Anti-N epsilon gamma glutamyl Lysine antibody [81D4]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The biological target N epsilon gamma glutamyl lysine also known as gamma lysine is a result of an enzymatic reaction where transglutaminase catalyzes the formation of an isopeptide bond between the gamma-carboxamide group of a glutamine and the epsilon-amino group of a lysine. This covalent linkage results in the crosslinking of proteins making them insoluble under physiological conditions. The target exists in various tissues but shows strong expression in areas requiring mechanical stability such as the skin hair and blood clot polymers.

Biological function summary

N epsilon gamma glutamyl lysine plays important roles in cellular stability and structure. It serves as a crosslinking agent helping stabilize protein complexes vital for cellular integrity. These complexes include but are not limited to the extracellular matrix proteins and cytoskeletal structures. This stability conferred by the target ensures the resilience and elasticity of tissues and contributes to processes like wound healing and blood clot formation.

Pathways

N epsilon gamma glutamyl lysine participates in significant biological pathways such as the coagulation cascade and skin barrier formation. The crosslinking alteration affects the stabilization of fibrin an important protein in the coagulation pathway which aids in forming a stable blood clot. It also supports epidermal keratin proteins in the skin formation pathway contributing to the maintenance of the skin barrier. These interactions highlight the target’s critical regulatory roles linking it to proteins like factor XIII and keratin within these pathways.

Associated diseases and disorders

N epsilon gamma glutamyl lysine shows connections to pathologies such as celiac disease and certain types of cancer. The target's role in protein crosslinking implicates it in celiac disease where altered transglutaminase activity leads to inappropriate immune responses. In cancer abnormal crosslinking can affect tissue rigidity and impact tumor development or progression. While other proteins are involved like tissue transglutaminase in celiac disease the modification of N epsilon gamma glutamyl lysine remains a critical aspect of these disorders.