FGL-1
Fibrinogen-like protein 1 (FGL-1) is a liver-secreted hepatokine of approximately 64 kDa composed of two fibrinogen-like domains joined by disulfide bonds, originally described for its mitogenic effect on hepatocytes and its expression in regenerating liver and liver cancers. FGL-1 came to prominence in immuno-oncology when it was identified by in vivo CRISPR screening as the major functional ligand of LAG-3 (lymphocyte activation gene-3), an inhibitory immune checkpoint receptor on exhausted T cells. FGL-1 binding to LAG-3 suppresses T-cell activation and interferon-γ secretion independent of MHC class II, constituting a tumor immune evasion axis: FGL-1 is overexpressed across many human cancers, plasma levels correlate with poor prognosis and resistance to PD-1 blockade, and genetic or antibody-mediated disruption of the FGL-1-LAG-3 interaction reinvigorates antitumor T-cell responses. FGL-1 also modulates hepatocellular carcinoma growth, liver regeneration and metabolic processes, illustrating a hepatokine repurposed as a checkpoint ligand.
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FGL-1 Recombinant Proteins (18)
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Recombinant Protein Expression Service
- Codon Optimization
- Gene Synthesis
- Construction of Expression Vector
- Strain Screening
- Protein Expression
- Purification & QC
- Protein Delivery
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- Formula: Human
- Molecular Weight: Sf9 insect cells
The EpCAM/TROP1 protein serves as an important homogeneous interacting molecule that promotes direct contact between intestinal epithelial cells (IEC) and intraepithelial lymphocytes (IEL) in the mucosal epithelium. This feature helps establish an immune barrier against mucosal infections. EpCAM/TROP1 Protein, Human (His-SUMO) is the recombinant human-derived EpCAM/TROP1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
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