Lacto-N-biosidase

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.

Cat. #	Product	Size	Price	License	Quantity	Details
4456	Lacto-N-biosidase	100 uU	USD $700.00
This enzyme specifically hydrolyzes oligosaccharides with type I chains and produces lacto-N-biose (Galb-3GlcNAc). It does not hydrolyze oligosaccharides with type II chain. The structure of the substrate essential for the enzyme activity is the terminal lacto-N-biosyl residue (Galb1-3GlcNAc). The enzyme does not hydrolyze a 2,3-sialyllacto-N-tetraose, lacto-N-fucopentaose I and II. One vial of this product (100 μl) allows 50–100 reactions of enzyme digestion of sugar chain up to 10 pmol. Notice to purchaser Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval. Documents Components Image Data Back 4456: Lacto-N-biosidase

More Information

Applications

Specific hydrolysis of oligosaccharides with type-I sugar chains and production of byproduct lacto-N-biose (Gal β 1-3 GlcNAc)

Source

Streptomyces sp. 142

Storage

–20°C

Properties

Concentration: 1 µU/µl
Molecular weight: 60 kDa (SDS-PAGE)
K_m (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.)

Form

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.

References

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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