Recombinant Human IDO2 Protein (His Tag)

    • Recombinant Human IDO2 Protein (C-His)-Elabscience
    • Recombinant Protein-Elabscience
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    • Recombinant Human IDO2 Protein (C-His)-Elabscience
    • Recombinant Protein-Elabscience
    • Recombinant Human IDO2 Protein (C-His)-Elabscience
    • Recombinant Protein-Elabscience

      Catalog number:PKSH033646

      Synonyms:INDOL1

      Size:
      • 10μg
      • 50μg
      Qty:
      - +
      Price: $328

      Lead Time: Order now, ship in 3 daysWelcome to order from local distributors.

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      Overview

      Synonyms INDOL1
      Species Human
      Expression_host E.coli
      Sequence Met14-Gly420
      Accession Q6ZQW0
      Mol_Mass 46.5 kDa
      AP_Mol_Mass 45 kDa
      Tag C-His

      Properties

      Purity > 95% as determined by reducing SDS-PAGE.
      Endotoxin < 1.0 EU per μg as determined by the LAL method.
      Storage Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
      Shipping This product is provided as liquid. It is shipped at frozen temperature with blue ice.Upon receipt, store it immediately at<-20°C.
      Formulation Supplied as a 0.2 μm filtered solution of 20mM Tris, 10% Glycerol,1mMEDTA,250mM NaCl,pH8.0.
      Reconstitution Please refer to the printed manual for detailed information.

      Background

      Indoleamine 2,3-dioxygenase-like protein 1(IDO2) belongs to the indoleamine 2,3-dioxygenase family. IDO2 can be detected in liver, small intestine, spleen, placenta, thymus, lung, brain, kidney, and colon. It also expressed at low level in testis and thyroid but not expressed in the majority of human tumor samples. IDO2 catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. It involved in immune regulation. IDO1 and IDO2 are 2 distinct enzymes which catalyze the same reaction. IDO2 affinity for tryptophan is much lower than that of IDO1. 50 % of Caucasians harbor polymorphisms which abolish IDO2 enzymatic activity. IDO2 is expressed in human tumors in an inactive form: tryptophan degradation is entirely provided by IDO1 in these cells. IDO2 may play a role as a negative regulator of IDO1 by competing for heme-binding with IDO1. Low efficiency IDO2 enzymes have been conserved throughout vertebrate evolution, whereas higher efficiency IDO1 enzymes are dispensable in many lower vertebrate lineages. IDO1 may have arisen by gene duplication of a more ancient proto-IDO gene before the divergence of marsupial and eutherian (placental) mammals.

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