Recombinant Human FGL1 Protein Standard

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Fibrinogen-like protein 1 (FGL1) also known as Hepassocin plays a significant role in modulating immune responses. FGL1 is a member of the fibrinogen family with a molecular mass of approximately 31 kDa. This protein is widely expressed in the liver and is also found in other tissues like the pancreas and lungs. Its structural homology to fibrinogen suggests potential binding capabilities with similar ligands influencing its mechanical actions in cellular processes.

Biological function summary

FGL1 modulates the immune system and maintains its homeostasis. It functions primarily as a ligand for the immune checkpoint receptor LAG-3. This FGL1-LAG-3 interaction inhibits T-cell activity leading to immune tolerance and helping prevent autoimmunity. FGL1 while not a part of a complex demonstrates significant standalone biological activity by affecting immune responses especially under pathological conditions.

Pathways

FGL1 integrates into the immune regulatory framework. It exerts its effects mainly through the immune checkpoint pathway impacting T-cell regulation. In addition to LAG-3 FGL1 interacts closely with the PD-1/PD-L1 pathway which is also important in checkpoint inhibition and immune evasion mechanisms. These pathways together orchestrate the immune surveillance system and play roles in maintaining immune equilibrium.

FGL1 has received attention in cancer particularly in its role of suppressing anti-tumor immunity. Its interaction with LAG-3 makes it a potential target for cancer immunotherapy as high FGL1 levels correlate with poor prognosis in various cancers. Additionally it has implications in autoimmune diseases where its regulation of T-cell activity prevents excessive immune responses. By modulating LAG-3 activity FGL1 emerges as a therapeutic target of interest in autoimmune conditions presenting new opportunities for managing such disorders.