IDO1 / IDO recombinant protein

Recombinant Human IDO1 / IDO Protein

Cat. Num. AAA2545055

• Gene Names: IDO1; IDO; INDO; IDO-1
• Purity: > 91 % as determined by SDS-PAGE
• Synonyms: IDO1 / IDO; Recombinant Human IDO1 / IDO Protein; IDO; IDO-1; INDO; Indoleamine 2; 3-dioxygenase; IDO1 / IDO recombinant protein

• Host: E Coli
• Purity/Purification: > 91 % as determined by SDS-PAGE
• Form/Format: Supplied as sterile 50 mM NaAC, 100 mM Nacl, 20 % glycerol, pH 5.5.
• Sequence Length: 403

• Application Notes: The recombinant human IDO1 consists of 403 amino acids and predicts a molecular mass of 45.2 KDa. It migrates as an approximately 46 KDa band in SDS-PAGE under reducing conditions.
• Source: Human
• Predicted N Terminal: Gly
• Endotoxin: < 1.0 EU per ug of the protein as determined by the LAL method.
• Stability: Samples are stable for up to twelve months from date of receipt at -70°C.
• Molecular Mass: The recombinant human IDO1 consists of 403 amino acids and predicts a molecular mass of 45.2 KDa. It migrates as an approximately 46 KDa band in SDS-PAGE under reducing conditions.
• Reconstitution: Calculated Concentration: 0.55mg/mL; Volume: 37uL.; Concentration is measured by UV-Vis.
• Preparation and Storage: Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted and be used as soon as possible. Avoid repeated freeze-thaw cycles.

SDS-PAGE

Related Product Information for IDO1 / IDO recombinant protein

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 type s. 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.

Description: A DNA sequence encoding the human IDO1 (NP_002155.1) (Ala2-Gly403) was expressed and purified with one additional amino acids (Gly) at the N-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 4504577
• NCBI GeneID: 3620
• NCBI Accession #: NP_002155.1
• NCBI GenBank Nucleotide #: NM_002164.5
• UniProt Accession #: P14902; Q540B4; E5RGR8; F6M9T7
• NCBI Official Full Name: indoleamine 2,3-dioxygenase 1
• NCBI Official Synonym Full Names: indoleamine 2,3-dioxygenase 1
• NCBI Official Symbol: IDO1
• NCBI Official Synonym Symbols: IDO; INDO; IDO-1
• NCBI Protein Information: indoleamine 2,3-dioxygenase 1
• UniProt Protein Name: Indoleamine 2,3-dioxygenase 1
• UniProt Gene Name: IDO1
• UniProt Synonym Gene Names: IDO; INDO; IDO-1

NCBI Description

This gene encodes indoleamine 2,3-dioxygenase (IDO) - a heme enzyme that catalyzes the first and rate-limiting step in tryptophan catabolism to N-formyl-kynurenine. This enzyme acts on multiple tryptophan substrates including D-tryptophan, L-tryptophan, 5-hydroxy-tryptophan, tryptamine, and serotonin. This enzyme is thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation, and antioxidant activity. Through its expression in dendritic cells, monocytes, and macrophages this enzyme modulates T-cell behavior by its peri-cellular catabolization of the essential amino acid tryptophan.[provided by RefSeq, Feb 2011]

Uniprot Description

INDO: Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen. Belongs to the indoleamine 2,3-dioxygenase family.

Protein type: Amino Acid Metabolism - tryptophan; Cell cycle regulation; EC 1.13.11.52; Oxidoreductase

Chromosomal Location of Human Ortholog: 8p11.21

Cellular Component: cytosol

Molecular Function: electron carrier activity; indoleamine 2,3-dioxygenase activity; tryptophan 2,3-dioxygenase activity

Biological Process: female pregnancy; regulation of activated T cell proliferation; tryptophan catabolic process