2. Signaling Pathways
  3. Metabolic Enzyme/Protease
  4. Transglutaminase

Transglutaminase

转谷氨酰胺酶

Transglutaminases are Ca²⁺-dependent enzymes that catalyze post-translational modifications of proteins by deamidation, transamidation, or esterification, transferring the γ-carboxamide group of protein-bound L-glutamine to primary amines. The transglutaminase superfamily includes TGM1-7 and Factor XIIIA, with Transglutaminase 2 (TG2), also known as tissue transglutaminase (tTG), being the most abundant and extensively studied member. TG2 plays diverse roles across tissues and is highly expressed in the liver and cytosol, while other isoforms exhibit tissue-specific expression: TG1, TG3, and TG5 in epithelial tissues; TG4 in the prostate gland; Factor XIII (FXIII) in blood; TG6 in the brain, lungs, and testis; and TG7 predominantly in the testis and lungs. TG2 has been implicated in a wide range of human diseases, including preeclampsia, hypertension, cardiovascular disease, organ fibrosis, cancer, neurodegenerative disorders such as Alzheimer's disease, and celiac disease, where it acts as a key autoantigen. This enzyme family’s functional diversity and pathological relevance make it a critical focus for therapeutic research[1][2].

Transglutaminase Related Products (1):

Cat. No. Product Name Effect Purity Chemical Structure
  • HY-E70393H
    Human Factor XIIIa
    Human Factor XIIIa is a transglutaminase, which catalyzes the cross-linking of proteins and stabilizes the blood clots. Human Factor XIIIa protects the clots from degradation by fibrinolytic enzymes, which is important for maintaining hemostasis and preventing excessive bleeding.
    Human Factor XIIIa