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

DNA polymerase beta (EC 2.7.7.7) (EC 4.2.99.-)

 DPOLB_RAT               Reviewed;         335 AA.
P06766; Q4G081;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
12-SEP-2018, entry version 185.
RecName: Full=DNA polymerase beta;
EC=2.7.7.7;
EC=4.2.99.-;
Name=Polb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3597402;
Matsukage A., Nishikawa K., Ooi T., Seto Y., Yamaguchi M.;
"Homology between mammalian DNA polymerase beta and terminal
deoxynucleotidyltransferase.";
J. Biol. Chem. 262:8960-8962(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar;
Konopinski R., Nowak R., Siedlecki J.A.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 18-335.
PubMed=2873575; DOI=10.1073/pnas.83.14.5106;
Zmudzka B.Z., Sengupta D., Matsukage A., Cobianchi F., Kumar P.,
Wilson S.H.;
"Structure of rat DNA polymerase beta revealed by partial amino acid
sequencing and cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 83:5106-5110(1986).
[5]
PARTIAL PROTEIN SEQUENCE, AND SEQUENCE REVISION TO 228.
PubMed=2404980;
Kumar P., Widen S.G., Williams K.R., Kedar P., Karpel R.L.,
Wilson S.H.;
"Studies of the domain structure of mammalian DNA polymerase beta.
Identification of a discrete template binding domain.";
J. Biol. Chem. 265:2124-2131(1990).
[6]
IMPORTANCE OF ARG-183 IN PRIMER BINDING.
PubMed=2198936; DOI=10.1021/bi00473a005;
Date T., Yamamoto S., Tanihara K., Nishimoto Y., Liu N., Matsukage A.;
"Site-directed mutagenesis of recombinant rat DNA polymerase beta:
involvement of arginine-183 in primer recognition.";
Biochemistry 29:5027-5034(1990).
[7]
MUTAGENESIS OF ASP-190 AND ASP-192, AND IMPORTANCE OF ASP-190 AND
ASP-192 IN PRIMER BINDING.
PubMed=2036395; DOI=10.1021/bi00235a023;
Date T., Yamamoto S., Tanihara K., Nishimoto Y., Matsukage A.;
"Aspartic acid residues at positions 190 and 192 of rat DNA polymerase
beta are involved in primer binding.";
Biochemistry 30:5286-5292(1991).
[8]
DNA-BINDING REGION.
PubMed=1420147; DOI=10.1021/bi00157a014;
Casas-Finet J.R., Kumar A., Karpel R.L., Wilson S.H.;
"Mammalian DNA polymerase beta: characterization of a 16-kDa
transdomain fragment containing the nucleic acid-binding activities of
the native enzyme.";
Biochemistry 31:10272-10280(1992).
[9]
MUTAGENESIS OF ASP-246, AND IMPORTANCE OF ASP-246 IN FIDELITY.
PubMed=14563842; DOI=10.1074/jbc.M309607200;
Dalal S., Kosa J.L., Sweasy J.B.;
"The D246V mutant of DNA polymerase beta misincorporates nucleotides:
evidence for a role for the flexible loop in DNA positioning within
the active site.";
J. Biol. Chem. 279:577-584(2004).
[10]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=8137427; DOI=10.1016/0092-8674(94)90388-3;
Davies J.F. II, Almassy R.J., Hostomska Z., Ferre R.A., Hostomsky Z.;
"2.3-A crystal structure of the catalytic domain of DNA polymerase
beta.";
Cell 76:1123-1133(1994).
[11]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=7516581; DOI=10.1126/science.7516581;
Sawaya M.R., Pelletier H., Kumar A., Wilson S.H., Kraut J.;
"Crystal structure of rat DNA polymerase beta: evidence for a common
polymerase mechanism.";
Science 264:1930-1935(1994).
[12]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=8841120; DOI=10.1021/bi960790i;
Pelletier H., Sawaya M.R.;
"Characterization of the metal ion binding helix-hairpin-helix motifs
in human DNA polymerase beta by X-ray structural analysis.";
Biochemistry 35:12778-12787(1996).
