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| Product Name | GALNTL1, Recombinant, Human, aa27-558 (GALNACT16, GalNAc-T-like protein 1, GALNT16) |
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| Description | Purity ~90% (SDSPAGE). Oglycosylation is a ubiquitous posttranslational modification present in secreted and membranebound proteins. Polypeptide Nacetylgalactosaminyltransferases (GALNTs) catalyze the initial step for Oglycosylation by transferring GalNAc to Thr or Ser residues (GalNAc alpha 1OSer/Thr) in the Golgi compartment. Structurally, the GALNTs consist of an Nterminal catalytic domain tethered by a short linker to a Cterminal ricinlike lectin domain containing three potential carbohydratebinding sites (1, 2). Twenty distinct GALNT isoforms have been detected in humans. These isoforms display both unique and overlapping substrate specificities (3, 4, 5) with no known universal consensus glycosylation sequence. Glycosylation of mucins results from the successive, often hierarchical, action of several specific GALNTs (6). GALNTL1 is active toward nonglycosylated peptides as well as some glycosylated peptides and is widely expressed in most tissues, especially high in |
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| Size | 20ug |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | n/a |
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| Gene, Accession, CAS # | SwissProt: Q8N428 |
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| Catalog # | 145793 |
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| Order / More Info | GALNTL1, Recombinant, Human, aa27-558 (GALNACT16, GalNAc-T-like protein 1, GALNT16) from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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