Alternative Name(s):

Modulator of drug activity A

Species: (Organism)

Escherichia coli (strain K12)

Gene Names:

nfsA

Tag info:

N-terminal 6xHis-SUMO-tagged

Target Protein AA Sequence:

MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR

Expression Region:

1-240aa

Subcellular Location:

Tissue Specificity:

Protein Length:

Full Length

Pathway:

Mol. Weight:

42.8 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Others

Function:

Catalyzes the reduction of nitroaromatic compounds using NADPH. Has a broad electron acceptor specificity. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major oxygen-insensitive nitroreductase in E.coli.

Involvement in disease:

Relevance:

Reduction of nitroaromatic compounds using NADH. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major component of the oxygen-insensitive nitroreductase activity in E.coli.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Flavin oxidoreductase frp family

Reference:

Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds alteration of pyridine nucleotide binding by a single amino acid substitution.Kobori T., Sasaki H., Lee W.C., Zenno S., Saigo K., Murphy M.E., Tanokura M.J. Biol. Chem. 276:2816-2823(2001)