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β1 4 galactosidase

Manufactured by Merck Group
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β1,4-galactosidase is an enzyme that catalyzes the hydrolysis of β-1,4-galactosidic linkages in various substrates. It is commonly used in laboratory settings for the analysis and modification of carbohydrates and glycosides.

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Lab products found in correlation

Papain, by Thermo Fisher Scientific (2 mentions) Neuraminidase, by New England Biolabs (2 mentions) Pngase f, by New England Biolabs (2 mentions) Endo h, by Promega (1 mentions) Pngase f, by Merck Group (1 mentions)

3 protocols using β1 4 galactosidase

1

Enzymatic Modification of IgG Glycans

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Enzymatic digestion was used to modify glycans as described in the SM. IgG was digested into Fab, F(ab)2, and Fc using IdeS (Genovis) and papain (Thermo Scientific). Glycans were digested with PNGase F (NEB), neuraminidase (NEB), and β1,4-galactosidase (EMD Millipore). G0 Abs were enriched using ECL-agarose beads (Vectors Labs) as described in SM.
Gunn B., Schneider J., Shansab M., Bastian A.R., Fahrbach K., Smith A I.V., Mahan A., Karim M., Licht A., Zvonar I., Tedesco J., Anderson M., Chapel A., Suscovich T., Malaspina D., Streeck H., Walker B.D., Kim A., Lauer G., Altfeld M., Pillai S., Szleifer I., Kelleher N.L., Kiser P.F., Hope T.J, & Alter G. (2016). Enhanced binding of antibodies generated during chronic HIV infection to mucus component MUC16. Mucosal immunology, 9(6), 1549-1558.
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2

Glycosylation Pattern Analysis of UUKV

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To assess the glycosylation pattern of the UUKV glycoproteins, virus stocks purified through a 25% sucrose cushion were denatured and exposed to one of the five following treatments: 1,000 units of endoglycosidase H (Endo H; Promega), 5 units of peptide-N-glycosidase F (PNGase F), 0.005 units of α-2(3, 6, 8, 9)-neuraminidase, 0.003 units of β-1,4-galactosidase, and 0.05 units of β-N-acetylglucosaminidase (all enzymes from Merck Millipore) according to the manufacturer's recommendations. Samples were then analyzed by SDS-PAGE on a 4 to 12% or 10% Bis-Tris NuPAGE Novex gel (Life Technologies) and immunoblotting.
Mazelier M., Rouxel R.N., Zumstein M., Mancini R., Bell-Sakyi L, & Lozach P.Y. (2016). Uukuniemi Virus as a Tick-Borne Virus Model. Journal of Virology, 90(15), 6784-6798.
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3

Enzymatic Modification of IgG Glycans

Check if the same lab product or an alternative is used in the 5 most similar protocols
Enzymatic digestion was used to modify glycans as described in the SM. IgG was digested into Fab, F(ab)2, and Fc using IdeS (Genovis) and papain (Thermo Scientific). Glycans were digested with PNGase F (NEB), neuraminidase (NEB), and β1,4-galactosidase (EMD Millipore). G0 Abs were enriched using ECL-agarose beads (Vectors Labs) as described in SM.
Gunn B., Schneider J., Shansab M., Bastian A.R., Fahrbach K., Smith A I.V., Mahan A., Karim M., Licht A., Zvonar I., Tedesco J., Anderson M., Chapel A., Suscovich T., Malaspina D., Streeck H., Walker B.D., Kim A., Lauer G., Altfeld M., Pillai S., Szleifer I., Kelleher N.L., Kiser P.F., Hope T.J, & Alter G. (2016). Enhanced binding of antibodies generated during chronic HIV infection to mucus component MUC16. Mucosal immunology, 9(6), 1549-1558.
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