Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ribonuclease HI (RNase HI) (EC 3.1.26.4) (Ribonuclease H) (RNase H)

 RNH_ECOLI               Reviewed;         155 AA.
P0A7Y4; P00647; Q8FKY5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
05-DEC-2018, entry version 123.
RecName: Full=Ribonuclease HI;
Short=RNase HI;
EC=3.1.26.4;
AltName: Full=Ribonuclease H;
Short=RNase H;
Name=rnhA; Synonyms=dasF, herA, rnh, sdrA;
OrderedLocusNames=b0214, JW0204;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6296074;
Kanaya S., Crouch R.J.;
"DNA sequence of the gene coding for Escherichia coli ribonuclease
H.";
J. Biol. Chem. 258:1276-1281(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=FB2;
PubMed=6316347; DOI=10.1073/pnas.80.23.7137;
Maki H., Horiuchi T., Sekiguchi M.;
"Structure and expression of the dnaQ mutator and the RNase H genes of
Escherichia coli: overlap of the promoter regions.";
Proc. Natl. Acad. Sci. U.S.A. 80:7137-7141(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6302075;
Kanaya S., Crouch R.J.;
"Low levels of RNase H activity in Escherichia coli FB2 rnh result
from a single-base change in the structural gene of RNase H.";
J. Bacteriol. 154:1021-1026(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3023634; DOI=10.1016/0022-2836(86)90080-X;
Cox E.C., Horner D.L.;
"DNA sequence and coding properties of mutD(dnaQ) a dominant
Escherichia coli mutator gene.";
J. Mol. Biol. 190:113-117(1986).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
4.0 - 6.0 min (189,987 - 281,416bp) region.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[9]
PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS OF CYSTEINE RESIDUES.
PubMed=2171503; DOI=10.1042/bj2710059;
Kanaya S., Kimura S., Katsuda C., Ikehara M.;
"Role of cysteine residues in ribonuclease H from Escherichia coli.
Site-directed mutagenesis and chemical modification.";
Biochem. J. 271:59-66(1990).
[10]
MUTAGENESIS OF ASP-10; GLU-48; ASP-70; HIS-124; ASN-130 AND ASP-134.
PubMed=1689729;
Kanaya S., Kohara A., Miura Y., Sekiguchi A., Iwai S., Inoue H.,
Ohtsuka E., Ikehara M.;
"Identification of the amino acid residues involved in an active site
of Escherichia coli ribonuclease H by site-directed mutagenesis.";
J. Biol. Chem. 265:4615-4621(1990).
[11]
COFACTOR, AND MUTAGENESIS OF HIS-124 AND ASP-134.
PubMed=9852071; DOI=10.1074/jbc.273.51.34128;
Keck J.L., Goedken E.R., Marqusee S.;
"Activation/attenuation model for RNase H. A one-metal mechanism with
second-metal inhibition.";
J. Biol. Chem. 273:34128-34133(1998).
[12]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=1698262; DOI=10.1038/347306a0;
Katayanagi K., Miyagawa M., Matsushima M., Ishikawa M., Kanaya S.,
Ikehara M., Matsuzaki T., Morikawa K.;
"Three-dimensional structure of ribonuclease H from E. coli.";
Nature 347:306-309(1990).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
PubMed=2169648; DOI=10.1126/science.2169648;
Yang W., Hendrickson W.A., Crouch R.J., Satow Y.;
"Structure of ribonuclease H phased at 2-A resolution by MAD analysis
of the selenomethionyl protein.";
Science 249:1398-1405(1990).
[14]
STRUCTURE BY NMR.
PubMed=1646006; DOI=10.1021/bi00238a030;
Yamazaki T., Yoshida M., Kanaya S., Nakamura H., Nagayama K.;
"Assignments of backbone 1H, 13C, and 15N resonances and secondary
structure of ribonuclease H from Escherichia coli by heteronuclear
three-dimensional NMR spectroscopy.";
Biochemistry 30:6036-6047(1991).
