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| Product Name
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Ribonucleoside-diphosphate reductase large subunit (RRM1), Recombinant Protein ★Popular Item★
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| Also Known As
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Recombinant Human Ribonucleoside-diphosphate reductase large subunit
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| Product Synonym Names
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Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit
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| Product Gene Name
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[Similar Products]
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| Research Use Only
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For Research Use Only. Not for use in diagnostic procedures.
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| Sequence Positions
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1-792aa; Full Length
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| Sequence
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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
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| OMIM
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180410
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| 3D Structure
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ModBase 3D Structure for P23921
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| Host
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E Coli or Yeast or Baculovirus or Mammalian Cell
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| Purity/Purification
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Greater than 90% as determined by SDS-PAGE. (lot specific)
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| Form/Format
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Liquid containing glycerol
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| Tag Information
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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.
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| Sterility
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Sterile filter available upon request.
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| Endotoxin
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Low endotoxin available upon request.
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| Preparation and Storage
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Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
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| ISO Certification
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Manufactured in an ISO 9001:2008 Certified Laboratory.
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| Other Notes
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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.
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Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
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| Product Categories/Family for RRM1 recombinant protein
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Epigenetics and Nuclear Signaling
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| SDS-PAGE of RRM1 recombinant protein
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(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
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| NCBI/Uniprot data below describe general gene information for RRM1. It may not necessarily be applicable to this product. |
| NCBI GI #
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4506749
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| NCBI GeneID
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6240
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| NCBI Accession #
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NP_001024.1
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[Other Products]
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| NCBI GenBank Nucleotide #
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NM_001033.4
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[Other Products]
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| UniProt Primary Accession #
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P23921
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[Other Products]
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| UniProt Secondary Accession #
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Q9UNN2
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[Other Products]
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| UniProt Related Accession #
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P23921
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[Other Products]
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| Molecular Weight
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106.01kD
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TOP
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| NCBI Official Full Name
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ribonucleoside-diphosphate reductase large subunit isoform 1
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| NCBI Official Synonym Full Names
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ribonucleotide reductase catalytic subunit M1
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| NCBI Official Symbol
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RRM1
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[Similar Products]
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| NCBI Official Synonym Symbols
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R1; RR1; RIR1
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[Similar Products]
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| NCBI Protein Information
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ribonucleoside-diphosphate reductase large subunit
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| UniProt Protein Name
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Ribonucleoside-diphosphate reductase large subunit
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| UniProt Synonym Protein Names
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Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit
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| Protein Family
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Ribonucleoside-diphosphate reductase
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| UniProt Gene Name
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RRM1
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[Similar Products]
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| UniProt Synonym Gene Names
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RR1
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[Similar Products]
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| UniProt Entry Name
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RIR1_HUMAN
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| NCBI Summary for RRM1
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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]
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| UniProt Comments for RRM1
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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
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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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| Research Articles on RRM1
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1. Adenoviral vector expressing short hairpin RNA targeting RRM1 exerts potent antitumor effects and increases sensitivity to gemcitabine.
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| Precautions
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All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.
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| Disclaimer
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While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.
It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.
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| Products associated with RRM1 recombinant protein | Pathways associated with RRM1 recombinant protein |
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| Diseases associated with RRM1 recombinant protein | Organs/Tissues associated with RRM1 recombinant protein |
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Recombinant Protein 
