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Isopeptidase-FluorogenicAssays

Transglutaminases are best known for their crosslinking activity but also can cleave isopeptide bonds. This feature is used to provide easy to handle, robust and precise fluorogenic assays to measure transglutaminase isoenzymes. The assays are suitable for drug discovery programs and quality assurance.

Transglutaminases cleave the carboxamide bond and thereby release the dark quencher (2,4-dinitrophenyl, DNP) linked to a cadaverine spacer. The increase in fluorescence results from the unquenched N-terminally attached fluorophore 2-amino benzoic acid (2-Abz).

 

Assay principle: Cleavage of a carboxamide bond is catalyzed by transglutaminase. The release of the dark quencher is followed by incorporation of glycine methylester. After the dark quencher is released, the fluorescence of the dequenched

2-Abz-dye increases – “the assay directly monitors transglutaminase activity”. The specific backbone provides selectivity and affinity to the assay peptides for the respective TG isoenzyme.

Further, the well-known fluorogenic substrate A101 is not only suitable for FXIII measurement but also for the determination of TG1, TG2, TG3, and TG6.

 

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