Inconclusive results, intact N-terminus verified by anti-poly-His Western
>80%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane
<1.0 EU per 1 μg of the protein by the LAL method.
51 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Kynurenine 3-monooxygenase (KMO), also known as kynurenine 3-hydroxylase, is a part of the kynurenine pathway of tryptophan degradation (1). KMO catalyzes the NADPH- and flavin adenine dinucleotide (FAD)-dependent 3-hydroxylation of kynurenine to 3-hydroxykynurenine (3-HK). 3-HK is neurotoxic via the generation of hydrogen peroxide (2) and through the excitotoxic effects of its downstream metabolite quinolinic acid (3). The levels of 3-HK and quinolinic acid are increased in the brain with Alzheimer's disease and Huntington's disease (1). Inhibition of KMO was shown to reverse cognitive and motor deficits in mouse models of those diseases via an increase in neuroprotective kynurenic acid (4). KMO is found in the mitochondrial outer membrane of microglial cells in the brain and dendritic cells and macrophages in the periphery (1). This recombinant human KMO was expressed as a C-terminally truncated protein.
Schwarcz, R. et al. (2012) Nat. Rev. Neurosci. 13:465.
Okuda, S. et al. (1996) Proc. Natl. Acad. Sci. 93:12553.
Stone, T.W. and M.N. Perkins. (1981) Eur. J. Pharmacol. 72:411.
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