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Transglutaminases are a family of enzymes that catalyze the posttranslational modification of proteins by inserting an isopeptide bond within or between polypeptide chains. Theseenzymes catalyze the acyl transfer reaction between the γ-carboxyamide groups of peptidebound glutamine residues and a variety of primary amines, particularly the ε-amino group of lysine. The resulting crosslink is of great significance, since it is highly stable and also resistant to mechanical and proteolytic degradation.
SourceE. coliTypeRecombinant ProteinsPurification> 95 % (SDS-PAGE)FormulationThe purified transglutaminase is lyophilized from 50 mM NaOAc pH 5.0 + 0.3 M NaCl.StorageStore at –20°C in working aliquots. Repeated freezing and thawing is not recommended. Delivery is possible at ambient temperature.NoteINTENDED FOR RESEARCH USE ONLY, NOT FOR USE IN HUMAN, THERAPEUTIC OR DIAGNOSTIC APPLICATIONS. Process Change Notification: Transfer of the Pro-MTG production protocol from shaker flask to stirred tank fermenter (T001 (MTG) Process Change Notification.pdf).Molecular Weight38,333 Da (Dispase-activated MTG with N-terminal sequence: FRAPDSDDR...)ClassMicrobial (Pro)TGaseReconstitutionAdd the volume of H2O the protein is lyophilized from (see Certificate of Analysis) to the vial of lyophilized powder. Rotate vial gently until solid dissolves.Reconstituted MTG solution might be turbid. However, MTG activity is not affected. In this case, centrifuge the solution and collect the supernatant.After reconstitution, the solution should be stored frozen in working aliquots.
Application DescriptionLabeling, immobilisation, conjugation and modification of proteins.MTG can tolerate up to 10% DMSO in aqueous solutions without significant influence on its catalytic activity. A small activity loss of 4% was observed in the presence of 20% DMSO.
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