[15]
X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
PubMed=1311386; DOI=10.1016/0022-2836(92)90260-Q;
Katayanagi K., Miyagawa M., Matsushima M., Ishikawa M., Kanaya S.,
Nakamura H., Ikehara M., Matsuzaki T., Morikawa K.;
"Structural details of ribonuclease H from Escherichia coli as refined
to an atomic resolution.";
J. Mol. Biol. 223:1029-1052(1992).
[16]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS.
PubMed=8381958; DOI=10.1093/protein/6.1.85;
Ishikawa K., Kimura S., Kanaya S., Morikawa K., Nakamura H.;
"Structural study of mutants of Escherichia coli ribonuclease HI with
enhanced thermostability.";
Protein Eng. 6:85-91(1993).
[17]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ASN-10; GLN-48 AND
ASN-70.
PubMed=8408067;
Katayanagi K., Ishikawa K., Okumura M., Ariyoshi M., Kanaya S.,
Kawano Y., Suzuki M., Tanaka I., Morikawa K.;
"Crystal structures of ribonuclease HI active site mutants from
Escherichia coli.";
J. Biol. Chem. 268:22092-22099(1993).
[18]
STRUCTURE BY NMR.
PubMed=8527428; DOI=10.1021/bi00051a003;
Yamazaki T., Ogasahara K., Yutani K., Oobatake M., Kanaya S.;
"Folding pathway of Escherichia coli ribonuclease HI: a circular
dichroism, fluorescence, and NMR study.";
Biochemistry 34:16552-16562(1995).
[19]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND MUTAGENESIS OF HIS-124 AND
ASP-134.
PubMed=8931125; DOI=10.1093/protein/9.10.857;
Kashiwagi T., Jeanteur D., Haruki M., Katayanagi K., Kanaya S.,
Morikawa K.;
"Proposal for new catalytic roles for two invariant residues in
Escherichia coli ribonuclease HI.";
Protein Eng. 9:857-867(1996).
[20]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
PubMed=11106164; DOI=10.1110/ps.9.10.1914;
Goedken E.R., Keck J.L., Berger J.M., Marqusee S.;
"Divalent metal cofactor binding in the kinetic folding trajectory of
Escherichia coli ribonuclease HI.";
Protein Sci. 9:1914-1921(2000).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS.
PubMed=11083878; DOI=10.1074/jbc.M009626200;
Goedken E.R., Marqusee S.;
"Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two
divalent metals bound in the active site.";
J. Biol. Chem. 276:7266-7271(2001).
[22]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS ALA-48 AND ASN-134 IN
COMPLEX WITH MANGANESE IONS.
PubMed=15644213; DOI=10.1016/j.jmb.2004.11.007;
Tsunaka Y., Takano K., Matsumura H., Yamagata Y., Kanaya S.;
"Identification of single Mn(2+) binding sites required for activation
of the mutant proteins of E.coli RNase HI at Glu48 and/or Asp134 by X-
ray crystallography.";
J. Mol. Biol. 345:1171-1183(2005).
-!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-
DNA hybrids. RNase H participates in DNA replication; it helps to
specify the origin of genomic replication by suppressing
initiation at origins other than the oriC locus; along with the
5'-3' exonuclease of pol1, it removes RNA primers from the Okazaki
fragments of lagging strand synthesis; and it defines the origin
of replication for ColE1-type plasmids by specific cleavage of an
RNA preprimer.
-!- CATALYTIC ACTIVITY:
Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
EC=3.1.26.4;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:9852071};
Note=Binds 1 Mg(2+) ion per subunit in the absence of substrate.
Requires millimolar levels of Mg(2+) for maximal activity. Has low
activity at micromolar concentrations of Mn(2+) and is inhibited
at higher Mn(2+) levels. Can bind a second metal ion at a
regulatory site, or after substrate binding.
{ECO:0000269|PubMed:9852071};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11083878,
ECO:0000269|PubMed:1311386, ECO:0000269|PubMed:15644213,
ECO:0000269|PubMed:2169648}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; K00985; AAA24565.1; -; Genomic_DNA.
EMBL; V00337; CAA23620.1; -; Genomic_DNA.
