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

DNA topoisomerase 2-beta (EC 5.99.1.3) (DNA topoisomerase II, beta isozyme)

 TOP2B_CRILO             Reviewed;        1612 AA.
Q64399;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 123.
RecName: Full=DNA topoisomerase 2-beta;
EC=5.99.1.3;
AltName: Full=DNA topoisomerase II, beta isozyme;
Name=TOP2B;
Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese
hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10030;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=7495861; DOI=10.1016/0167-4781(95)00164-C;
Dereuddre S., Frey S., Delaporte C., Jacquemin-Sablon A.;
"Cloning and characterization of full-length cDNAs coding for the DNA
topoisomerase II beta from Chinese hamster lung cells sensitive and
resistant 9-OH-ellipticine.";
Biochim. Biophys. Acta 1264:178-182(1995).
-!- FUNCTION: Control of topological states of DNA by transient
breakage and subsequent rejoining of DNA strands. Topoisomerase II
makes double-strand breaks. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
of double-stranded DNA. {ECO:0000255|PROSITE-ProRule:PRU00995}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00995};
Note=Binds two Mg(2+) per subunit. The magnesium ions form salt
bridges with both the protein and the DNA. Can also accept other
divalent metal cations, such as Mn(2+) or Ca(2+).
{ECO:0000255|PROSITE-ProRule:PRU00995};
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q02880}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
-!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
negative and positive supercoils, whereas prokaryotic enzymes
relax only negative supercoils.
-!- SIMILARITY: Belongs to the type II topoisomerase 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; X86455; CAA60173.1; -; mRNA.
ProteinModelPortal; Q64399; -.
SMR; Q64399; -.
PRIDE; Q64399; -.
HOVERGEN; HBG052998; -.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003916; F:DNA topoisomerase activity; ISS:UniProtKB.
GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043021; F:ribonucleoprotein complex binding; ISS:UniProtKB.
GO; GO:0006265; P:DNA topological change; ISS:UniProtKB.
CDD; cd00075; HATPase_c; 1.
CDD; cd00187; TOP4c; 1.
CDD; cd03365; TOPRIM_TopoIIA; 1.
Gene3D; 1.10.268.10; -; 1.
Gene3D; 3.30.230.10; -; 1.
Gene3D; 3.30.565.10; -; 1.
Gene3D; 3.40.50.670; -; 2.
Gene3D; 3.90.199.10; -; 3.
InterPro; IPR012542; DTHCT.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
InterPro; IPR001241; Topo_IIA.
InterPro; IPR013760; Topo_IIA-like_dom_sf.
InterPro; IPR002205; Topo_IIA_A/C.
InterPro; IPR013758; Topo_IIA_A/C_ab.
InterPro; IPR013757; Topo_IIA_A_a_sf.
InterPro; IPR013759; Topo_IIA_B_C.
InterPro; IPR013506; Topo_IIA_bsu_dom2.
InterPro; IPR018522; TopoIIA_CS.
InterPro; IPR031660; TOPRIM_C.
InterPro; IPR006171; TOPRIM_domain.
InterPro; IPR034157; TOPRIM_TopoII.
PANTHER; PTHR10169; PTHR10169; 1.
Pfam; PF00204; DNA_gyraseB; 1.
Pfam; PF00521; DNA_topoisoIV; 1.
Pfam; PF08070; DTHCT; 1.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF01751; Toprim; 1.
Pfam; PF16898; TOPRIM_C; 1.
SMART; SM00433; TOP2c; 1.
SMART; SM00434; TOP4c; 1.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF55874; SSF55874; 1.
SUPFAM; SSF56719; SSF56719; 1.
PROSITE; PS00177; TOPOISOMERASE_II; 1.
PROSITE; PS50880; TOPRIM; 1.
2: Evidence at transcript level;
Acetylation; ATP-binding; DNA-binding; Isomerase; Isopeptide bond;
Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Topoisomerase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q64511}.
CHAIN 2 1612 DNA topoisomerase 2-beta.
/FTId=PRO_0000145368.
DOMAIN 464 581 Toprim. {ECO:0000255|PROSITE-
ProRule:PRU00995}.
NP_BIND 157 159 ATP. {ECO:0000250}.
NP_BIND 170 177 ATP. {ECO:0000250}.
NP_BIND 385 387 ATP. {ECO:0000250}.
REGION 351 353 Interaction with DNA. {ECO:0000250}.
REGION 999 1008 Interaction with DNA. {ECO:0000250}.
ACT_SITE 814 814 O-(5'-phospho-DNA)-tyrosine intermediate.
{ECO:0000250}.
METAL 470 470 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
METAL 550 550 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
METAL 550 550 Magnesium 2. {ECO:0000255|PROSITE-
ProRule:PRU00995}.
METAL 552 552 Magnesium 2. {ECO:0000255|PROSITE-
ProRule:PRU00995}.
BINDING 100 100 ATP. {ECO:0000250}.
BINDING 129 129 ATP. {ECO:0000250}.
SITE 498 498 Interaction with DNA.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
SITE 501 501 Interaction with DNA.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
SITE 670 670 Interaction with DNA.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
SITE 671 671 Interaction with DNA.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
SITE 732 732 Interaction with DNA.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
SITE 766 766 Interaction with DNA.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
SITE 813 813 Transition state stabilizer.
{ECO:0000250}.
SITE 865 865 Important for DNA bending; intercalates
between base pairs of target DNA.
{ECO:0000250}.
SITE 940 940 Interaction with DNA.
{ECO:0000255|PROSITE-ProRule:PRU00995}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q64511}.
MOD_RES 3 3 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q64511}.
MOD_RES 1224 1224 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1280 1280 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1324 1324 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1328 1328 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1330 1330 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1332 1332 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1346 1346 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1358 1358 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q64511}.
