Relationship Proteases - Transglutaminases

Transglutaminases catalyze the acyl-transfer reaction between a γ-carboxamide group of glutamine and the ε-amino group of lysine, which results in the formation of isopeptide bonds. Human transglutaminases possess a catalytic triad and the reaction proceeds via a reactive intermediate linked to the nucleophilic cysteine of the enzyme. The mechanism is similar to the proteolysis reaction catalyzed by thiol proteases that posses the same catalytic triad. It turned out that transglutaminases are using a similar structural architecture as papain-like thiol proteases and obviously even have an evolutionary relationship.

Also biology and physiology are closely related. E.g. the transglutaminase coagulation factor XIIIa cross-links fibrin and therefore plays an important role in blood clot formation. The serine protease thrombin (T056) activates factor XIII cleaving the activation peptide. Subsequently, plasmin (P012) degrades the fibrin clot. Therefore proteases are important tools in transglutaminase research.

Art. No.
D005 Metalloprotease-Assay-Substance
2 mg
310 €
P003 Prolylendopeptidase from Myxococcus xanthus, recombinant
150 U
370 €
P009 human Pro-Glu-Plasminogen, recombinant
100 µg
415 €
P012 human Plasmin, recombinant
(from Glu-Plasminogen, activated by Urokinase)
100 µg
415 €
P014 Urokinase
1 mg
370 €
P016 Tissue Plasminogen Activator, t-PA
100 µg
370 €
T004 Plasmin substrate Tosyl-GPKpNA, chromogenic
N-(p-Tosyl)-Gly-Pro-Lys-pNA acetate
25 mg
315 €
T056 Human alpha thrombin, highly active
200 U
185 €
T090 Thrombin, recombinant
20 µg
370 €
T091 Prothrombin, recombinant
20 µg
370 €

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