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Overview
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Transglutaminases are able to also cleave the isopeptide bond. This principle is used to provide easy to handle, robust and precise fluorogenic assays suitable for screening of compound libraries and drug development. Further, it reliably detects levels as low as 5% of the physiological amount of FXIIIa (0.05 IU/ml) in plasma (Oertel et al., Anal. Biochem. 2007, 367:152-8).
Mechanism: transglutaminase cleaves the isopeptide bond releasing the dark quencher (2,4-dinitrophenyl) linked to the cadaverine spacer. Subsequently, the increase of fluorescence results from the N-terminally attached fluorophore 2-aminobenzoyl (2-Abz).Please contact us at for specific academic pricing.
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- Properties
- Applications
- Reference
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Overview