This is an abbreviated version! For detailed information about alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, go to the full flat file.
construction of a vector including the N-terminally FLAG (DYKDDDDK)-tagged lumenal region (Leu27eAla498) including the stem domain and the catalytic domain of BmGnTII together with a signal peptide sequence from bombyxin and transformed into Escherichia coli BmDH10Bac-CP--Chi- competent cells, which contain the cysteine protease- and chitinase-deficient BmNPV bacmid. RT-PCR expression analysis. The cDNA templates are synthesized from total RNAs extracted from whole bodies of first to fifth-instar larvae and pupa and tissues of fifth-instar larvae. Tissues used are as follows: fat body, midgut, silk gland, epidermis, and Malpighian tubule. To produce the soluble form of BmGnTII n hemolymph, chitosan/BmNPV bacmid nanocomplexes are prepared and then injected into fifth-instar silkworm larvae. The bacmid-injected larvae are reared on an artificial diet
construction of a vector including the N-terminally FLAG (DYKDDDDK)-tagged lumenal region (Leu27eAla498) including the stem domain and the catalytic domain of BmGnTII together with a signal peptide sequence from bombyxin and transformed into Escherichia coli BmDH10Bac-CP--Chi- competent cells, which contain the cysteine protease- and chitinase-deficient BmNPV bacmid. RT-PCR expression analysis. The cDNA templates are synthesized from total RNAs extracted from whole bodies of first to fifth-instar larvae and pupa and tissues of fifth-instar larvae. Tissues used are as follows: fat body, midgut, silk gland, epidermis, and Malpighian tubule. To produce the soluble form of BmGnTII n hemolymph, chitosan/BmNPV bacmid nanocomplexes are prepared and then injected into fifth-instar silkworm larvae. The bacmid-injected larvae are reared on an artificial diet
MGAT2 catalytic domain expression construct (residues 29-447) is generated by replacement of the NH2-terminal membrane anchor with a fusion peptide cassette to target the secretion of the recombinant fusion protein product in mammalian cells
MGAT2 catalytic domain expression construct (residues 29-447) is generated by replacement of the NH2-terminal membrane anchor with a fusion peptide cassette to target the secretion of the recombinant fusion protein product in mammalian cells
gene replacement strategy is used to create TbGT15 null mutant cells and subsequent insertion of tetracycline-inducible ectopic copy. Constructs for gene replacement and ectopic expression are stably transformed into Trypanosoma brucei bloodstream form cells (strain 427, variant 221). Mouse infectivity studies with wild-type and TbGT15 null mutant bloodstream form trypanosomes. No morphological differences between the wild-type and TbGT15 null mutant parasites are ascertained by light microscopy or by scanning electron microscopy. Compared with wild-type cells, the TbGT15 null mutant parasites exhibit slightly slower growth kinetics in vitro, and this mild growth phenotype is partially reversed in TbGT15 conditional null cells grown under permissive conditions. In addition, no difference in its ability to infect mice can be detected for the TbGT15 null mutant. Mutant phenotype, overview
gene replacement strategy is used to create TbGT15 null mutant cells and subsequent insertion of tetracycline-inducible ectopic copy. Constructs for gene replacement and ectopic expression are stably transformed into Trypanosoma brucei bloodstream form cells (strain 427, variant 221). Mouse infectivity studies with wild-type and TbGT15 null mutant bloodstream form trypanosomes. No morphological differences between the wild-type and TbGT15 null mutant parasites are ascertained by light microscopy or by scanning electron microscopy. Compared with wild-type cells, the TbGT15 null mutant parasites exhibit slightly slower growth kinetics in vitro, and this mild growth phenotype is partially reversed in TbGT15 conditional null cells grown under permissive conditions. In addition, no difference in its ability to infect mice can be detected for the TbGT15 null mutant. Mutant phenotype, overview