UDP-Alpha-d-n-acetylgalactosamine, disodium salt
UDP-Alpha-d-n-acetylgalactosamine, disodium salt structure
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Common Name | UDP-Alpha-d-n-acetylgalactosamine, disodium salt | ||
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| CAS Number | 108320-87-2 | Molecular Weight | 651.31700 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C17H25N3Na2O17P2 | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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Expression of the functional recombinant human glycosyltransferase GalNAcT2 in Escherichia coli.
Microb. Cell Fact. 14 , 3, (2015) Recombinant protein-based therapeutics have become indispensable for the treatment of many diseases. They are produced using well-established expression systems based on bacteria, yeast, insect and mammalian cells. The majority of therapeutic proteins are gly... |
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Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy.
PLoS ONE 9(2) , e99026, (2014) Patients with IgA nephropathy (IgAN) have elevated circulating levels of IgA1 with some O-glycans consisting of galactose (Gal)-deficient N-acetylgalactosamine (GalNAc) with or without N-acetylneuraminic acid (NeuAc). We have analyzed O-glycosylation heteroge... |
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Prediction of functional modules based on comparative genome analysis and Gene Ontology application.
Nucleic Acids Res. 33 , 2822-37, (2005) We present a computational method for the prediction of functional modules encoded in microbial genomes. In this work, we have also developed a formal measure to quantify the degree of consistency between the predicted and the known modules, and have carried ... |
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Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation.
Nat. Commun. 6 , 6937, (2015) Protein O-glycosylation is controlled by polypeptide GalNAc-transferases (GalNAc-Ts) that uniquely feature both a catalytic and lectin domain. The underlying molecular basis of how the lectin domains of GalNAc-Ts contribute to glycopeptide specificity and cat... |