- Purification products
- Two-hybrid and one-hybrid systems
- Mass spectrometry reagents
- Expression vectors & systems
- Antibodies and immunoprecipitation
- SDS-PAGE & western blotting
- Protein sequencing
- Accessory enzymes
Lacto-N-biosidase may be used during glycoprotein analysis to better study the structure and function of glycoprotein and glycolipid sugar chains. This product can be used for specific oligosaccharide hydrolysis of type-I chain oligosaccharides, producing lacto-N-biose (Gal β 1-3 GlcNAc) as a byproduct, but not oligosaccharide hydrolysis of type-II chain oligosaccharides. As a result, Lacto-N-biosidase can be used to distinguish type-I versus type-II glycoprotein as well as glycolipid sugar chains. When used in conjunction with α-1,3/4-Fucosidase, Lacto-N-biosidase can also help distinguish Sialyl-Lewis x and Sialyl-Lewis α structures.
One vial of Lacto-N-biosidase (100 µU) allows 50–100 enzymatic digestions of up to 10 pmol of sugar chains.
- Specific hydrolysis of oligosaccharides with type-I sugar chains and production of byproduct lacto-N-biose (Gal β 1-3 GlcNAc)
Streptomyces sp. 142
- Concentration: 1 µU/µl
- Molecular weight: 60 kDa (SDS-PAGE)
- Km (substrate): 6.80 µM (Pyridylamino (PA)-lacto-N-tetraose); 38.9 µM (PA-oligosaccharide c)
- Optimum pH: pH 5.5 (sodium citrate buffer, sodium phosphate buffer)
- Range of pH stability: pH 4.0–10 (4°C, 16 hrs.)
Solution in 50 mM sodium acetate buffer, pH 5.5, containing 0.05% Brij-58
Definition of activity
One unit is the amount of enzyme required to hydrolyze 1 µmol of PA-lacto-N-tetraose in 1 minute at 37°C, pH 5.5.
Sano, M., Hayakawa, K. & Kato, I. Purification and characterization of an enzyme releasing lacto-N-biose from oligosaccharides with type 1 chain. J. Biol. Chem. 268, 18560–18566 (1993).
Sano, M., Hayakawa, K. & Kato, I. Purification and characterization of alpha-L-fucosidase from Streptomyces species. J. Biol. Chem. 267, 1522–7 (1992).
Stroud, M. R. et al. Extended type 1 chain glycosphingolipids: Dimeric Lea (III4V4Fuc2Lc6) as human tumor-associated antigen. J. Biol. Chem. 266, 8439–8446 (1991).
Takasaki, S. & Kobata, A. Asparagine-linked sugar chains of fetuin: occurrence of tetrasialyl triantennary sugar chains containing the Gal beta 1—3GlcNAc sequence. Biochemistry 25, 5709–15 (1986).
Townsend, R. R., Hardy, M. R., Wong, T. C. & Lee, Y. C. Binding of N-linked bovine fetuin glycopeptides to isolated rabbit hepatocytes: Gal/GalNAc hepatic lectin discrimination between Gal beta(1,4)GlcNAc and Gal beta(1,3)GlcNAc in a triantennary structure. Biochemistry 25, 5716–5725 (1986).
Additional product information
Please see the product's Certificate of Analysis for information about storage conditions, product components, and technical specifications. Please see the Kit Components List to determine kit components. Certificates of Analysis and Kit Components Lists are located under the Documents tab.
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