MOD_RES 1363 1363 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1387 1387 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1390 1390 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1400 1400 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1408 1408 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1411 1411 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1428 1428 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1439 1439 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1441 1441 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1448 1448 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1453 1453 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1460 1460 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1509 1509 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1511 1511 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1513 1513 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1537 1537 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1539 1539 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1562 1562 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1563 1563 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1568 1568 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1596 1596 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q02880}.
MOD_RES 1600 1600 Phosphoserine.
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 21 21 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 165 165 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 166 166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 216 216 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 287 287 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 355 355 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 361 361 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 425 425 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 427 427 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 434 434 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 588 588 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 593 593 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 623 623 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 631 631 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 634 634 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 664 664 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 700 700 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1080 1080 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1202 1202 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1205 1205 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1214 1214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1215 1215 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1238 1238 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1250 1250 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1259 1259 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1311 1311 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1315 1315 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1385 1385 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1427 1427 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1443 1443 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
CROSSLNK 1477 1477 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q02880}.
SEQUENCE 1612 AA; 182075 MW; C01D6FC40620FC68 CRC64;
MAKSSLAGAD GALTWVNNAA KKEELETSNK NDSSKKLSVE RVYQKKTQLE HILLRPDTYI
GSVEPLTQLM WVYDEDVGMN CREVTFVPGL YKIFDEILVN AADNKQRDKN MTCIKVSIDP
ESNIISIWNN GKGIPVVEHK VEKVYVPALI FGQLLTSSNY DDDEKKVTGG RNGYGAKLCN
IFSTKFTVET ACKEYKHSFK QTWMNNMMKT SEAKIKHFDG EDYTCITFQP DLAKFKMEKL
DKDIVALMTR RAYDLAGSCK GVKVMFNGKK LPVNGFRSYV DLYVKDKLDE TGVALKVIHE
LANERWDVCL TLSEKGFQQI SFVNSIATTK GGRHVDYVVD QVVGKLIEVV KKKNKAGVSV
KPFQVKNHIW VFINCLIENP TFDSQTKENM TLQPKSFGSK CQLSEKFFKA ASNCGIVESI
LNWVKFKAQT QLNKKCSSVK YSKIKGIPKL DDANDAGGKH SLECTLILTE GDSAKSLAVS
GLGVIGRDRY GVFPLRGKIL NVREASHKQI MENAEINNII KIVGLQYKKS YDDAESLKTL
RYGKIMIMTD QDQDGSHIKG LLINFIHHNW PSLLKHGFLE EFITPIVKAS KNKQELSFYS
IPEFDEWKKH IENQKAWKIK YYKGLGTSTA KEAKEYFADM ERHRILFRYA GPEDDAAITL
AFSKKKIDDR KEWLTNFMED RRQRRLHGLP EQFLYGTATK HLTYNDFINK ELILFSNSDN
ERSIPSLVDG FKPGQRKVLF TCFKRNDKRE VKVAQLAGSV AEMSAYHHGE QALMMTIVNL
AQNFVGSNNI NLLQPIGQFG TRLHGGKDAA SPRYIFTMLS SLARLLFPAV DDNLLKFLYD
DNQRVEPEWY IPIIPMVLIN GAEGIGTGWA CKLPNYDARE IVNNVRRMLD GLDPHPMLPN
YKNFKGTIQE LGQNQYAVSG EIFVVDRNTV EITELPVRTW TQVYKEQVLE PMLNGTDKTP
ALISDYKEYH TDTTVKFVVK MTEEKLAQAE AAGLHKVFKL QTTLTCNSMV LFDHMGCLKK
YETVQDILKE FFDLRLSYYG LRKEWLVGML GAESTKLNNQ ARFILEKIQG KITIENRSKK
DLIQMLVQRG YESDPVRAWK EAQEKAAEEE DTQNQHDDSS SDSGTPSGPD FNYILNMSLW
SLTKEKVEEL IKQRDTKGRE VNDLKRKSPS DLWKEDLAAF VEELDKVEAQ EREDILAGMS
GKAIKGKVGK PKVKKLQLEE TMPSPYGRRI VPEITAMKAD ASRKLLKKKK GDPDTPVVKV
EFDEEFSGTP VEGTGEETLT PSAPVNKGPK PKREKKEPGT RVRKTPTSAG KPNAKKVKKR
NPWSDDESKS ESDLEETEPV VIPRDSLLRR AAAERPKYTF DFSEEEEEDA DDDDDNNDLE
ELKVKASPIT NDGEDEFVPS DGLDKDEYAF SPGKSKATPE KSSHDKKSQD FGNLFSFPSY
SQKSEDDSAK FDSNEEDTAS VFTPSFGLKQ TDKVPSKTVA AKKGKPPSDT APKAKRAPKQ
KKVVETVNSD SDSEFGIPKK TTTPKGKGRG AKKRKASGSE NEGDYNPGRK PSKTASKKPK
KTSFDQDSDV DIFPSDFTSE PPALPRTGRA RKEVKYFAES DEEEDVDFAM FN


