mProX™ Human IDO1 Stable Cell Line
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- Membrane Protein Stable Cell Lines
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Published Data
Fig.1 Knockdown of IDO1 by siRNA in SKOV-3 cells.
The IDO1 protein expression in SKOV-3 cells was assessed through Western blot analysis, wherein siRNA-mediated knockdown of IDO1 was performed and compared to control samples.
Ref: Opitz, Christiane A., et al. "The indoleamine-2, 3-dioxygenase (IDO) inhibitor 1-methyl-D-tryptophan upregulates IDO1 in human cancer cells." PloS one 6.5 (2011): e19823.
Pubmed: 21625531
DOI: 10.1371/journal.pone.0019823
Research Highlights
Q Trinh, Jonathan. et al. "Durable and dramatic response to checkpoint inhibition combined with COX-2 inhibitor celecoxib in a patient with p16+ metastatic sinonasal undifferentiated carcinoma: A case study." Cancer reports (Hoboken, N.J.), 2023.
Sinonasal undifferentiated carcinoma (SNUC) is a rare form of head and neck malignancy. Its treatment for metastatic disease remains controversial, as no established consensus has been reached. This type of cancer has a high mortality rate and limited treatment options, making it a challenging condition for clinicians to manage. The unique characteristics and unpredictable behavior of SNUC require further research and investigation to improve outcomes for patients with this disease.
Q Trinh, Jonathan. et al. "Durable and dramatic response to checkpoint inhibition combined with COX-2 inhibitor celecoxib in a patient with p16+ metastatic sinonasal undifferentiated carcinoma: A case study." Cancer reports (Hoboken, N.J.), 2023.
Pubmed:
37867289
DOI:
10.1002/cnr2.1915
Singh, Rahul. et al. "Imidazo[2,1-b]thiazole Based Indoleamine-2,3-dioxygenase (IDO)-1 Inhibitor: Structure Based Design, Synthesis, Bio-evaluation and Docking Studies." Bioorganic & medicinal chemistry letters, 2023.
Indoleamine-2,3-dioxygenase 1 (IDO1) is an immunomodulatory enzyme that regulates the kynurenine pathway of L-tryptophan metabolism. It is associated with the progression of cancer, malaria, multiple sclerosis, and other life-threatening diseases. Researchers have dedicated significant efforts over the last two decades to discover IDO1 inhibitors. The plasticity of the IDO1 enzyme's ligand binding pocket offers potential for developing new heterocyclic scaffolds targeting this enzyme. Using the X-ray crystal structure of human IDO1 and coordinating it with various ligands, the authors synthesized new fused heterocyclic compounds. These compounds (30 and 41) showed potential human IDO1 inhibitory activity with IC50 values of 63 nM and 85 nM, respectively.
Singh, Rahul. et al. "Imidazo[2,1-b]thiazole Based Indoleamine-2,3-dioxygenase (IDO)-1 Inhibitor: Structure Based Design, Synthesis, Bio-evaluation and Docking Studies." Bioorganic & medicinal chemistry letters, 2023.
Pubmed:
37866714
DOI:
10.1016/j.bmcl.2023.129532