EMBL; X04027; CAA27660.1; -; Genomic_DNA.
EMBL; U70214; AAB08636.1; -; Genomic_DNA.
EMBL; U00096; AAC73319.1; -; Genomic_DNA.
EMBL; AP009048; BAA77885.1; -; Genomic_DNA.
PIR; A92401; NRECH.
RefSeq; NP_414750.1; NC_000913.3.
RefSeq; WP_000917883.1; NZ_LN832404.1.
PDB; 1F21; X-ray; 1.40 A; A=1-155.
PDB; 1G15; X-ray; 1.90 A; A=1-155.
PDB; 1GOA; X-ray; 1.90 A; A=1-155.
PDB; 1GOB; X-ray; 2.00 A; A=1-155.
PDB; 1GOC; X-ray; 2.00 A; A=1-155.
PDB; 1JL1; X-ray; 1.30 A; A=1-155.
PDB; 1JL2; X-ray; 1.76 A; A/B/C/D=1-49, A/B/C/D=121-155.
PDB; 1JXB; X-ray; 1.60 A; A=1-155.
PDB; 1KVA; X-ray; 1.80 A; A=1-155.
PDB; 1KVB; X-ray; 1.90 A; A=1-155.
PDB; 1KVC; X-ray; 1.90 A; A=1-155.
PDB; 1LAV; X-ray; 1.80 A; A=1-155.
PDB; 1LAW; X-ray; 1.80 A; A=1-155.
PDB; 1RBR; X-ray; 1.80 A; A=1-155.
PDB; 1RBS; X-ray; 1.80 A; A=1-155.
PDB; 1RBT; X-ray; 1.80 A; A=1-155.
PDB; 1RBU; X-ray; 1.80 A; A=1-155.
PDB; 1RBV; X-ray; 1.80 A; A=1-155.
PDB; 1RCH; NMR; -; A=1-155.
PDB; 1RDA; X-ray; 2.15 A; A=1-155.
PDB; 1RDB; X-ray; 1.90 A; A=1-155.
PDB; 1RDC; X-ray; 2.30 A; A=1-155.
PDB; 1RDD; X-ray; 2.80 A; A=1-155.
PDB; 1RNH; X-ray; 2.00 A; A=1-155.
PDB; 1WSE; X-ray; 2.30 A; A/B=1-155.
PDB; 1WSF; X-ray; 2.30 A; A/B/C/D=1-155.
PDB; 1WSG; X-ray; 2.20 A; A/B/C/D=1-155.
PDB; 1WSH; X-ray; 1.90 A; A/B/C/D=1-155.
PDB; 1WSI; X-ray; 2.00 A; A/B/C/D=1-155.
PDB; 1WSJ; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-155.
PDB; 2RN2; X-ray; 1.48 A; A=1-155.
PDB; 2YV0; X-ray; 1.40 A; X=1-155.
PDB; 2Z1G; X-ray; 2.10 A; A=1-155.
PDB; 2Z1H; X-ray; 2.60 A; A=1-155.
PDB; 2Z1I; X-ray; 2.00 A; A/B=1-155.
PDB; 2Z1J; X-ray; 2.38 A; A=1-155.
PDB; 3AA2; X-ray; 1.90 A; A=1-155.
PDB; 3AA3; X-ray; 2.20 A; A=1-155.
PDB; 3AA4; X-ray; 1.79 A; A=1-155.
PDB; 3AA5; X-ray; 2.10 A; X=1-155.
PDB; 3HYF; X-ray; 1.70 A; A=79-102.
PDB; 3QIN; X-ray; 1.70 A; A=79-102.
PDB; 3QIO; X-ray; 1.40 A; A=79-102.
PDB; 4Z0U; X-ray; 2.00 A; A/B=1-155.
PDBsum; 1F21; -.
PDBsum; 1G15; -.
PDBsum; 1GOA; -.
PDBsum; 1GOB; -.
PDBsum; 1GOC; -.
PDBsum; 1JL1; -.
PDBsum; 1JL2; -.
