Recombinant human IL-4I1 protein

IL-4I1, also known as FIG1, is a secreted L-amino-acid oxidase that acts as a key immunoregulator. It is highly expressed in primary metastinal B-cell lymphomas. This protein acts as a negative regultaotr of anti-tumor immunity by mediating Trp degradation via ans indole pyruvate pathway that activates the transcription factor AHR. IL-4I1-mediated Trp catabolism generates I3P, giving rise to indole metabolites and kynurenic acid, which act as ligands for AHR, a ligand-activated transcription factor that plays important roles in immunity and cancer. IL-41I also regulates M2 macrophage polarization by inhibiting T-cell activation and has antibacterial properties by inhibiting growth of Gram negative and Gram positive bacteria through the production of NH4+ and H2O2. Recombinant human IL-4I1, fused to His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques.