NDOR1 Antibodies, cDNA Clones Research Reagents

NDOR1 (NADPH Dependent Diflavin Oxidoreductase 1, also known as NR1; CIAE1), located on 9q34.3, is a Protein Coding gene. The encoded protein catalyzes the transfer of electrons from NADPH through FAD and FMN cofactors to potential redox partners. The predicted 597-amino acid, 62-kD NR1 protein shares 41 to 44% sequence similarity with nitric oxide synthase-2, methionine synthase transferase, and POR. NDOR1 may play a role in the metabolic activation of bioreductive anticancer drugs and other chemicals activated by 1-electron reduction.

NDOR1 Antibody (1)

    NDOR1 cDNA Clone (15)

    BC015735

    クローニングベクター cDNA 製品

    In lentiviral vector

    NDOR1 qPCR Primer (1)

    NDOR1 の背景知識

    NDOR1 (NADPH Dependent Diflavin Oxidoreductase 1) is a Protein Coding gene. The NDOR1 gene, located on 9q34.3, is conserved in chimpanzee, dog, cow, and mouse, etc. This gene encodes an NADPH-dependent diflavin reductase that contains both flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) binding domains. The encoded protein catalyzes the transfer of electrons from NADPH through FAD and FMN cofactors to potential redox partners. Human novel oxidoreductase 1 (NDOR1) is a diflavin reductase closely related to cytochrome P450 reductase (POR) and nitric oxide synthase (NOS), which are involved in the metabolism of antitumor agents. A variant cDNA sequence of NDOR1, NDOR1 p.518-519ins9 or NDOR1_v1, has been deposited in GenBank (accession no. AK026089 and AY077845) that encodes an additional nine amino acids.

    NDOR1 の参考文献

    • Olteanu H, et al. (2003) Redundancy in the pathway for redox regulation of mammalian methionine synthase: Reductive activation by the dual flavoprotein, novel reductase 1. J Biol Chem 278 (40): 38310-38314.
    • Finn RD, et al. (2005) Identification of a functionally impaired allele of human novel oxidoreductase 1 (ndor1), ndor1*1. Pharmacogenet Genomics 15 (6): 381-386.
    • Banci L, et al. (2013) Molecular view of an electron transfer process essential for iron-sulfur protein biogenesis. Proc Natl Acad Sci U S A 110 (18): 7136-7141.

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