Recombinant Human IDO1 / IDO Protein

  • Catalog number
    PKSH030355-10µg
  • Price
    Please ask
  • Size
    10µg
  • Synonym
    IDO;IDO-1;INDO;Indoleamine 2,3‑dioxygenase
  • Activity
    Measured by its ability to oxidize L-tryptophan to N-formylk-ynurenine.The specific activity is > 500 pmoles/min/μg.
  • Sequence
    Ala2-Gly403
  • Fusion tag
    NA
  • Accession
    NP_002155.1
  • Expressed Host
    E. coli
  • Shipping
    Liquid. It is shipped out with blue ice.
  • Purity
    >85 % as determined by SDS-PAGE
  • Endotoxin
    Please contact us for more information.
  • Stability and Storage
    Samples are stable for up to twelve months from date of receipt at -70℃.Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Mol Mass
    45.2 kDa
  • AP Mol Mass
    46 kDa
  • Formulation
    Lyophilized from sterile 50 mM NaAC, 100 mM Nacl, 20 % glycerol, pH 5.5
  • 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 2007, 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 Immunotherapy   Cancer Immunotherapy   Targeted Therapy
  • Properties
    Human proteins, cDNA and human recombinants are used in human reactive ELISA kits and to produce anti-human mono and polyclonal antibodies. Modern humans (Homo sapiens, primarily ssp. Homo sapiens sapiens). Depending on the epitopes used human ELISA kits can be cross reactive to many other species. Mainly analyzed are human serum, plasma, urine, saliva, human cell culture supernatants and biological samples.
  • Source
    Recombinants or rec. proteins
  • Group
    recombinants
  • Gene target
    IDO1   IDO   Protein  
  • Gene symbol
    IDO1
  • Short name
    Recombinant IDO1 / IDO Protein
  • Technique
    Recombinant, E. coli recombinant proteins are genetic recombinations in Escherichia coli, supplied as white sterile powder lyopillized. Elabscience advises they will be reconstituted in a buffer soluion or culture medium for cell culture.
  • Species
    Human, Humans
  • Alternative name
    Rec. H. sapiens indoleamine 2,3-dioxygenase 1 / Indoleamine 2,3-dioxygenase 1 Protein
  • Alternative technique
    rec
  • Alternative to gene target
    indoleamine 2,3-dioxygenase 1, IDO and IDO-1 and INDO, IDO1 and IDBG-18750 and ENSG00000131203 and 3620, tryptophan 2, Cytoplasm, Ido1 and IDBG-142448 and ENSMUSG00000031551 and 15930, BT.19792 and IDBG-629572 and ENSBTAG00000020602 and 506281
Gene info
MeSH Data
  • Name
  • Concept
    Scope note: The initial culturing of cells derived directly from fresh TISSUES.
  • Tree numbers
    • E01.370.225.500.223.500
    • E05.200.500.265.500
    • E05.242.223.500
    • E05.481.500.249.500
  • Qualifiers
    ethics, trends, veterinary, history, classification, economics, instrumentation, methods, standards, statistics & numerical data
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