A synthetic peptide corresponding to residues in Human IDO2.
Conjugation:
Unconjugated
Alternative Names:
Indoleamine 2,3-dioxygenase 2 (EC:1.13.11.-), IDO-2, Indoleamine 2,3-dioxygenase-like protein 1, Indoleamine-pyrrole 2,3-dioxygenase-like protein 1, IDO2, INDOL1
Tryptophan is an essential amino acid that is necessary for protein synthesis, serotonin and melatonin biosynthesis and energy production, energy being a product of the catabolism of tryptophan through the kynurenine pathway. The kynurenine pathway has many downstream metabolites which may be a part of physiological or patho-physiological processes. INDOL1 (indoleamine 2,3-dioxygenase-like protein 1) is an enzyme that catalyzes the first step of the kynurenine pathway of tryptophan metabolism. INDOL1 is also known as IDO2 (indoleamine 2,3-dioxygenase 2) and is a 407 amino acid protein that is expressed in various tissues, including liver, small intestine, spleen, placenta, thymus, lung, brain, kidney, colon and dendritic cells. INDOL1 is selectively inhibited by D-1MT (1-methyl-d-tryptophan), which also inhibits IDO (indoleamine 2,3-dioxygenase) and is significant because IDO expression causes suppression of T cell responses to tumors in dendritic cells. The inhibition of INDOL1 by D-1MT suggests a common function in immunomodulation. In the human INDOL1 gene, two single nucleotide polymorphisms have been detected which abolish the enzymatic function of INDOL1.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
IDO2 polyclonal antibody detects endogenous levels of IDO2 protein.
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