Mucin-type O-glycans are initiated with an O-GalNAc attachment to a serine or threonine in a polypeptide. The O-GalNAc residues are subsequently extended by various glycosyltransferases resulting in different types of O-glycans. Most O-glycans contain the core 1 structure, Gal beta 1-3GalNAc. GCNT4 is a member of the glucosaminyl (N-acetyl) transferase family and it converts the core 1 O-glycan to core 2 O-glycan, Gal beta 1-3(GlcNAc beta 1-6) GalNAc, via the addition of a GlcNAc residue. Various ligand carbohydrates can be formed from core 2 branched oligosaccharides. For example, sialyl Lex in mucin‑type glycoproteins of blood cells can be formed from core 2 branched oligosaccharides. GCNT4 does not have core 4 O-glycan or I-branching enzyme activity. GCNT4 has been shown to play a role in gastric cancers, where GCNT4 is downregulated and its overexpression prevents cancer cell growth. The activity of the recombinant human GCNT-4 was determined using a phosphatase‑coupled glycosyltransferase assay.
59.9 kDa, under reducing conditions; 62.1 & 122.2 kDa, under non-reducing conditions.
分子类型
蛋白质
产品线
生物产品
储存与运输
物理形态
冻干(Lyophilized)
储存缓冲液
Lyophilized from PBS, pH 7.4.
浓度
见COA
复溶
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 0.5 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
储存条件
-20°C储存,避免反复冻融
运输条件
超低温运输
稳定性与储存
Store at -20℃ for 12 months. Upon reconstitution, it is recommended to aliquot. Avoid freeze/thaw cycle.
图片
Recombinant Human C2GNT3/GCNT4 Protein (rp188463) - SDS-PAGE 3 μg/lane of Recombinant Human Canine CD8 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 59.9 kDa under reducing conditions and 62.1&122.2 kDa under non-reducing conditions. The observation of C2GNT3/GCNT4 Protein as both dimers and monomers under non-reducing (NR) conditions suggests that a portion of the protein forms dimers. This dimerization may be mediated by (or stabilized by) disulfide bonds (Uniprot: Q9P109).
ZJ25F0926713
危险品化学品经营许可证（带存储）