[13]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed=11330999; DOI=10.1021/bi002176j;
Arndt J.W., Gong W., Zhong X., Showalter A.K., Liu J., Dunlap C.A.,
Lin Z., Paxson C., Tsai M.-D., Chan M.K.;
"Insight into the catalytic mechanism of DNA polymerase beta:
structures of intermediate complexes.";
Biochemistry 40:5368-5375(2001).
[14]
STRUCTURE BY NMR OF 1-87.
PubMed=8639559; DOI=10.1021/bi952656o;
Liu D., Prasad R., Wilson S.H., DeRose E.F., Mullen G.P.;
"Three-dimensional solution structure of the N-terminal domain of DNA
polymerase beta and mapping of the ssDNA interaction interface.";
Biochemistry 35:6188-6200(1996).
[15]
STRUCTURE BY NMR OF 1-87.
PubMed=10656829; DOI=10.1006/jmbi.1999.3455;
Maciejewski M.W., Liu D., Prasad R., Wilson S.H., Mullen G.P.;
"Backbone dynamics and refined solution structure of the N-terminal
domain of DNA polymerase beta. Correlation with DNA binding and dRP
lyase activity.";
J. Mol. Biol. 296:229-253(2000).
-!- FUNCTION: Repair polymerase that plays a key role in base-excision
repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity
that removes the 5' sugar phosphate and also acts as a DNA
polymerase that adds one nucleotide to the 3' end of the arising
single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a
stepwise distributive fashion rather than in a processive fashion
as for other DNA polymerases.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 2 magnesium ions per subunit.;
-!- SUBUNIT: Interacts with APEX1, HUWE1/ARF-BP1, STUB1/CHIP and USP47
(By similarity). Monomer. Interacts with FAM168A (By similarity).
{ECO:0000250|UniProtKB:P06746}.
-!- INTERACTION:
P18887:XRCC1 (xeno); NbExp=4; IntAct=EBI-15845002, EBI-947466;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
Note=Cytoplasmic in normal conditions. Translocates to the nucleus
following DNA damage (By similarity). {ECO:0000250}.
-!- DOMAIN: Residues 239-252 form a flexible loop which appears to
affect the polymerase fidelity.
-!- PTM: Methylation by PRMT6 stimulates the polymerase activity by
enhancing DNA binding and processivity. {ECO:0000250}.
-!- PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated
by HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of
STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin,
leading to degradation by the proteasome. USP47 mediates the
deubiquitination of monoubiquitinated protein, preventing
polyubiquitination by STUB1/CHIP and its subsequent degradation
(By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the DNA polymerase type-X 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; J02776; AAA41901.1; -; mRNA.
EMBL; U38801; AAB00389.1; -; mRNA.
EMBL; BC098668; AAH98668.1; -; mRNA.
EMBL; M13961; AAA41900.1; -; mRNA.
PIR; A27112; A27112.
RefSeq; NP_058837.2; NM_017141.2.
UniGene; Rn.9346; -.
PDB; 1BNO; NMR; -; A=1-87.
PDB; 1BNP; NMR; -; A=1-87.
PDB; 1BPB; X-ray; 2.30 A; A=88-335.
PDB; 1BPD; X-ray; 3.60 A; A=1-335.
PDB; 1BPE; X-ray; 2.90 A; A=1-335.
PDB; 1DK2; NMR; -; A=2-87.
PDB; 1DK3; NMR; -; A=1-87.
PDB; 1HUO; X-ray; 2.60 A; A/B=1-335.
PDB; 1HUZ; X-ray; 2.60 A; A/B=1-335.
PDB; 1JN3; X-ray; 2.35 A; A=85-335.
PDB; 1NOM; X-ray; 3.00 A; A=88-335.
PDB; 1RPL; X-ray; 2.30 A; A=85-335.
PDB; 1ZQU; X-ray; 2.60 A; A=88-335.
PDB; 1ZQV; X-ray; 2.70 A; A=88-335.
PDB; 1ZQW; X-ray; 2.30 A; A=88-335.
