Description
Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig. Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site aa eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins.
Recombinant protein corresponding to the N-terminal region of human Tissue Transglutaminase, expressed in HEK 293-EBNA cell line, fused to His-Tag