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    >> Transglutaminases

    Transglutaminases (TGases), also named protein-glutamine γ-glutamyltransferases, are enzymes belonging to the proteases class that catalyze Ca2+-dependent post-translational modifications of proteins by introducing protein cross-links, amine incorporation, and site-specific deamidation.

    TGases are involved in diverse physiological and physiopathological processes, such as neurodegenerative diseases, blood coagulation disorders, bone tissue healing, growth regulation, cell differentiation, and tissue stabilization. TGases are also considered to play an important role in allergies prevention.

    • Microbial Transglutaminase

    TGases are widely distributed in nature, being found in mammalian, plants, microorganisms, etc. Since its isolation from streptomyces mobaraensis in 1989, TGase production has been discovered in a variety of other microorganisms. Compared to the eukaryotic TGases, bacterial TGases (BTG or synonymous MTG for microbial transglutaminase) possess obvious advantages such as small size, cofactor independence, improved performance, high stability, and low deamination activity. Therefore, they have become one of the most frequently used tools for site-specific bioconjugation.

    In biotechnology and pharmaceutical research, the ability of MTG to catalyze protein cross-linkage is used to produce stable conjugates composed of a variety of functional biomolecules and to immobilize desired payloads onto different surfaces. In biotechnological applications, the usage of highly purified MTG is recommended to avoid the disturbing side reactions of impurities.

    In addition, MTG is applied in the food industry as food additives and in wool textiles as biopolymers. Convenient MTG assay kits are developed for quality control in industry and academia.

    • Mammalian Transglutaminase

    In mammals, nine isoenzymes of the TGase family have been identified at the genomic level with a good structural homology. The best characterized enzymes include:

    TGase 1, also known as keratinocyte transglutaminase, is primarily expressed in epithelial tissues in membrane-bound and soluble forms and is activated by proteolysis upon terminal differentiation of keratinocytes.

    Class Cat. No. Product Name Source Inquiry
    TGase 1 (Human) T009 Human keratinocyte transglutaminase E. coli Inquiry >
    T035 Human keratinocyte transglutaminase Insect cells Inquiry >

    TGase 2, also known as tissue transglutaminase, is the most comprehensively studied and ubiquitous transglutaminase. TGase 2 has both catalytic as well as noncatalytic functions and is associated with several diseases, among which it is best known for its association with celiac disease.

    TGase 3, also named epidermal transglutaminase, is expressed as an inactive zymogen that must undergo proteolytic processing to be activated. Like TGase 1, TGase 3 is also involved in the terminal differentiation of the keratinocyte.

    Class Cat. No. Product Name Source Inquiry
    TGase 3 T013 Human epidermal transglutaminase, Dispase activated Insect cells Inquiry >
    T024 Human epidermal transglutaminase Insect cells Inquiry >

    TGase 4 is exclusively expressed in the prostate and is involved in semen coagulation, essential for fertility in rodents.

    TGase 5 is expressed in the epidermal granular cells, where it cross-links a variety of structural proteins in the terminal differentiation of the epidermis to form the cornified cell envelope.

    TGase 6 encoded by the TGM6 gene is associated with central nervous system development and motor function.

    Class Cat. No. Product Name Source Inquiry
    TGase 4 T042 Human prostate Transglutaminase E. coli Inquiry >
    TGase 5 T086 Human Transglutaminase 5 E. coli Inquiry >
    TGase 6 T021 Human neuronal transglutaminase Insect cells Inquiry >
    TGase 7 T011 Human transglutaminase 7 E. coli Inquiry >
    • Human Factor XIII

    Factor XIII, also known as the fibrin stabilizing factor, is one of the best-known TGases in human blood. Factor XIII is a key clotting factor in the coagulation cascade known for forming cross-links of fibrin molecules and stabilizing fibrin polymers to help stop the bleeding. Deficiency of Factor XIII causes hemostatic problems (even life-threatening bleeding), poor wound healing, and tissue repair. Recombination Factor XIII has been developed as the substitutive therapy at rare genetic defects of blood coagulation.

    Factor XIII is a protein tetrameric complex of A and B subunits. The A subunit (FXIII-A) is a transglutaminase zymogen. The B subunit (FXIII-B) is an inhibitory glycoprotein with no enzymatic function that protects the catalytic A subunits from clearance.

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