Recombinant Human Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase(ST8SIA3)

Code CSB-CF022776HU
Product Type Transmembrane Protein
Size Pls inquiry other sizes
Uniprot No. O43173
Storage Buffer Tris-based buffer,50% glycerol
Species Homo sapiens (Human)
Sequence MRNCKMARVASVLGLVMLSVALLILSLISYVSLKKENIFTTPKYASPGAPRMYMFHAGFRSQFALKFLDPSFVPITNSLTQELQEKPSKWKFNRTAFLHQRQEILQHVDVIKNFSLTKNSVRIGQLMHYDYSSHKYVFSISNNFRSLLPDVSPIMNKHYNICAVVGNSGILTGSQCGQEIDKSDFVFRCNFAPTEAFQRDVGRKTNLTTFNPSILEKYYNNLLTIQDRNNFFLSLKKLDGAILWIPAFFFHTSATVTRTLVDFFVEHRGQLKVQLAWPGNIMQHVNRYWKNKHLSPKRLSTGILMYTLASAICEEIHLYGFWPFGFDPNTREDLPYHYYDKKGTKFTTKWQESHQLPAEFQLLYRMHGEGLTKLTLSHCA
Source in vitro E.coli expression system
Gene Names ST8SIA3
Protein Names Recommended name: Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R:alpha 2,8-sialyltransferase EC= 2.4.99.- Alternative name(s): Alpha-2,8-sialyltransferase 8C Alpha-2,8-sialyltransferase III ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3 Si
Expression Region 1-380
Tag Info N-terminal 10xHis-tagged
Protein Description full length protein
Storage Store at -20°C, for extended storage, conserve at -20°C or -80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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Function Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto the terminal sialic acid of an acceptor through alpha-2,8-linkages. Is active with alpha-2,3-linked, alpha-2,6-linked and alpha-2,8-linked sialic acid of N-linked oligosaccharides of glycoproteins and glycolipids. Displays preference for substrates with alpha-2,3-linked terminal sialic acid. It can form polysialic acid in vitro directly on alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid.
Subcellular Location Golgi apparatus membrane, Single-pass type II membrane protein
Protein Families Glycosyltransferase 29 family
Tissue Specificity Expressed in fetal and adult brain and fetal liver.
Database Links

HGNC: 14269

OMIM: 609478

KEGG: hsa:51046

STRING: 9606.ENSP00000320431

UniGene: Hs.23172

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