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Merck

SAE0096

Sigma-Aldrich

IDO1, human

recombinant, expressed in E. coli, lyophilized powder, His tagged

Sinónimos:

Indoleamine 2,3-dioxygenase 1

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About This Item

Comisión internacional de enzimas:
UNSPSC Code:
12352202
NACRES:
NA.26

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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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)
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)

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