IDO1 (NM_002164) Human Tagged ORF Clone Lentiviral Particle
CAT#: RC206592L1V
- LentiORF®
Lenti ORF particles, IDO1 (Myc-DDK tagged) - Human indoleamine 2,3-dioxygenase 1 (IDO1), 200ul, >10^7 TU/mL
Lentiviral Particles: DDK w/ Puro mGFP mGFP w/ Puro
Specifications
Product Data | |
Type | Human Tagged ORF Clone Lentiviral Particle |
Tag | Myc-DDK |
Symbol | IDO1 |
Synonyms | IDO; IDO-1; INDO |
Mammalian Cell Selection | None |
Vector | pLenti-C-Myc-DDK |
ACCN | NM_002164 |
ORF Size | 1209 bp |
Sequence Data |
The ORF insert of this clone is exactly the same as(RC206592).
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OTI Disclaimer | The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info |
OTI Annotation | This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. |
Reference Data | |
RefSeq | NM_002164.3 |
RefSeq Size | 1944 bp |
RefSeq ORF | 1212 bp |
Locus ID | 3620 |
UniProt ID | P14902 |
Cytogenetics | 8p11.21 |
Protein Families | Druggable Genome |
Protein Pathways | Metabolic pathways, Tryptophan metabolism |
MW | 45.3 kDa |
Gene Summary | 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] |
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