PDBsum; 1JXB; -.
PDBsum; 1KVA; -.
PDBsum; 1KVB; -.
PDBsum; 1KVC; -.
PDBsum; 1LAV; -.
PDBsum; 1LAW; -.
PDBsum; 1RBR; -.
PDBsum; 1RBS; -.
PDBsum; 1RBT; -.
PDBsum; 1RBU; -.
PDBsum; 1RBV; -.
PDBsum; 1RCH; -.
PDBsum; 1RDA; -.
PDBsum; 1RDB; -.
PDBsum; 1RDC; -.
PDBsum; 1RDD; -.
PDBsum; 1RNH; -.
PDBsum; 1WSE; -.
PDBsum; 1WSF; -.
PDBsum; 1WSG; -.
PDBsum; 1WSH; -.
PDBsum; 1WSI; -.
PDBsum; 1WSJ; -.
PDBsum; 2RN2; -.
PDBsum; 2YV0; -.
PDBsum; 2Z1G; -.
PDBsum; 2Z1H; -.
PDBsum; 2Z1I; -.
PDBsum; 2Z1J; -.
PDBsum; 3AA2; -.
PDBsum; 3AA3; -.
PDBsum; 3AA4; -.
PDBsum; 3AA5; -.
PDBsum; 3HYF; -.
PDBsum; 3QIN; -.
PDBsum; 3QIO; -.
PDBsum; 4Z0U; -.
ProteinModelPortal; P0A7Y4; -.
SMR; P0A7Y4; -.
BioGrid; 4263455; 263.
DIP; DIP-47864N; -.
IntAct; P0A7Y4; 22.
STRING; 316385.ECDH10B_0195; -.
BindingDB; P0A7Y4; -.
ChEMBL; CHEMBL1770039; -.
PaxDb; P0A7Y4; -.
PRIDE; P0A7Y4; -.
EnsemblBacteria; AAC73319; AAC73319; b0214.
EnsemblBacteria; BAA77885; BAA77885; BAA77885.
GeneID; 946955; -.
KEGG; ecj:JW0204; -.
KEGG; eco:b0214; -.
PATRIC; fig|1411691.4.peg.2070; -.
EchoBASE; EB0853; -.
EcoGene; EG10860; rnhA.
eggNOG; ENOG4108UMW; Bacteria.
eggNOG; COG0328; LUCA.
HOGENOM; HOG000040465; -.
InParanoid; P0A7Y4; -.
KO; K03469; -.
PhylomeDB; P0A7Y4; -.
BioCyc; EcoCyc:EG10860-MONOMER; -.
BioCyc; MetaCyc:EG10860-MONOMER; -.
BRENDA; 3.1.26.4; 2026.
EvolutionaryTrace; P0A7Y4; -.
PRO; PR:P0A7Y4; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004519; F:endonuclease activity; IDA:EcoliWiki.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0003676; F:nucleic acid binding; IDA:EcoliWiki.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:EcoCyc.
GO; GO:0043137; P:DNA replication, removal of RNA primer; IMP:EcoCyc.
GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
CDD; cd09278; RNase_HI_prokaryote_like; 1.
Gene3D; 3.30.420.10; -; 1.
HAMAP; MF_00042; RNase_H; 1.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR022892; RNaseHI.
Pfam; PF00075; RNase_H; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS50879; RNASE_H; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
Reference proteome.
CHAIN 1 155 Ribonuclease HI.
/FTId=PRO_0000195372.
DOMAIN 1 142 RNase H.
METAL 10 10 Magnesium 1.
{ECO:0000269|PubMed:1311386}.
METAL 10 10 Magnesium 2.
{ECO:0000269|PubMed:1311386}.
METAL 48 48 Magnesium 1.
{ECO:0000269|PubMed:1311386}.
METAL 70 70 Magnesium 1.
{ECO:0000269|PubMed:1311386}.
METAL 134 134 Magnesium 2.
{ECO:0000269|PubMed:1311386}.
MUTAGEN 10 10 D->N: Loss of activity.
{ECO:0000269|PubMed:1689729}.
