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nrdA recombinant protein :: Ribonucleoside-diphosphate reductase 1 subunit alpha Recombinant Protein

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Catalog # MBS1264323
Unit / Price
  0.01 mg (E-Coli)  /  $110 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $285 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
  0.05 mg (Yeast)  /  $1,215 +1 FREE 8GB USB
  0.05 mg (Baculovirus)  /  $1,330 +1 FREE 8GB USB
  0.05 mg (Mammalian-Cell)  /  $1,585 +1 FREE 8GB USB
  0.2 mg (Yeast)  /  $1,650 +2 FREE 8GB USB
  0.1 mg (Baculovirus)  /  $1,690 +2 FREE 8GB USB
  0.5 mg (Yeast)  /  $1,870 +2 FREE 8GB USB
  0.1 mg (Mammalian-Cell)  /  $2,375 +2 FREE 8GB USB
  0.5 mg (Baculovirus)  /  $2,410 +3 FREE 8GB USB
  1 mg (Yeast)  /  $2,825 +3 FREE 8GB USB
  1 mg (Baculovirus)  /  $3,150 +3 FREE 8GB USB
SDS-PAGE
Product Name

Ribonucleoside-diphosphate reductase 1 subunit alpha (nrdA), Recombinant Protein

Popular Item
Also Known As

Recombinant Escherichia coli Ribonucleoside-diphosphate reductase 1 subunit alpha

Product Synonym Names
Protein B1; Ribonucleoside-diphosphate reductase 1 R1 subunit; Ribonucleotide reductase 1
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
1-761aa; Full Length
Sequence Length
761
Sequence
MNQNLLVTKR DGSTERINLD KIHRVLDWAA EGLHNVSISQ VELRSHIQFY DGIKTSDIHE TIIKAAADLI SRDAPDYQYL AARLAIFHLR KKAYGQFEPP ALYDHVVKMV EMGKYDNHLL EDYTEEEFKQ MDTFIDHDRD MTFSYAAVKQ LEGKYLVQNR VTGEIYESAQ FLYILVAACL FSNYPRETRL QYVKRFYDAV STFKISLPTP IMSGVRTPTR QFSSCVLIEC GDSLDSINAT SSAIVKYVSQ RAGIGINAGR IRALGSPIRG GEAFHTGCIP FYKHFQTAVK SCSQGGVRGG AATLFYPMWH LEVESLLVLK NNRGVEGNRV RHMDYGVQIN KLMYTRLLKG EDITLFSPSD VPGLYDAFFA DQEEFERLYT KYEKDDSIRK QRVKAVELFS LMMQERASTG RIYIQNVDHC NTHSPFDPAI APVRQSNLCL EIALPTKPLN DVNDENGEIA LCTLSAFNLG AINNLDELEE LAILAVRALD ALLDYQDYPI PAAKRGAMGR RTLGIGVINF AYYLAKHGKR YSDGSANNLT HKTFEAIQYY LLKASNELAK EQGACPWFNE TTYAKGILPI DTYKKDLDTI ANEPLHYDWE ALRESIKTHG LRNSTLSALM PSETSSQISN ATNGIEPPRG YVSIKASKDG ILRQVVPDYE HLHDAYELLW EMPGNDGYLQ LVGIMQKFID QSISANTNYD PSRFPSGKVP MQQLLKDLLT AYKFGVKTLY YQNTRDGAED AQDDLVPSIQ DDGCESGACK I
3D Structure
ModBase 3D Structure for P00452
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of nrdA recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
nrdA recombinant protein
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines.

nrdA recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for nrdA. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
Molecular Weight
101.72kD
NCBI Official Full Name
ribonucleoside-diphosphate reductase 1, alpha subunit
NCBI Official Symbol
NCBI Official Synonym Symbols
dnaF; ECK2226; JW2228
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NCBI Protein Information
ribonucleoside-diphosphate reductase 1, alpha subunit
UniProt Protein Name
Ribonucleoside-diphosphate reductase 1 subunit alpha
UniProt Synonym Protein Names
Protein B1; Ribonucleoside-diphosphate reductase 1 R1 subunit; Ribonucleotide reductase 1
UniProt Gene Name
UniProt Synonym Gene Names
UniProt Entry Name
RIR1_ECOLI
NCBI Summary for nrdA
Reducing equivalents provided by glutaredoxin or thioredoxin. [More information is available at EcoGene: EG10660]. The B1 protein of ribonucleoside-diphosphate reductase consists of two polypeptide chains of similar or identical size. [More information is available at EcoCyc: EG10660].
UniProt Comments for nrdA
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines.
Product References and Citations for nrdA recombinant protein
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) Nucleotide sequence of the gene coding for the large subunit of ribonucleotide reductase of Escherichia coli. Correction.Nilsson O., Aaberg A., Lundqvist T., Sjoeberg B.-M.Nucleic Acids Res. 16:4174-4174(1988) Sjoeberg B.-M.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) Protein B1 of ribonucleotide reductase. Direct analytical data and comparisons with data indirectly deduced from the nucleotide sequence of the Escherichia coli nrdA gene.Sjoeberg B.-M., Eriksson S., Joernvall H., Carlquist M., Eklund H.Eur. J. Biochem. 150:423-427(1985) Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli.Aaberg A., Hahne S., Karlsson M., Larsson A., Ormoe M., Aahgren A., Sjoeberg B.-M.J. Biol. Chem. 264:12249-12252(1989) Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase.Ekberg M., Sahlin M., Eriksson M., Sjoberg B.M.J. Biol. Chem. 271:20655-20659(1996) Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.Mol. Cell. Proteomics 8:215-225(2009) Structure of ribonucleotide reductase protein R1.Uhlin U., Eklund H.Nature 370:533-539(1994) A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase.Persson A.L., Eriksson M., Katterle B., Potsch S., Sahlin M., Sjoberg B.M.J. Biol. Chem. 272:31533-31541(1997) 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) Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction.Berardi M.J., Bushweller J.H.J. Mol. Biol. 292:151-161(1999)

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Disclaimer
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