Proteases_ZEDIRA - 코아사이언스

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Proteases

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Relationship Proteases - Transglutaminases

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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 possess the same catalytic triad. Transglutaminases use a similar structural architecture as papain-like thiol proteases and even have an evolutionary relationship.

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The biology and physiology of these enzymes are closely related. For example, 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.

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Cat. No.	Name	Unit
D005	Metalloprotease-Assay-Substance DABCYL-Ser-Phe-EDANS	2 mg
D017	Thrombin-Assay Substance, fluorescent	10 mg
P003	Prolylendopeptidase from Myxococcus xanthus, recombinant	150 U
P012	human Plasmin, recombinant (from Glu-Plasminogen, activated by Urokinase)	100 µg
T004	Plasmin substrate Tosyl-GPKpNA, chromogenic N-(p-Tosyl)-Gly-Pro-Lys-pNA acetate	25 mg
T056	Human alpha thrombin, highly active	2x 100 U
Z020	Thrombin-Generation-Assay Substance, fluorescent	25 mg

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