MUTAGEN 48 48 E->Q: Loss of activity.
{ECO:0000269|PubMed:1689729}.
MUTAGEN 70 70 D->N: Loss of activity.
{ECO:0000269|PubMed:1689729}.
MUTAGEN 124 124 H->A: Reduces activity.
{ECO:0000269|PubMed:1689729,
ECO:0000269|PubMed:8931125,
ECO:0000269|PubMed:9852071}.
MUTAGEN 130 130 N->A: Reduces activity.
{ECO:0000269|PubMed:1689729}.
MUTAGEN 134 134 D->A: Loss of activity.
{ECO:0000269|PubMed:1689729,
ECO:0000269|PubMed:8931125,
ECO:0000269|PubMed:9852071}.
MUTAGEN 134 134 D->H,N: Slight decrease of activity.
{ECO:0000269|PubMed:1689729,
ECO:0000269|PubMed:8931125,
ECO:0000269|PubMed:9852071}.
STRAND 2 4 {ECO:0000244|PDB:1RDD}.
STRAND 5 15 {ECO:0000244|PDB:1JL1}.
STRAND 18 28 {ECO:0000244|PDB:1JL1}.
STRAND 31 42 {ECO:0000244|PDB:1JL1}.
HELIX 44 57 {ECO:0000244|PDB:1JL1}.
STRAND 64 69 {ECO:0000244|PDB:1JL1}.
HELIX 72 79 {ECO:0000244|PDB:1JL1}.
HELIX 82 87 {ECO:0000244|PDB:1JL1}.
TURN 88 90 {ECO:0000244|PDB:1JL1}.
STRAND 95 97 {ECO:0000244|PDB:2YV0}.
HELIX 101 110 {ECO:0000244|PDB:1JL1}.
TURN 111 113 {ECO:0000244|PDB:1JL1}.
STRAND 115 120 {ECO:0000244|PDB:1JL1}.
HELIX 123 125 {ECO:0000244|PDB:1LAV}.
HELIX 128 142 {ECO:0000244|PDB:1JL1}.
SEQUENCE 155 AA; 17597 MW; B8EF81EEB2F94CBE CRC64;
MLKQVEIFTD GSCLGNPGPG GYGAILRYRG REKTFSAGYT RTTNNRMELM AAIVALEALK
EHCEVILSTD SQYVRQGITQ WIHNWKKRGW KTADKKPVKN VDLWQRLDAA LGQHQIKWEW
VKGHAGHPEN ERCDELARAA AMNPTLEDTG YQVEV


Related products :

Catalog number Product name Quantity
EIAAB35513 Homo sapiens,HP-RNase,Human,RIB1,RIB-1,Ribonuclease 1,Ribonuclease A,Ribonuclease pancreatic,RNase 1,RNase A,RNase UpI-1,RNASE1,RNS1
H-2782.0025 rec Human Pancreatic Ribonuclease (RNase) (expressed in E.coli) Salt _ Binding _ Synonym rec Ribonuclease (RNase), rec Pancreatic Ribonuclease (RNase) SumFormula 25.0 mg
H-2782.0005 rec Human Pancreatic Ribonuclease (RNase) (expressed in E.coli) Salt _ Binding _ Synonym rec Ribonuclease (RNase), rec Pancreatic Ribonuclease (RNase) SumFormula 5.0 mg
U0765h CLIA EDN,Eosinophil-derived neurotoxin,Homo sapiens,Human,Non-secretory ribonuclease,Ribonuclease 2,Ribonuclease US,RNase 2,RNase UpI-2,RNASE2,RNS2 96T
E0765h ELISA EDN,Eosinophil-derived neurotoxin,Homo sapiens,Human,Non-secretory ribonuclease,Ribonuclease 2,Ribonuclease US,RNase 2,RNase UpI-2,RNASE2,RNS2 96T
E0765h ELISA kit EDN,Eosinophil-derived neurotoxin,Homo sapiens,Human,Non-secretory ribonuclease,Ribonuclease 2,Ribonuclease US,RNase 2,RNase UpI-2,RNASE2,RNS2 96T
EIAAB35609 AGS4,Aicardi-Goutieres syndrome 4 protein,Homo sapiens,Human,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H(35),RNase H2 subunit A,RNase HI large subunit,RNA
