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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of INDOL1 of mouse and human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping near the N-terminus of INDOL1 of human origin
Tissue Specificity
epitope mapping near the N-terminus of INDOL1 of human origin