Tissue transglutaminase (tTG) is a 75 kDa monomeric globular protein expressed in the majority of cells and tissues. tTG localizes mainly in the cytoplasm but some tGT is present on the cell surface and is association with the extracellular matrix. In addition to its guanosine triphosphatase (GTPase) activity, tTG catalyzes the posttranslational modification of proteins by transamidation of available glutamine residues. Extracellular tTG is able to bind to and cross-link several ECM proteins including FN/Fibronectin and SPP1, and may function to stabilize the ECM and basement membranes. The protein is translated as a fully active enzyme and there is no evidence for proteolytic activation. High constitutive expression and accumulation of active tTG is observed in (among others) endothelial cells, platelets, vascular smooth muscle cells and epithelial cells of the lens. tTG is expressed at very low levels in skeletal muscle cells and neurons and may be difficult to detect in these cell/tissue types.

Optimal dilution of the recombinant Transglutaminase 2 antibody should be determined by the researcher.

Recombinant full-length human protein was used as the immunogen for the recombinant Transglutaminase 2 antibody.

Aliquot the recombinant Transglutaminase 2 antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.