EIAAB35510 2-5A-dependent ribonuclease,2-5A-dependent RNase,Homo sapiens,Human,Ribonuclease 4,Ribonuclease L,RNase L,RNASEL,RNS4
EIAAB35523 Bos taurus,Bovine,K6b,Ribonuclease K2,Ribonuclease K6,RK6B,RNase K2,RNase K6,RNASE6,RNS6
EIAAB35511 2-5A-dependent ribonuclease,2-5A-dependent RNase,Mouse,Mus musculus,Ribonuclease 4,Ribonuclease L,RNase L,Rnasel,Rns4
18-003-43617 Ribonuclease H2 subunit A - EC 3.1.26.4; RNase H2 subunit A; Ribonuclease HI subunit A; Ribonuclease HI large subunit; RNase HI large subunit; RNase H(35); Aicardi-Goutieres syndrome 4 protein; AGS4 P 0.05 mg Aff Pur
18-003-43618 Ribonuclease H2 subunit A - EC 3.1.26.4; RNase H2 subunit A; Ribonuclease HI subunit A; Ribonuclease HI large subunit; RNase HI large subunit; RNase H(35); Aicardi-Goutieres syndrome 4 protein; AGS4 P 0.1 mg Protein A
15-288-10801F Ribonuclease pancreatic - EC 3.1.27.5; RNase 1; RNase A; RNase UpI-1; RIB-1; HP-RNase Polyclonal 0.05 mg
15-288-10801F Ribonuclease pancreatic - EC 3.1.27.5; RNase 1; RNase A; RNase UpI-1; RIB-1; HP-RNase Polyclonal 0.1 mg
U0765m CLIA Ear4,Eosinophil cationic-type ribonuclease 4,Mouse,MR-4,Mus musculus,Non-secretory ribonuclease,Ribonuclease 2,RNase 2,Rnase2 96T
E0765m ELISA kit Ear4,Eosinophil cationic-type ribonuclease 4,Mouse,MR-4,Mus musculus,Non-secretory ribonuclease,Ribonuclease 2,RNase 2,Rnase2 96T
E0765m ELISA Ear4,Eosinophil cationic-type ribonuclease 4,Mouse,MR-4,Mus musculus,Non-secretory ribonuclease,Ribonuclease 2,RNase 2,Rnase2 96T
EIAAB35615 AGS3,Aicardi-Goutieres syndrome 3 protein,AYP1,Homo sapiens,Human,Ribonuclease H2 subunit C,Ribonuclease HI subunit C,RNase H1 small subunit,RNase H2 subunit C,RNASEH2C
18-003-42930 2-5A-dependent ribonuclease - EC 3.1.26.-; 2-5A-dependent RNase; Ribonuclease L; RNase L; Ribonuclease 4 Polyclonal 0.1 mg Protein A
EIAAB35628 Bos taurus,Bovine,Ribonuclease BS-1,Seminal ribonuclease,Seminal RNase,SRN,S-RNase
EIAAB35607 Mouse,Mus musculus,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H2 subunit A,RNase HI large subunit,Rnaseh2a,Rnasehi
EIAAB35515 Bos taurus,Bovine,Ribonuclease pancreatic,RNase 1,RNase A,RNASE1,RNS1
EIAAB35514 Pig,Ribonuclease pancreatic,RNase 1,RNase A,RNASE1,RNS1,Sus scrofa
EIAAB35512 Mouse,Mus musculus,Rib1,Rib-1,Ribonuclease pancreatic,RNase 1,RNase A,Rnase1,Rns1
EIAAB35606 Rat,Rattus norvegicus,Ribonuclease H2 subunit A,Ribonuclease HI large subunit,Ribonuclease HI subunit A,RNase H2 subunit A,RNase HI large subunit,Rnaseh2a


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur