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Your Position: Casa > Protein > IDO1 > ID1-H5143

Human IDO1 Protein, His Tag (active enzyme, MALS verified)

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  • Synonym
    IDO, IDO-1, INDO
  • Source
    Human IDO1 Protein, His Tag(ID1-H5143) is expressed from E. coli cells. It contains AA Ala 2 - Gly 403 (Accession # P14902-1).
    Predicted N-terminus: Met
  • Molecular Characterization
    IDO1 Structure

    This protein carries a polyhistidine tag at the N-terminus.

    The protein has a calculated MW of 47.2 kDa. The protein migrates as 45-50 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >90% as determined by SDS-PAGE.

  • Formulation

    Supplied as 0.2 μm filtered solution in 20 mM Tris, 300 mM NaCl, pH7.5 with glycerol as protectant.

    Contact us for customized product form or formulation.

  • Shipping

    This product is supplied and shipped with dry ice, please inquire the shipping cost.

  • Storage

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. The product MUST be stored at -70°C or lower upon receipt;
    2. -70°C for 3 months under sterile conditions.
SDS-PAGE
IDO1 SDS-PAGE

Human IDO1 Protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90% (With Star Ribbon Pre-stained Protein Marker).

SEC-MALS
IDO1 MALS images

The purity of Human IDO1 Protein, His Tag (Cat. No. ID1-H5143) is more than 85% and the molecular weight of this protein is around 40-60 kDa verified by SEC-MALS.

Bioactivity

Measured by its ability to oxidize L-tryptophan to N-formyl-kynurenine.The specific activity is >400 pmol/min/μg(QC tested).

  • Background
    This gene encodes indoleamine 2,3-dioxygenase (IDO) - a heme enzyme that catalyzes the first and rate-limiting step in tryptophan catabolism to N-formyl-kynurenine. This enzyme acts on multiple tryptophan substrates including D-tryptophan, L-tryptophan, 5-hydroxy-tryptophan, tryptamine, and serotonin. This enzyme is thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation, and antioxidant activity. Through its expression in dendritic cells, monocytes, and macrophages this enzyme modulates T-cell behavior by its peri-cellular catabolization of the essential amino acid tryptophan.
  • Clinical and Translational Updates

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  • Latest Research Phase:Phase 3 Clinical

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