USE - The invention relates generally to beta (1,4)-galactosyltransferase I mutants having altered donor and acceptor specificities, and methods of use thereof. In addition, the invention relates to methods for synthesizing oligosaccharides using the beta (1,4)-galactosyltransferase I mutants and to using the beta (1,4)-galactosyltransferase I mutants to conjugate agents, such as therapeutic agents or diagnostic agents, to acceptor molecules. | 06-26-2014 |
20150018522 | CATALYTIC DOMAINS OF BETA(1,4)-GALACTOSYLTRANSFERASE I HAVING ALTERED METAL ION SPECIFICITY - Disclosed are mutants of galactosyltransferases that can catalyze formation of oligosaccharides in the presence of magnesium; mutants of galactosyltransferases having altered donor and acceptor specificity which can catalyze formation of oligosaccharides in the presence of magnesium; methods and compositions that can be used to synthesize oligosaccharides; methods for increasing the immunogenicity of an antigen; and methods to stabilize platelets. | 01-15-2015 |
20160130359 | HER2-SPECIFIC MONOCLONAL ANTIBODIES AND CONJUGATES THEREOF - The identification of Her2-specific monoclonal antibody m860 is described. The m860 antibody was identified from a human naïve phage display Fab library by panning against the extracellular domain of human Her2. M860 binds to cell surface-associated Her2 with an affinity comparable to that of trastuzumab (Herceptin®), but binds to a different epitope. Using site-specific glycan engineering, m860 was conjugated to the small molecule drug auristatin F. The antibody-drug conjugate was stable, bound cell-surface expressed Her2 and exhibited potent cell killing of Her2-positive cancer cells, including trastuzumab-resistant breast cancer cells. | 05-12-2016 |