Abstract: Substantially pure glycosidases capable for cleaving selected glycosidic bonds have been described including glycosidases isolated from Xanthomonas and recombinant glycosidases. Substrate specificity of isolated enzymes have been identified for GlcNac?1-x, Gal?1-3R, Gal?1-6R, Gal?1-3R, Fuc?-2R, Fuc?1-3R, Fuc?1-4R, Man?1-2R, Man?1-3R, Man?1-6R, Man?1-4R, Xyl?1-2R, Glc?1-4R, and Gal?1-4R providing improved capability for selectively cleaving a glycosidic linkage in a carbohydrate substrate and for forming modified carbohydrates.

Abstract: The invention provides cells that produce increased levels of recombinant protein by modulating the activity of translational regulator gene products that are downstream targets of PKB alpha, methods of making such cells, and methods of using such cells. Such translational regulator gene products include 4E-BP1 and mTOR.

Abstract: Substantially pure glycosidases capable for cleaving selected glycosidic bonds have been described including glycosidases isolated from Xanthomonas and recombinant glycosidases. Substrate specificity of isolated enzymes have been identified for GlcNac&bgr;1-x, Gal&agr;1-3R, Gal&agr;1-6R, Gal&bgr;1-3R, Fuc&agr;-2R, Fuc&agr;1-3R, Fuc&agr;1-4R, Man&agr;1-2R, Man&agr;1-3R, Man&agr;1-6R, Man&bgr;1-4R, Xyl&bgr;1-2R, Glc&bgr;1-4R, and Gal&bgr;1-4R providing improved capability for selectively cleaving a glycosidic linkage in a carbohydrate substrate and for forming modified carbohydrates.

Abstract: The invention provides improved methods of recombinant protein production in cell culture. More specifically, the invention relates to the activation of NF-kappa-B transcription factor complex in cells so as to improve production characteristics.

Abstract: Substantially pure glycosidases capable for cleaving selected glycosidic bonds have been described including glycosidases isolated from Xanthomonas and recombinant glycosidases. Substrate specificity of isolated enzymes have been identified for GlcNac&bgr;1-X, Gal&agr;1-3R, Gal&agr;1-6R, Gal&bgr;1-3R, Fuc&agr;-2R, Fuc&agr;1-3R, Fuc&agr;1-4R, Man&agr;1-2R, Man&agr;1-3R, Man&agr;1-6R, Man&bgr;1-4R, Xyl&bgr;1-2R, Glc&bgr;1-4R, and Gal&bgr;1-4R providing improved capability for selectively cleaving a glycosidic linkage in a carbohydrate substrate and for forming modified carbohydrates.

Abstract: Substantially pure glycosidases capable for cleaving selected glycosidic bonds have been described including glycosidases isolated from Xanthomonas and recombinant glycosidases. Substrate specificity of isolated enzymes have been identified for GlcNac&bgr;1-X, Gal&agr;1-3R, Gal&agr;1-6R, Gal&bgr;1-3R, Fuc&agr;1-2R, Fuc&agr;1-3R, Fuc&agr;1-4R, Man&agr;1-2R, Man&agr;1-3R, Man&agr;1-6R, Man&bgr;1-4R, Xyl&bgr;1-2R, Glc&bgr;1-4R, and Gal&bgr;1-4R providing improved capability for selectively cleaving a glycosidic linkage in a carbohydrate substrate and for forming modified carbohydrates.

Abstract: Purified N-acetylglucosaminidase and .alpha.1-3,6 Galactosidase endogenous to Xanthomonas have been described. Substrate specificity of isolated enzymes have been identified from GlcNAc.beta.1-x and Gal.alpha.1-3R, Gal.alpha.1-6R, providing improved capability for selectively cleaving a glycosidic linkage in a carbohydrate substrate and for forming modified carbohydrates.

Abstract: The present invention relates to a method for cloning and expressing an exogenous phosphorylation-dependent protein kinase in E. coli, and in particular to the co-expression of one or more components of a signal-transduction pathway in E. coli.