PDB; 1ZQX; X-ray; 2.50 A; A=88-335.
PDB; 1ZQY; X-ray; 2.30 A; A=88-335.
PDB; 1ZQZ; X-ray; 2.70 A; A=88-335.
PDB; 2BPC; X-ray; 2.80 A; A=88-335.
PDB; 2BPF; X-ray; 2.90 A; A=1-335.
PDB; 2BPG; X-ray; 3.60 A; A/B=1-335.
PDB; 2VAN; X-ray; 2.10 A; A=91-335.
PDB; 3K75; X-ray; 2.95 A; D/E=91-335.
PDB; 3LQC; X-ray; 2.35 A; B=142-335.
PDB; 3UXN; X-ray; 2.50 A; A/B=1-335.
PDB; 3UXO; X-ray; 2.10 A; A/B=1-335.
PDB; 3UXP; X-ray; 2.72 A; A/B=1-335.
PDB; 3V72; X-ray; 2.49 A; A=1-335.
PDB; 3V7J; X-ray; 2.25 A; A=4-335.
PDB; 3V7K; X-ray; 2.27 A; A=4-335.
PDB; 3V7L; X-ray; 2.66 A; A=4-335.
PDBsum; 1BNO; -.
PDBsum; 1BNP; -.
PDBsum; 1BPB; -.
PDBsum; 1BPD; -.
PDBsum; 1BPE; -.
PDBsum; 1DK2; -.
PDBsum; 1DK3; -.
PDBsum; 1HUO; -.
PDBsum; 1HUZ; -.
PDBsum; 1JN3; -.
PDBsum; 1NOM; -.
PDBsum; 1RPL; -.
PDBsum; 1ZQU; -.
PDBsum; 1ZQV; -.
PDBsum; 1ZQW; -.
PDBsum; 1ZQX; -.
PDBsum; 1ZQY; -.
PDBsum; 1ZQZ; -.
PDBsum; 2BPC; -.
PDBsum; 2BPF; -.
PDBsum; 2BPG; -.
PDBsum; 2VAN; -.
PDBsum; 3K75; -.
PDBsum; 3LQC; -.
PDBsum; 3UXN; -.
PDBsum; 3UXO; -.
PDBsum; 3UXP; -.
PDBsum; 3V72; -.
PDBsum; 3V7J; -.
PDBsum; 3V7K; -.
PDBsum; 3V7L; -.
ProteinModelPortal; P06766; -.
SMR; P06766; -.
DIP; DIP-44707N; -.
IntAct; P06766; 1.
STRING; 10116.ENSRNOP00000026039; -.
BindingDB; P06766; -.
ChEMBL; CHEMBL4343; -.
iPTMnet; P06766; -.
PhosphoSitePlus; P06766; -.
PaxDb; P06766; -.
PRIDE; P06766; -.
Ensembl; ENSRNOT00000026039; ENSRNOP00000026039; ENSRNOG00000019150.
GeneID; 29240; -.
KEGG; rno:29240; -.
UCSC; RGD:3363; rat.
CTD; 5423; -.
RGD; 3363; Polb.
eggNOG; KOG2534; Eukaryota.
eggNOG; COG1796; LUCA.
GeneTree; ENSGT00530000063002; -.
HOGENOM; HOG000007787; -.
HOVERGEN; HBG002359; -.
InParanoid; P06766; -.
KO; K02330; -.
OMA; DLFNKNM; -.
OrthoDB; EOG091G0HMG; -.
PhylomeDB; P06766; -.
TreeFam; TF103002; -.
Reactome; R-RNO-110362; POLB-Dependent Long Patch Base Excision Repair.
Reactome; R-RNO-110373; Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
Reactome; R-RNO-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
Reactome; R-RNO-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
Reactome; R-RNO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
Reactome; R-RNO-5689880; Ub-specific processing proteases.
Reactome; R-RNO-73930; Abasic sugar-phosphate removal via the single-nucleotide replacement pathway.
EvolutionaryTrace; P06766; -.
PRO; PR:P06766; -.
Proteomes; UP000002494; Chromosome 16.
