Microbial Transglutaminase  (Synonyms: MTG; MTGase; Protein-glutamine-γ-glutamyltransferase)

Microbial Transglutaminase (MTG) is a transglutaminase. Enzymes have high catalytic efficiency, high specificity, and mild operating conditions. It can be applied in industries such as pharmaceuticals, industrial production, food manufacturing, and aquaculture^[1].

Product Information
Microbial Transglutaminase (mTGase) is a highly active transglutaminase derived from Streptomyces mobaraensis, recombinantly expressed in Escherichia coli (E.coli). Compared to animal-derived transglutaminases, this enzyme exhibits distinct advantages including smaller molecular weight and calcium-independent catalytic activity. It specifically catalyzes the formation of stable amide bonds between the γ-carboxamide group of glutamine residue at position 295 of deglycosylated antibodies and primary amines in substrates. With no requirement for additional peptide donors, mTGase demonstrates remarkable flexibility by functioning solely through the presence of primary amine groups on target molecules. These properties make it a preferred choice in antibody-drug conjugate (ADC) preparation.

Usage Guidelines (For reference only)
mTGase facilitates the coupling reaction between deglycosylated antibodies and azido-amines. The resulting antibody-azido intermediate can subsequently react with amine-containing drug linkers or reactive linkers to achieve conjugation with deglycosylated antibodies. Enzyme dosage should be optimized based on specific process requirements. Recommended reaction conditions for the azido-amine coupling step are 25°C or 37°C for 16-20 hours (overnight incubation).

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

80146-85-6

Liquid

Colorless to light yellow

[Microbial Transglutaminase]

Shipping with dry ice.

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

• [1]. van Beilen JB, et al. Enzyme technology: an overview. Curr Opin Biotechnol. 2002 Aug;13(4):338-44.  [Content Brief]