Human beta -1,3-Glucuronyltransferase 1/B3GAT1 Antibody
Human beta -1,3-Glucuronyltransferase 1/B3GAT1 Antibody Summary
His25-Ile334
Accession # Q9P2W7
Applications
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.
Scientific Data
beta ‑1,3‑Glucuronyltransferase 1/B3GAT1 in SH‑SY5Y Human Cell Line. beta ‑1,3‑Glucuronyltransferase 1/B3GAT1 was detected in immersion fixed SH‑SY5Y human neuroblastoma cell line (positive) and A549 human lung carcinoma cell line (negative control) using Mouse Anti-Human beta ‑1,3‑Glucuronyltransferase 1/B3GAT1 Monoclonal Antibody (Catalog # MAB85601) at 8 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. Staining was performed using our Fluorescent ICC Staining of Cells on Coverslips Protocol.
Reconstitution Calculator
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.
Product Datasheets
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