Recombinant Human Ribonucleoside-diphosphate reductase large subunit | MyBioSource MBS717732 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Human Ribonucleoside-diphosphate reductase large subunit

catalog :

MBS717732

quantity :

0.05 mg (E-Coli)

price :

190 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS717732

products type :

Recombinant Protein

products full name :

Recombinant Human Ribonucleoside-diphosphate reductase large subunit

products short name :

Ribonucleoside-diphosphate reductase large subunit

products name syn :

Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit

other names :

ribonucleoside-diphosphate reductase large subunit isoform 1; Ribonucleoside-diphosphate reductase large subunit; ribonucleoside-diphosphate reductase large subunit; ribonucleotide reductase catalytic subunit M1; Ribonucleoside-diphosphate reductase subunit M1; Ribonucleotide reductase large subunit

products gene name :

RRM1

other gene names :

RRM1; RRM1; R1; RR1; RIR1; RR1

uniprot entry name :

RIR1_HUMAN

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

1-792

sequence length :

792

sequence :

MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQI
TMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILA
ARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVA
KSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYL
LKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSE
RWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDT
LKQCALISKSAGGIGVAVSCI

purity :

Greater than 90% as determined by SDS-PAGE.

form :

Liquid containing glycerol; lyophilization may be available upon request.

storage stability :

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

products categories :

Epigenetics and Nuclear Signaling

products description :

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

products references :

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)

ncbi gi num :

4506749

ncbi acc num :

NP_001024.1

ncbi gb acc num :

NM_001033.4

uniprot acc num :

P23921

ncbi mol weight :

106.01kD

ncbi pathways :

E2F Transcription Factor Network Pathway (137934); Fluoropyrimidine Activity Pathway (198778); Glutathione Metabolism Pathway (82973); Glutathione Metabolism Pathway (343); Integrated Pancreatic Cancer Pathway (711360); Metabolic Pathways (132956); Metabolism Pathway (1269956); Metabolism Of Nucleotides Pathway (1270133); Nucleotide Metabolism Pathway (198876); Purine Metabolism Pathway (82944)

ncbi summary :

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 summary :

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

size1 :

0.05 mg (E-Coli)

price1 :

190 USD

size2 :

0.05 mg (Yeast)

price2 :

190

size3 :

0.2 mg (E-Coli)

price3 :

460

size4 :

0.2 mg (Yeast)

price4 :

460

size5 :

0.5 mg (Yeast)

price5 :

750

more info or order :

MyBioSource product webpage