Bovin beta-1,4-galactosyltransferase 1 (Y289L)  (Synonyms: Bovin B4GALT1 (Y289L))

Bovin beta-1,4-galactosyltransferase 1 (Y289L) (Bovin B4GALT1 (Y289L)) is a mutated form of bovine-derived galactosyltransferase with a mutation at the Y289L genetic site. Bovin beta-1,4-galactosyltransferase 1 can label O-GlcNAcylated proteins with an N-azidoacetylgalactosamine (GalNAz) group. This labeling method allows for the specific, unbiased, and global labeling of O-GlcNAcylated proteins. After labeling, the appended azide group can react with a wide variety of alkyne-modified chemical probes, facilitating multiple downstream analyses^[1].

Product Information
Bovin B4GALT1(Y289L) is a mutant galactosyltransferase capable of efficiently transferring GalNAc or GalNAz to terminal GlcNAc residues. The latter finds application in antibody-drug conjugates (ADCs) for targeted cancer therapy and other purposes.This product is recombinantly expressed using the HEK293 cell expression system, with a C-terminal His tag. It has a molecular weight of 50.8 kDa and is stored in a buffer consisting of 20 mM Tris-HCl (pH 7.4), 200 mM NaCl, and 20% glycerin.

Instructions
1. Reaction System:
50 mM Tris-HCl (pH 7.5), 6 mM MnCl2
2. Reaction Reagents:
UDP-GalNAz to Antibody Ratio: 300:1 (by equivalent)
Enzyme Addition Amount: Enzyme/antibody = 5%
3. Prepare the reaction solution according to the above conditions, react at 37°C for 48 h, then place at -15~-25°C to stop the reaction and perform sample testing.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

Liquid

Colorless to light yellow

[Bovin beta-1,4-galactosyltransferase 1 (Y289L)]

Bovin

HEK293 cell

C-terminal His Tagged

50.8 kDa

2500 U/mg

One unit is defined as the amount of enzyme that will transfer 1 nmol GalNAz from UDP-GalNAz to

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Thompson JW, et al. Methods for the Detection, Study, and Dynamic Profiling of O-GlcNAc Glycosylation. Methods Enzymol. 2018;598:101-135.  [Content Brief]