Genetically engineered host animal cells capable of producing glycoproteins having modified glycosylation patterns, e.g., defucosylation and/or monoglycosylation. Such host animal cells can be engineered to express fucosidase, endoglycosidase or both.

Provided in certain embodiments are new methods for forming azido modified biomolecule conjugates of reporter molecules, carrier molecules or solid support. In other embodiments are provided methods for enzymatically labeling a biomolecules with an azide group.

A therapeutic agent containing, as an effective component, a glycolytic enzyme which is different from a deficient protein of a patient with lysosomal storage disease as a subject and/or a glycolytic enzyme which does not have a mannose 6-phosphate moiety or a mannose moiety.

Provided herein are deglycosylating enzymes that remove a broad range of N-glycans from N-glycosylated proteins. Further provided are methods of recombinantly producing and expressing the deglycosylating enzymes. The presently described deglycosylating enzymes can be used to produce free glycans for characterization, and for prebiotic and immunostimulatory uses. In addition, the presently described deglycosylating enzymes can be used to produce deglycosylated proteins for characterization, to improve digestion, and to reduce immunogenicity.

The present invention concerns a method for treating a demyelinating condition in a subject, by administering an agent to the subject that inhibits vascular endothelial cell phagocytosis. The method of the invention is useful in treating, for example, a demyelinating condition associated with an injury, such as a spinal cord injury or traumatic brain injury, as well as other demyelinating conditions, such as multiple sclerosis.

Provided herein are deglycosylating enzymes that remove a broad range of N-glycans from N-glycosylated proteins. Further provided are methods of recombinantly producing and expressing the deglycosylating enzymes. The presently described deglycosylating enzymes can be used to produce free glycans for characterization, and for prebiotic and immunostimulatory uses. In addition, the presently described deglycosylating enzymes can be used to produce deglycosylated proteins for characterization, to improve digestion, and to reduce immunogenicity.

The object is to provide a lysis method and lysis treatment solution for efficiently lysing cells of various Streptococcus bacteria in milk of a livestock animal to release a specific antigen substance contained in the cells for detecting whether causative bacterium of mastitis is a Streptococcus bacterium or not by using the milk, as well as a detection method using an immunochromatographic device. There is provided a method for lysing a Streptococcus bacterium, which comprises the step of mixing a lysis agent containing a lytic enzyme with milk obtained form a livestock animal to lyse a Streptococcus bacterium existing in the milk. The lytic enzyme is preferably at least one selected from the group consisting of lysozyme, labiase, and -N-acetylglucosaminidase.

The present disclosure provides engineered eukaryotic cells comprising a surface displayed catalytic domain of an endoglycosidase and methods of use.

Provided herein are deglycosylating enzymes that remove a broad range of N-glycans from N-glycosylated proteins. Further provided are methods of recombinantly producing and expressing the deglycosylating enzymes. The presently described deglycosylating enzymes can be used to produce free glycans for characterization, and for prebiotic and immunostimulatory uses. In addition, the presently described deglycosylating enzymes can be used to produce deglycosylated proteins for characterization, to improve digestion, and to reduce immunogenicity.

Provided herein are deglycosylating enzymes that remove a broad range of N-glycans from N-glycosylated proteins. Further provided are methods of recombinantly producing and expressing the deglycosylating enzymes. The presently described deglycosylating enzymes can be used to produce free glycans for characterization, and for prebiotic and immunostimulatory uses. In addition, the presently described deglycosylating enzymes can be used to produce deglycosylated proteins for characterization, to improve digestion, and to reduce immunogenicity.