Ribonucleoside-diphosphate reductase 1 subunit beta Recombinant Protein | nrdB recombinant protein

Recombinant Escherichia coli Ribonucleoside-diphosphate reductase 1 subunit beta

Cat. Num. AAA114581

• Gene Names: nrdB; ECK2227; ftsB; JW2229
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Ribonucleoside-diphosphate reductase 1 subunit beta; N/A; Recombinant Escherichia coli Ribonucleoside-diphosphate reductase 1 subunit beta; Protein B2; Protein R2; Ribonucleotide reductase 1; nrdB recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 2-376aa; Full Length
• Sequence: AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL
• Sequence Length: 376

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for nrdB recombinant protein

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis.

References

Primary structure of the Escherichia coli ribonucleoside diphosphate reductase operon.Carlson J., Fuchs J.A., Messing J.Proc. Natl. Acad. Sci. U.S.A. 81:4294-4297(1984) Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.DNA Res. 4:91-113(1997) The complete genome sequence of Escherichia coli K-12.Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.Science 277:1453-1462(1997) Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.Mol. Syst. Biol. 2:E1-E5(2006) Cloning, overproduction, and purification of the B2 subunit of ribonucleoside-diphosphate reductase.Salowe S.P., Stubbe J.J. Bacteriol. 165:363-366(1986) Three-dimensional structure of the free radical protein of ribonucleotide reductase.Nordlund P., Sjoeberg B.-M., Eklund H.Nature 345:593-598(1990) Structure and function of the Escherichia coli ribonucleotide reductase protein R2.Nordlund P., Eklund H.J. Mol. Biol. 232:123-164(1993) Crystal structure of reduced protein R2 of ribonucleotide reductase the structural basis for oxygen activation at a dinuclear iron site.Logan D.T., Su X.-D., Aaberg A., Regnstroem K., Hajdu J., Eklund H., Nordlund P.Structure 4:1053-1064(1996) Binding of allosteric effectors to ribonucleotide reductase protein R1 reduction of active-site cysteines promotes substrate binding.Eriksson M., Uhlin U., Ramaswamy S., Ekberg M., Regnstroem K., Sjoeberg B.-M., Eklund H.Structure 5:1077-1092(1997) Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography.Tong W., Burdi D., Riggs-Gelasco P., Chen S., Edmondson D., Huynh B.H., Stubbe J., Han S., Arvai A., Tainer J.Biochemistry 37:5840-5848(1998) Crystal structures of two self-hydroxylating ribonucleotide reductase protein R2 mutants structural basis for the oxygen-insertion step of hydroxylation reactions catalyzed by diiron proteins.Logan D.T., De;Mare F., Persson B.O., Slaby A., Sjoeberg B.-M., Nordlund P.Biochemistry 37:10798-10807(1998) Crystal structures of oxidized dinuclear manganese centres in Mn-substituted class I ribonucleotide reductase from Escherichia coli carboxylate shifts with implications for O2 activation and radical generation.Hogbom M., Andersson M.E., Nordlund P.J. Biol. Inorg. Chem. 6:315-323(2001)

NCBI and Uniprot Product Information

• NCBI GI #: 16130170
• NCBI GeneID: 946732
• NCBI Accession #: NP_416738.1
• NCBI GenBank Nucleotide #: NC_000913.3
• UniProt Accession #: P69924; P00453
• Molecular Weight: 45.4 kDa
• NCBI Official Full Name: ribonucleoside-diphosphate reductase 1, beta subunit, ferritin-like protein
• NCBI Official Symbol: nrdB
• NCBI Official Synonym Symbols: ECK2227; ftsB; JW2229
• NCBI Protein Information: ribonucleoside-diphosphate reductase 1, beta subunit, ferritin-like protein
• UniProt Protein Name: Ribonucleoside-diphosphate reductase 1 subunit beta
• UniProt Gene Name: nrdB
• UniProt Synonym Gene Names: ftsB
• UniProt Entry Name: RIR2_ECOLI