Bgee; ENSRNOG00000019150; Expressed in 10 organ(s), highest expression level in testis.
Genevisible; P06766; RN.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0005876; C:spindle microtubule; IEA:Ensembl.
GO; GO:0003684; F:damaged DNA binding; IDA:RGD.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:RGD.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0016829; F:lyase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
GO; GO:0006287; P:base-excision repair, gap-filling; IDA:RGD.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0071897; P:DNA biosynthetic process; IMP:RGD.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
GO; GO:0071707; P:immunoglobulin heavy chain V-D-J recombination; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0048535; P:lymph node development; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0006290; P:pyrimidine dimer repair; IDA:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0007435; P:salivary gland morphogenesis; IEA:Ensembl.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Ensembl.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
CDD; cd00141; NT_POLXc; 1.
Gene3D; 1.10.150.110; -; 1.
Gene3D; 3.30.210.10; -; 1.
InterPro; IPR002054; DNA-dir_DNA_pol_X.
InterPro; IPR019843; DNA_pol-X_BS.
InterPro; IPR010996; DNA_pol_b-like_N.
InterPro; IPR028207; DNA_pol_B_palm_palm.
InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
InterPro; IPR037160; DNA_Pol_thumb_sf.
InterPro; IPR022312; DNA_pol_X.
InterPro; IPR002008; DNA_pol_X_beta-like.
InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
InterPro; IPR029398; PolB_thumb.
Pfam; PF14792; DNA_pol_B_palm; 1.
Pfam; PF14791; DNA_pol_B_thumb; 1.
Pfam; PF10391; DNA_pol_lambd_f; 1.
Pfam; PF14716; HHH_8; 1.
PRINTS; PR00869; DNAPOLX.
PRINTS; PR00870; DNAPOLXBETA.
SMART; SM00278; HhH1; 2.
SMART; SM00483; POLXc; 1.
SUPFAM; SSF47802; SSF47802; 1.
PROSITE; PS00522; DNA_POLYMERASE_X; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA damage; DNA repair; DNA replication;
DNA synthesis; DNA-binding; DNA-directed DNA polymerase;
Isopeptide bond; Lyase; Magnesium; Metal-binding; Methylation;
Nucleotidyltransferase; Nucleus; Reference proteome; Sodium;
Transferase; Ubl conjugation.
CHAIN 1 335 DNA polymerase beta.
/FTId=PRO_0000218780.
REGION 183 192 DNA binding.
ACT_SITE 72 72 Schiff-base intermediate with DNA.
{ECO:0000250}.
METAL 101 101 Sodium; via carbonyl oxygen.
METAL 103 103 Sodium; via carbonyl oxygen.
METAL 106 106 Sodium; via carbonyl oxygen.
METAL 190 190 Magnesium 1.
METAL 190 190 Magnesium 2.
METAL 192 192 Magnesium 1.
METAL 192 192 Magnesium 2.
METAL 256 256 Magnesium 2.
MOD_RES 72 72 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8K409}.
MOD_RES 83 83 Omega-N-methylarginine; by PRMT6.
{ECO:0000250|UniProtKB:P06746}.
MOD_RES 152 152 Omega-N-methylarginine; by PRMT6.
{ECO:0000250|UniProtKB:P06746}.
CROSSLNK 41 41 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P06746}.
CROSSLNK 61 61 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P06746}.
CROSSLNK 81 81 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P06746}.
MUTAGEN 190 190 D->E,S: Loss of activity.
{ECO:0000269|PubMed:2036395}.
MUTAGEN 191 191 M->I: No loss of activity.
MUTAGEN 191 191 M->T: 50% loss of activity.
MUTAGEN 192 192 D->E,S: Loss of activity.
{ECO:0000269|PubMed:2036395}.
MUTAGEN 246 246 D->V: Misincorporates T nucleotide
opposite G/C template.
{ECO:0000269|PubMed:14563842}.
CONFLICT 228 228 L -> R (in Ref. 1; AAA41901, 2; AAB00389
and 4; AAA41900). {ECO:0000305}.
