TGM2 Human, Sf9
Description
Tissue Transglutaminase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a molecular mass of 83 kDa. tTG is expressed with a -6xHis tag and purified by proprietary chromatographic techniques. By point mutation of the active center the catalytic transglutaminase activity has been eliminated, resulting in increased stability during storage and coating.
Product Specs
Product Science Overview
Tissue Transglutaminase (tTG), also known as Transglutaminase 2 (TGM2), is an enzyme that plays a crucial role in various biological processes, including apoptosis, cellular differentiation, and extracellular matrix stabilization. It is a member of the transglutaminase family, which catalyzes the formation of covalent bonds between proteins. This enzyme is particularly significant in the context of celiac disease, where it is identified as the primary autoantigen .
Human recombinant tissue transglutaminase is produced using the Sf9 insect cell expression system. The Sf9 cells are derived from the fall armyworm, Spodoptera frugiperda, and are commonly used for the production of recombinant proteins due to their high yield and post-translational modification capabilities. The recombinant tTG produced in Sf9 cells is glycosylated and has a molecular mass of approximately 78,018 Daltons .
The production process involves the insertion of the human TGM2 gene into a baculovirus vector, which is then used to infect the Sf9 cells. The infected cells express the recombinant tTG, which is subsequently purified using chromatographic techniques. The recombinant protein is often tagged with a His-tag to facilitate purification and detection .
Tissue transglutaminase is a multifunctional enzyme with both transamidation and GTPase activities. The transamidation activity involves the formation of isopeptide bonds between glutamine residues and various amine donors, leading to protein cross-linking. This activity is essential for the stabilization of the extracellular matrix and the formation of the cornified envelope in the skin .
The GTPase activity of tTG is involved in signal transduction pathways, where it regulates cellular processes such as apoptosis and cell adhesion. The enzyme’s ability to bind and hydrolyze GTP is crucial for its role in these pathways .
Recombinant tissue transglutaminase has several applications in research and clinical diagnostics. In the context of celiac disease, highly pure recombinant tTG is used to detect autoantibodies in patient sera, providing a sensitive and specific diagnostic tool . Additionally, tTG is used in studies investigating its role in various diseases, including cancer, neurodegenerative disorders, and fibrosis.
The availability of recombinant tTG produced in Sf9 cells offers a reliable and consistent source of the enzyme for these applications. The use of recombinant technology ensures high purity and activity, making it a valuable tool for both basic and applied research .
