Anti-TGase2/TGM2 Antibody

Transglutaminase 2 (TGM2, also written TGase2) is a calcium-dependent, multifunctional enzyme that catalyzes the formation of isopeptide bonds between glutamine and lysine residues in substrate proteins. Beyond its transglutaminase activity, TGM2 functions as a GTP-binding protein, a protein disulfide isomerase, and a scaffold in cell signaling cascades. This unconjugated, affinity-purified reagent is supplied by Antibodies.com as a 100 µl polyclonal antibody raised in rabbit, validated for Western blot and immunohistochemistry on human, mouse, and rat specimens.

The antibody is presented at 1 mg/ml in PBS supplemented with 0.1% sodium azide and 50% glycerol, a cryoprotective formulation that supports storage at -20°C and limits loss of activity across freeze-thaw cycles when the vial is aliquoted before use. As a polyclonal reagent, it recognizes multiple epitopes on the TGM2 polypeptide, which improves signal consistency across varied sample preparations and fixation protocols.

TGM2 is implicated in celiac disease, where it modifies gluten-derived gliadin peptides, and is frequently studied in the context of tumor progression, drug resistance, and fibrosis. Researchers also examine TGM2 in neurodegeneration and in models of wound healing, since the enzyme contributes to extracellular matrix stabilization. The unconjugated format allows direct conjugation to fluorophores, biotin, or enzymes in custom detection workflows.