HELIX 13 28 {ECO:0000244|PDB:3UXO}.
STRAND 29 31 {ECO:0000244|PDB:1DK2}.
HELIX 33 48 {ECO:0000244|PDB:3UXO}.
HELIX 56 61 {ECO:0000244|PDB:3UXO}.
STRAND 62 64 {ECO:0000244|PDB:3V7L}.
HELIX 67 76 {ECO:0000244|PDB:3UXO}.
STRAND 79 81 {ECO:0000244|PDB:3UXO}.
HELIX 83 90 {ECO:0000244|PDB:3UXO}.
HELIX 92 100 {ECO:0000244|PDB:2VAN}.
TURN 101 104 {ECO:0000244|PDB:3V7L}.
HELIX 108 115 {ECO:0000244|PDB:2VAN}.
TURN 116 118 {ECO:0000244|PDB:2VAN}.
HELIX 122 126 {ECO:0000244|PDB:2VAN}.
HELIX 129 131 {ECO:0000244|PDB:2VAN}.
HELIX 134 141 {ECO:0000244|PDB:2VAN}.
TURN 142 144 {ECO:0000244|PDB:2VAN}.
HELIX 145 147 {ECO:0000244|PDB:2VAN}.
HELIX 152 169 {ECO:0000244|PDB:2VAN}.
STRAND 174 177 {ECO:0000244|PDB:2VAN}.
HELIX 179 182 {ECO:0000244|PDB:2VAN}.
STRAND 186 196 {ECO:0000244|PDB:2VAN}.
TURN 202 204 {ECO:0000244|PDB:1BPB}.
HELIX 208 220 {ECO:0000244|PDB:2VAN}.
STRAND 224 230 {ECO:0000244|PDB:2VAN}.
STRAND 232 239 {ECO:0000244|PDB:2VAN}.
STRAND 244 247 {ECO:0000244|PDB:3V7J}.
STRAND 253 259 {ECO:0000244|PDB:2VAN}.
HELIX 262 264 {ECO:0000244|PDB:2VAN}.
HELIX 265 273 {ECO:0000244|PDB:2VAN}.
HELIX 276 288 {ECO:0000244|PDB:2VAN}.
STRAND 291 293 {ECO:0000244|PDB:2VAN}.
STRAND 298 301 {ECO:0000244|PDB:2VAN}.
STRAND 303 305 {ECO:0000244|PDB:3UXO}.
HELIX 316 322 {ECO:0000244|PDB:2VAN}.
HELIX 330 332 {ECO:0000244|PDB:2VAN}.
SEQUENCE 335 AA; 38327 MW; BBF8498C0D3FBFC9 CRC64;
MSKRKAPQET LNGGITDMLV ELANFEKNVS QAIHKYNAYR KAASVIAKYP HKIKSGAEAK
KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVTGIGPSA ARKLVDEGIK
TLEDLRKNED KLNHHQRIGL KYFEDFEKRI PREEMLQMQD IVLNEVKKLD PEYIATVCGS
FRRGAESSGD MDVLLTHPNF TSESSKQPKL LHRVVEQLQK VRFITDTLSK GETKFMGVCQ
LPSENDENEY PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP
LGVTGVAGEP LPVDSEQDIF DYIQWRYREP KDRSE


Related products :

Catalog number Product name Quantity
EIAAB29846 Homo sapiens,Human,PAP-beta,PAPOLB,PAPT,Poly(A) polymerase beta,Polynucleotide adenylyltransferase beta,Testis-specific poly(A) polymerase
EIAAB29845 Mouse,Mus musculus,PAP-beta,Papolb,Papt,Poly(A) polymerase beta,Polynucleotide adenylyltransferase beta,Testis-specific poly(A) polymerase,Tpap
EIAAB11829 DNA polymerase beta-2,DNA polymerase kappa,DNA polymerase lambda,Homo sapiens,Human,Pol beta2,Pol Lambda,POLL
20-272-190715 RNA polymerase beta - Mouse monoclonal [8RB13] to RNA polymerase beta Monoclonal 0.05 ml
20-272-192241 DNA Polymerase beta - Mouse monoclonal [61] to DNA Polymerase beta; Monoclonal 0.25 ml
30-455 POLR3B belongs to the RNA polymerase beta chain family. DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. POLR3B is th 0.05 mg
PCR-253 Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: PCR Control Kit, Kit Amplification of a beta-actin gene fragment from human genomic DNA 500reactions
EIAAB11819 DNA polymerase gamma accessory 55 kDa subunit,DNA polymerase subunit gamma-2, mitochondrial,Homo sapiens,Human,Mitochondrial DNA polymerase accessory subunit,MtPolB,MTPOLB,p55,POLG2,PolG-beta
