Human beta-1,3-Glucuronyltransferase 1/B3GAT1 Antibody Summary
Accession # Q9P2W7
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Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
beta ‑1,3‑Glucuronyltransferase 1/B3GAT1 in Human Brain. beta -1,3-Glucuronyltransferase 1/B3GAT1 was detected in immersion fixed paraffin-embedded sections of human brain (cortex) using Mouse Anti-Human beta -1,3-Glucuronyltransferase 1/B3GAT1 Monoclonal Antibody (Catalog # MAB8560) at 5 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC001). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm in neurons. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: beta-1,3-Glucuronyltransferase 1/B3GAT1
B3GAT1 is a key enzyme involved in human natural killer1 (HNK1) epitope synthesis. It adds a glucuronic residue to the terminal lactosamine residue (Gal beta 14GlcNAc) of a glycoprotein or glycolipid, which can be further sulfated to become the HNK1 epitope, a unique trisaccharide structure, HSO3-3GlcA beta 1-3Gal beta 1-4GlcNAc (1, 2). The enzyme activity was found to be enhanced in the presence of sphingomyelin and phosphatidylinositol (3). The HNK1 carbohydrate epitope is characteristically expressed on a series of cell adhesion molecules in addition to some glycolipids in the extracellular matrix and on the cell surface in the nervous system, where it is involved in cell-cell and cell-substratum interaction and recognition during the development of the nervous system (4). Like most known glycosyltransferases, B3GAT1 is a type II Golgi-resident transmembrane protein with a short N-terminal cytoplasmic domain and a single pass transmembrane domain followed by an enzymatic domain in the lumen of Golgi apparatus. The enzyme activity was assayed using a phosphatase-coupled method (5).
- Terayama, K. et al. (1997) Proc. Natl. Acad. Sci. USA 94:6093.
- Shogo, O. et al. (1992) J. Biol. Chem. 267: 22711.
- Kakuda, S. et al. (2005) Glycobiology 2:203.
- Bollensen, E. and Schachner, M. (1987) Neurosci Lett. 82:77.
- Wu, Z.L. et al. (2011) Glycobiology 21:727.
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