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RRM1 recombinant protein :: Ribonucleoside-diphosphate reductase large subunit Recombinant Protein

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Catalog # MBS717732
Unit / Price
  0.01 mg (Yeast)  /  $110 +1 FREE 8GB USB
  0.01 mg (E-Coli)  /  $110 +1 FREE 8GB USB
  0.05 mg (Yeast)  /  $190 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $190 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $285 +1 FREE 8GB USB
  0.1 mg (Yeast)  /  $285 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $460 +1 FREE 8GB USB
  0.2 mg (Yeast)  /  $460 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $750 +1 FREE 8GB USB
  0.5 mg (Yeast)  /  $750 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,180 +1 FREE 8GB USB
  1 mg (Yeast)  /  $1,180 +1 FREE 8GB USB
  0.05 mg (Baculovirus)  /  $1,355 +1 FREE 8GB USB
  0.05 mg (Mammalian-Cell)  /  $1,610 +2 FREE 8GB USB
  0.1 mg (Baculovirus)  /  $1,720 +2 FREE 8GB USB
  0.1 mg (Mammalian-Cell)  /  $2,415 +3 FREE 8GB USB
  0.5 mg (Baculovirus)  /  $2,455 +3 FREE 8GB USB
  1 mg (Baculovirus)  /  $3,205 +4 FREE 8GB USB
SDS-PAGE
Product Name

Ribonucleoside-diphosphate reductase large subunit (RRM1), Recombinant Protein

Popular Item
Also Known As

Recombinant Human Ribonucleoside-diphosphate reductase large subunit

Product Synonym Names
Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
1-792aa; Full Length
Sequence Length
792
Sequence
MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG VTTVELDTLA AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED LYNYINPHNG KHSPMVAKST LDIVLANKDR LNSAIIYDRD FSYNYFGFKT LERSYLLKIN GKVAERPQHM LMRVSVGIHK EDIDAAIETY NLLSERWFTH ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL ISKSAGGIGV AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL MCPNECPGLD EVWGEEFEKL YASYEKQGRV RKVVKAQQLW YAIIESQTET GTPYMLYKDS CNRKSNQQNL GTIKCSNLCT EIVEYTSKDE VAVCNLASLA LNMYVTSEHT YDFKKLAEVT KVVVRNLNKI IDINYYPVPE ACLSNKRHRP IGIGVQGLAD AFILMRYPFE SAEAQLLNKQ IFETIYYGAL EASCDLAKEQ GPYETYEGSP VSKGILQYDM WNVTPTDLWD WKVLKEKIAK YGIRNSLLIA PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL WHEEMKNQII ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA FIDQSQSLNI HIAEPNYGKL TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF TLNKEKLKDK EKVSKEEEEK ERNTAAMVCS LENRDECLMC GS
OMIM
180410
3D Structure
ModBase 3D Structure for P23921
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 RRM1 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
RRM1 recombinant protein
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

RRM1 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 RRM1. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
106.01kD
NCBI Official Full Name
ribonucleoside-diphosphate reductase large subunit isoform 1
NCBI Official Synonym Full Names
ribonucleotide reductase catalytic subunit M1
NCBI Official Symbol
NCBI Official Synonym Symbols
R1; RR1; RIR1
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NCBI Protein Information
ribonucleoside-diphosphate reductase large subunit
UniProt Protein Name
Ribonucleoside-diphosphate reductase large subunit
UniProt Synonym Protein Names
Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit
UniProt Gene Name
UniProt Synonym Gene Names
UniProt Entry Name
RIR1_HUMAN
NCBI Summary for RRM1
This gene encodes the large and catalytic subunit of ribonucleotide reductase, an enzyme essential for the conversion of ribonucleotides into deoxyribonucleotides. A pool of available deoxyribonucleotides is important for DNA replication during S phase of the cell cycle as well as multiple DNA repair processes. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2015]
UniProt Comments for RRM1
RRM1: an enzyme involved in DNA replication that provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Belongs to the ribonucleoside diphosphate reductase large chain family. Heterodimer of a large and a small subunit. Heterodimer with small subunit RRM2 or RRM2B. The heterodimer with RRM2 has higher catalytic activity than the heterodimer with RRM2B. Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the M1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site. Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on M1, is formed only in the presence of the second subunit M2. The level of the enzyme activity is closely correlated with the growth rate of a cell and appears to vary with the cell cycle. Patients with advanced non-small cell lung cancer responded favorably to gemcitabine.

Protein type: Oxidoreductase; Other Amino Acids Metabolism - glutathione; EC 1.17.4.1; Nucleotide Metabolism - pyrimidine; DNA replication; Nucleotide Metabolism - purine

Chromosomal Location of Human Ortholog: 11p15.5

Cellular Component: cell projection; cell soma; cytoplasm; cytosol; nuclear envelope; nucleoplasm; ribonucleoside-diphosphate reductase complex

Molecular Function: ATP binding; protein binding; ribonucleoside-diphosphate reductase activity

Biological Process: cell proliferation in forebrain; deoxyribonucleotide biosynthetic process; DNA replication; male gonad development; mitotic cell cycle; nucleobase, nucleoside and nucleotide interconversion; nucleobase, nucleoside and nucleotide metabolic process; protein heterotetramerization; pyrimidine base metabolic process; response to ionizing radiation; retina development in camera-type eye
Product References and Citations for RRM1 recombinant protein
Human M1 subunit of ribonucleotide reductase cDNA sequence and expression in stimulated lymphocytes.Parker N.J., Begley C.G., Fox R.M.Nucleic Acids Res. 19:3741-3741(1991) Sequence analysis of the large and small subunits of human ribonucleotide reductase.Pavloff N., Rivard D., Masson S., Shen S.-H., Mes-Masson A.-M.DNA Seq. 2:227-234(1992) A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region.Bepler G., O'Briant K.C., Kim Y.-C., Schreiber G., Pitterle D.M.Genomics 55:164-175(1999) Human R1 subunit of ribonucleotide reductase (RRM1) 5' flanking region of the gene.Parker N.J., Begley C.G., Fox R.M.Genomics 19:91-96(1994) Human ribonucleotide reductase. Activation and inhibition by analogs of ATP.Harrington J.A., Spector T.Biochem. Pharmacol. 42:759-763(1991) Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits.Xue L., Zhou B., Liu X., Qiu W., Jin Z., Yen Y.Cancer Res. 63:980-986(2003) Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits.Qiu W., Zhou B., Darwish D., Shao J., Yen Y.Biochem. Biophys. Res. Commun. 340:428-434(2006) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) Enzyme regulation. IRBIT is a novel regulator of ribonucleotide reductase in higher eukaryotes.Arnaoutov A., Dasso M.Science 345:1512-1515(2014) Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization.Fairman J.W., Wijerathna S.R., Ahmad M.F., Xu H., Nakano R., Jha S., Prendergast J., Welin R.M., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis C.G.Nat. Struct. Mol. Biol. 18:316-322(2011)

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Disclaimer
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