Transglutaminases (TG) are a family of enzymes that catalyze isopeptide bond formation. This bond formation occurs between the gamma-carboxyamide group of glutamine and various primary amines (primarily the epsilon-amino group of lysine). The resulting intermolecular or intramolecular cross-linking of transglutaminase is highly stable and shows high resistance to proteolytic degradation. The transglutaminase crosslinking activity support the formation of blood clots , skin and hair. On the other hand, TG is now being implicated in Celiac disease as well as in Huntington and Parkinson diseases. Historically, Microbial transglutaminase has been heavily used in the food industry. Microbial TG is often preferred for newer applications (such as site-specific protein modification and antibody drug conjugation) due to its small molecular weight and lack of calcium dependency when compared to the mammalian forms.
Storage: -20C
Application: Microbial Transglutaminase has been used for:• Protein cross-linking & site-specific labeling• Antibody Drug Conjugation• 3D bioprinting bioink preparation • Food related immunogenicity/pathogenicity related research