Recombinant Human IDO1/IDO Protein (Gly & Ala2-Gly403) (Active)

Cat. No : CDRP-00152

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Target Information
Target Name	IDO1/IDO
Synonyms	Indole 2; 3-dioxygenase; Indoleamine 2; 3-dioxygenase 1; IDO-1; IDO1; IDO; INDO
UniProt ID	P01258
Accession	P14902-1

Product Details
Expression Host	E.coli
Species	Human
Tag	N-His
Molar Mass	46 kDa
Sequence	Val 20-Thr 547

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.

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.

Properties
Purity	>98% as determined by reducing SDS-PAGE.
Formulation	Supplied as sterile solution of 50 mM Tris, 0.15M NaCl, 10% Glycerol, pH8.0.
Reconstitution	Please refer to the printed manual for detailed information.
Shipping	This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs.
Storage	Store at < -20 °C, stable for 6 months. Please minimize freeze-thaw cycles.

! For research use only. Not intended for any clinical use.