General descriptionTransglutaminases (TG) are a family of enzymes that catalyze isopeptide bond formation. This bond formation occurs between the γ-carboxyamide group of glutamine and various primary amines (primarily the ε-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.
ApplicationMicrobial Transglutaminase has been used for:
- Protein cross-linking & site-specific labeling
- Antibody Drug Conjugation
- 3D bioprinting bioink preparation
- Food related immunogenicity/pathogenicity related research
Features and Benefits- Small (~38kDa) and calcium independent enzyme
- Highly purified lyophilized enzyme
- Consistent and reproducible activity
- Characterized for endotoxin content
Preparation NoteFor R&D use only. Not for drug, household, or other uses. Please consult the Safety Data Sheet for information regarding hazards and safe handling practices
Store the freeze-dried product at –20 °C. It is recommended to store the reconstituted protein in working aliquots at –20 °C to avoid repeated freeze/ thaw cycles.