EIAAB11821 DNA polymerase gamma accessory 55 kDa subunit,DNA polymerase subunit gamma-2, mitochondrial,Mitochondrial DNA polymerase accessory subunit,Mouse,MtPolB,Mtpolb,Mus musculus,p55,Polg2,PolG-beta
EIAAB11820 Bos taurus,Bovine,DNA polymerase subunit gamma-2, mitochondrial,Mitochondrial DNA polymerase accessory subunit,MtPolB,MTPOLB,POLG2,PolG-beta
PCR-207S Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: Pfu-X Polymerase, S pack Proofreading DNA polymerase for highest accuracy 100units
PCR-207L Polymerase chain reaction PCR and reverse transcriptase polymerase chain reaction RT PCR products: Pfu-X Polymerase, L pack Proofreading DNA polymerase for highest accuracy 500units
PCR-603L Gene specific polymerase chain reaction PCR kits: T7 RNA Polymerase, L pack RNA Polymerase 10units
PCR-603S Gene specific polymerase chain reaction PCR kits: T7 RNA Polymerase, S pack RNA Polymerase 2units
PCR-604L Gene specific polymerase chain reaction PCR kits: SP6 RNA Polymerase, L pack RNA Polymerase 10units
PCR-604S Gene specific polymerase chain reaction PCR kits: SP6 RNA Polymerase, S pack RNA Polymerase 2units
orb90215 Pfu DNA Polymerase protein Pfu DNA Polymerase is thermo-stable enzyme having Mw of about 90kDa. Pfu DNA Polymerase is derived from E.coli that and cloned from Pyrococcus furiosus strain Vc1 DSM3638. P 100 U
EIAAB35750 DNA-directed RNA polymerase I subunit E,DNA-directed RNA polymerase I subunit RPA49,Homo sapiens,Human,PAF53,POLR1E,PRAF1,RNA polymerase I subunit A49,RNA polymerase I-associated factor 1,RNA polymera
EIAAB35749 DNA-directed RNA polymerase I subunit E,DNA-directed RNA polymerase I subunit RPA49,Mouse,Mus musculus,Paf53,Polr1e,Praf1,RNA polymerase I subunit A49,RNA polymerase I-associated factor 1,RNA polymera
EIAAB41304 Mouse,Mus musculus,Paf65b,PAF65-beta,PCAF-associated factor 65 beta,Taf5l,TAF5-like RNA polymerase II p300_CBP-associated factor-associated factor 65 kDa subunit 5L
10-101 DNA polymerase Beta (Rat) 20 ug
10-102 DNA polymerase Beta (Rat) 100 ug
EIAAB41303 Homo sapiens,Human,PAF65B,PAF65-beta,PCAF-associated factor 65 beta,TAF5L,TAF5-like RNA polymerase II p300_CBP-associated factor-associated factor 65 kDa subunit 5L
18-003-42245 TAF5-like RNA polymerase II p300_CBP-associated factor-associated factor 65 kDa subunit 5L - PCAF-associated factor 65 beta; PAF65-beta Polyclonal 0.1 mg Protein A
EIAAB35809 DNA-directed RNA polymerase III subunit K,DNA-directed RNA polymerase III subunit RPC10,Homo sapiens,hRPC11,HsC11p,Human,My010,POLR3K,RNA polymerase III 12.5 kDa subunit,RNA polymerase III subunit C10


 

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 Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | 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

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
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 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
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | 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
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

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