Recombinant IDO Protein, Human (His Tag) Recombinant Proteins The human IDO1 (P14902-1) (Ala 2-Gly 403) was expressed, with a polyhistide tag at the N-terminus The recombinant human IDO1 consisting of 409a.a and has a calculated molecular weight of 46 kDa. It migrates as an approximately 44 kDa band in SDS-PAGE under reducing conditions.
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Formulation: The recombinant human IDO1 consisting of 409a.a and has a calculated molecular weight of 46 kDa. It migrates as an approximately 44 kDa band in SDS-PAGE under reducing conditions.
Source: E. coli
Usage: Our products are for research use only. This product is not intended or approved for human, diagnostics or veterinary use

Recombinant IDO Protein, Human (His Tag)

Formulation: Recombinant IDO ProteinSupplied as sterile 50mM Tris, 0.15M NaCl, 10% glycerol, pH 8.01

Source: E. coli

Product Name Recombinant IDO Protein, Human (His Tag)
Product Type Recombinant Protein
Source E. coli
Formulation Recombinant IDO ProteinSupplied as sterile 50mM Tris, 0.15M NaCl, 10% glycerol, pH 8.01
Molecular Weight The recombinant human IDO1 consisting of 409a.a and has a calculated molecular weight of 46 kDa. It migrates as an approximately 44 kDa band in SDS-PAGE under reducing conditions.
Purity Greater than 88% as determined by SDS-PAGE
Description The human IDO1 (P14902-1) (Ala 2-Gly 403) was expressed, with a polyhistide tag at the N-terminus
Host Species Homo sapiens (Human)
Usage Our products are for research use only. This product is not intended or approved for human, diagnostics or veterinary use
Storage Store recombinant protein under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
AA Sequence Ala 2-Gly 403
Product Background Indoleamine 2,3-dioxygenase-1, also known as Indoleamine-pyrrole 2,3-dioxygenase, IDO1 and IDO, is a member of the indoleamine 2,3-dioxygenase family. IDO1 / IDO and tryptophan 2,3-dioxygenase (TDO) are tryptophan-degrading enzymes that catalyze the first step in tryptophan catabolism via the kynurenine pathway. TDO is widely distributed in both eukaryotes and bacteria. In contrast, IDO has been found only in mammals and yeast. In 27, a third enzyme, indoleamine 2,3-dioxygenase-2 (IDO2), was discovered. IDO2 is found not only in mammals but also in lower vertebrates. IDO1 / IDO is an immunosuppressive molecule inducible in various cells. IDO1 / IDO catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen. It mediates oxidative cleavage of tryptophan, an amino acid essential for cell proliferation and survival. IDO1 / IDO inhibition is proposed to have therapeutic potential in immunodeficiency-associated abnormalities, including cancer. The IDO pathway is activated in multiple tumor types. Selective inhibition of IDO1 may represent an attractive cancer therapeutic strategy via up-regulation of cellular immunity. IDO1 / IDO is an enzyme that suppresses adaptive T-cell immunity by catabolizing tryptophan from the cellular microenvironment. Inhibition of IDO pathway might enhance the efficacy of immunotherapeutic strategies for cancer.Immune CheckpointImmune Checkpoint Detection: ELISA AntibodiesCo-inhibitory Immune Checkpoint Targets ImmunotherapyCancer ImmunotherapyTargeted Therapy
Memo IDO Protein, Human;IDO-1 Protein, Human;INDO Protein, Human;Indoleamine 2,3‑dioxygenase Protein, Human
Uniprot Number P14902
Terminal Met
Bioactivity Measured by its ability to oxidize L-tryptophan to N-formylk-ynurenine.The specific activity is > 400 pmoles/min/ug.