Anti-TDO2 / Tryptophan 2,3-dioxygenase

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. TDO2 antibody detects tryptophan 2,3-dioxygenase, a heme-dependent enzyme that catalyzes the first step of the kynurenine pathway, converting L-tryptophan to N-formylkynurenine. The UniProt recommended name is Tryptophan 2,3-dioxygenase (TDO2). This enzyme regulates systemic tryptophan levels and influences serotonin biosynthesis, immune tolerance, and NAD+ metabolism.Functionally, TDO2 antibody identifies a homotetrameric enzyme that incorporates molecular oxygen into the indole ring of tryptophan. The enzyme is predominantly expressed in liver but is inducible in many tumor types. TDO2 activity shapes the immune microenvironment by depleting tryptophan and generating immunosuppressive kynurenine metabolites. This mechanism contributes to tumor immune evasion and cancer progression.The TDO2 gene is located on chromosome 4q32.1 and encodes a 406-amino-acid protein with a conserved heme-binding pocket. Its expression is transcriptionally induced by glucocorticoids, stress, and pro-inflammatory cytokines. Elevated TDO2 levels have been reported in hepatocellular carcinoma, glioblastoma, and melanoma, positioning it as a therapeutic target in oncology. TDO2 also regulates neuroactive tryptophan metabolites implicated in mood disorders and neurodegeneration.Pathologically, upregulation of TDO2 disturbs immune cell proliferation and antigen presentation through depletion of tryptophan and accumulation of kynurenine. Inhibiting TDO2 restores T-cell activity and is an emerging immunotherapeutic strategy complementary to checkpoint blockade. In metabolic studies, altered TDO2 activity links to hepatic inflammation and altered redox homeostasis.TDO2 antibody is widely applied in cancer immunology, metabolism, and neurobiology research. It is suitable for immunoblotting, immunohistochemistry, and enzyme assays detecting TDO2 expression or localization. NSJ Bioreagents supplies high-quality TDO2 antibody reagents validated for use in relevant metabolic and immunological assays.Structurally, tryptophan 2,3-dioxygenase possesses a catalytic heme group coordinated by a proximal histidine. Substrate binding induces conformational changes that enhance dioxygen activation. This antibody supports biochemical and translational studies targeting TDO2 for metabolic modulation and immunotherapy development.