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| Product Name | GALNT10, Recombinant, Human, aa71-603, His-Tag (GalNAc-T10, PPGALNACT10, PPGANTASE10) |
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| Description | Purity ~80% (SDS-PAGE). O-glycosylation is a ubiquitous post-translational modification present in secreted and membrane-bound proteins. Polypeptide N-acetylgalactosaminyltransferases (GALNTs) calalyze the initial step for o-glycosylation by transferring GalNAc to Thr or Ser residues (GalNAc alpha1-O-Ser/Thr) in the Golgi compartment. Structurally, the GALNTs consist of an N-terminal catalytic domain tethered by a short linker to a C-terminal ricin-like lectin domain containing three potential carbohydrate-binding 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). GALNT10 exhibits a single large preference for Ser/Thr-O-GalNAc at the +1 (C-terminal) position relative to the Ser or Thr acceptor site (7) and is ab |
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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: Q86SR1 |
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| Catalog # | 145792 |
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| Order / More Info | GALNT10, Recombinant, Human, aa71-603, His-Tag (GalNAc-T10, PPGALNACT10, PPGANTASE10) from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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