Related products :

Catalog number Product name Quantity
EIAAB43439 DNA topoisomerase 2-beta,DNA topoisomerase II, beta isozyme,Homo sapiens,Human,TOP2B
EIAAB43438 DNA topoisomerase 2-beta,DNA topoisomerase II, beta isozyme,Mouse,Mus musculus,Top2b
18-272-196475 Topoisomerase II beta - Rabbit polyclonal to Topoisomerase II beta; EC 5.99.1.3; DNA topoisomerase II. beta isozyme Polyclonal 0.5 ml
18-272-196476 Topoisomerase II beta prediluted - Rabbit polyclonal to Topoisomerase II beta prediluted; EC 5.99.1.3; DNA topoisomerase II. beta isozyme Polyclonal 7 ml
EIAAB43437 Chicken,DNA topoisomerase 2-beta,DNA topoisomerase II, beta isozyme,Gallus gallus,TOP2B
EIAAB43442 DNA topoisomerase 3-beta-1,DNA topoisomerase III beta-1,Homo sapiens,Human,TOP3B,TOP3B1
EIAAB43443 DNA topoisomerase 3-beta-1,DNA topoisomerase III beta-1,Mouse,Mus musculus,Top3b,Top3b1
GWB-66C822 DNA Topoisomerase II Beta Isozyme (TOP2B) Rabbit anti-Human Polyclonal Antibody
GWB-484571 DNA Topoisomerase II Beta Isozyme (TOP2B) Rabbit anti-Mouse Polyclonal (aa1554-1565) Antibody
EIAAB43432 DNA topoisomerase 2-alpha,DNA topoisomerase II, alpha isozyme,Homo sapiens,Human,TOP2,TOP2A
EIAAB43434 DNA topoisomerase 2-alpha,DNA topoisomerase II, alpha isozyme,Rat,Rattus norvegicus,Top2,Top-2,Top2a
EIAAB43435 DNA topoisomerase 2-alpha,DNA topoisomerase II, alpha isozyme,Mouse,Mus musculus,Top2,Top-2,Top2a
20-272-191336 Topoisomerase II alpha - Mouse monoclonal [SWT3D1] to Topoisomerase II alpha; EC 5.99.1.3; DNA topoisomerase II. alpha isozyme Monoclonal 0.5 ml
18-272-195679 Topoisomerase II alpha - Rabbit polyclonal [BL893] to Topoisomerase II alpha; EC 5.99.1.3; DNA topoisomerase II. alpha isozyme Polyclonal 0.05 mg
EIAAB43444 DNA topoisomerase 2-binding protein 1,DNA topoisomerase II-beta-binding protein 1,DNA topoisomerase II-binding protein 1,Homo sapiens,Human,KIAA0259,TopBP1,TOPBP1
EIAAB43433 DNA topoisomerase 2-alpha,DNA topoisomerase II, alpha isozyme,Pig,Sus scrofa,TOP2A
EIAAB43445 DNA topoisomerase 2-binding protein 1,DNA topoisomerase II-beta-binding protein 1,DNA topoisomerase II-binding protein 1,Kiaa0259,Mouse,Mus musculus,TopBP1,Topbp1
18-003-42906 DNA topoisomerase 2-alpha - EC 5.99.1.3; DNA topoisomerase II. alpha isozyme Polyclonal 0.1 mg Protein A
EIAAB43436 Chicken,DNA topoisomerase 2-alpha,DNA topoisomerase II, alpha isozyme,Gallus gallus,TOP2A
TOP2B21-A Anti-human Topoisomerase II beta (TOP2 beta) protein IgG 100 ug
TOP2B21-A Anti_human Topoisomerase II beta (TOP2 beta) protein IgG 100 ug
20-272-190787 Topoisomerase I - Mouse monoclonal [Mab1] to Topoisomerase I; EC 5.99.1.2; DNA topoisomerase I Monoclonal 0.05 ml
RP 124-05 Topoisomerase II beta; 0.5ml
EIAAB43428 DNA topoisomerase 1,DNA topoisomerase I,Homo sapiens,Human,TOP1
EIAAB43427 DNA topoisomerase 1,DNA topoisomerase I,Rat,Rattus norvegicus,Top1


 

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