SAE0096
IDO1, human
recombinant, expressed in E. coli, lyophilized powder, His tagged
Sinónimos:
Indoleamine 2,3-dioxygenase 1
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About This Item
Productos recomendados
recombinant
expressed in E. coli
form
lyophilized powder
specific activity
800 units/μg
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
General description
IDO1 is a heme-enzyme that is induced by INF-γ and catalyzes the conversion of tryptophan to kynurenine. This leads to a depletion of tryptophan that results in T cells and dendritic cells inactivation. IDO activity has been identified as an important immune effector pathway in tumor cells to escape a potentially effective immune response. Inhibition of IDO1 has been found to delay cancer growth and enhance dendritic vaccines. Therapeutic inhibition of IDO1 is of interest because of its proposed role in the pathogenesis of several diseases, including cancer, hypotension, neurodegenerative disorders, and its potential to aid cancer immunotherapy and organ transplant.
This recombinant human IDO1 has a 6x histidine tag at its N-terminus. This product is lyophilized from a solution containing 10 mM Trizma buffer (pH 7.0), with 500 mM NaCl and a carbohydrate carrier.
Unit Definition
One unit of enzyme hydrolyzes 1.0 pmole of L-Tryptophan to N-formyl-Lkynurenine per minute at pH-6.5 at 37°C
Storage Class
11 - Combustible Solids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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Immune-modulating enzyme indoleamine 2,3-dioxygenase is effectively inhibited by targeting its apo-form
Nelp, M.T. et al.
Proceedings of the National Academy of Sciences of the USA, 115(13), 3249-3254 (2018)
Indoleamine 2,3-dioxygenase: is it an immune suppressor?
Sollman, H. et al.
Cancer Journal, 16(4), 354-359 (2010)
Human bone marrow stromal cells inhibit allogeneic T-cell responses by indoleamine 2,3-dioxygenase-mediated tryptophan degradation.
Meisel, R. et al.
Blood, 103(12), 4619-4621 (2004)
Ji-Hee Shin et al.
European journal of nutrition, 59(8), 3591-3601 (2020-02-15)
Growing evidence shows that nutrient metabolism affects inflammatory bowel diseases (IBD) development. Previously, we showed that deficiency of indoleamine 2,3-dioxygenase 1 (Ido1), a tryptophan-catabolizing enzyme, reduced the severity of dextran sulfate sodium (DSS)-induced colitis in mice. However, the roles played
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