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

DNA oxidative demethylase ALKBH2 (EC 1.14.11.33) (Alkylated DNA repair protein alkB homolog 2) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2) (Oxy DC1)

 ALKB2_HUMAN             Reviewed;         261 AA.
Q6NS38; A4PET2; Q5XLE3;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
12-SEP-2018, entry version 124.
RecName: Full=DNA oxidative demethylase ALKBH2;
EC=1.14.11.33;
AltName: Full=Alkylated DNA repair protein alkB homolog 2;
AltName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2;
AltName: Full=Oxy DC1;
Name=ALKBH2; Synonyms=ABH2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Lin Y., Xie Y., Mao Y.;
"Cloning and expression of human 2OG-Fe(II) oxy DC1.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=17979886; DOI=10.1111/j.1582-4934.2007.00094.x;
Tsujikawa K., Koike K., Kitae K., Shinkawa A., Arima H., Suzuki T.,
Tsuchiya M., Makino Y., Furukawa T., Konishi N., Yamamoto H.;
"Expression and sub-cellular localization of human ABH family
molecules.";
J. Cell. Mol. Med. 11:1105-1116(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[5]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=12486230; DOI=10.1073/pnas.262589799;
Duncan T., Trewick S.C., Koivisto P., Bates P.A., Lindahl T.,
Sedgwick B.;
"Reversal of DNA alkylation damage by two human dioxygenases.";
Proc. Natl. Acad. Sci. U.S.A. 99:16660-16665(2002).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12594517; DOI=10.1038/nature01363;
Aas P.A., Otterlei M., Falnes P.O., Vaagboe C.B., Skorpen F.,
Akbari M., Sundheim O., Bjoeraas M., Slupphaug G., Seeberg E.,
Krokan H.E.;
"Human and bacterial oxidative demethylases repair alkylation damage
in both RNA and DNA.";
Nature 421:859-863(2003).
[7]
FUNCTION, MUTAGENESIS OF ASP-173 AND HIS-236, AND TISSUE SPECIFICITY.
PubMed=16174769; DOI=10.1074/jbc.M509881200;
Lee D.-H., Jin S.-G., Cai S., Chen Y., Pfeifer G.P., O'Connor T.R.;
"Repair of methylation damage in DNA and RNA by mammalian AlkB
homologues.";
J. Biol. Chem. 280:39448-39459(2005).
[8]
FUNCTION, ACTIVITY REGULATION, AND COFACTOR.
PubMed=18519673; DOI=10.1158/0008-5472.CAN-08-0796;
Ringvoll J., Moen M.N., Nordstrand L.M., Meira L.B., Pang B.,
Bekkelund A., Dedon P.C., Bjelland S., Samson L.D., Falnes P.O.,
Klungland A.;
"AlkB homologue 2-mediated repair of ethenoadenine lesions in
mammalian DNA.";
Cancer Res. 68:4142-4149(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 56-258 IN COMPLEXES WITH
DS-DNA; ALPHA-KETOGLUTARATE AND METAL IONS, FUNCTION, AND COFACTOR.
PubMed=18432238; DOI=10.1038/nature06889;
Yang C.G., Yi C., Duguid E.M., Sullivan C.T., Jian X., Rice P.A.,
He C.;
"Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to
dsDNA.";
Nature 452:961-965(2008).
[11]
X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 56-261 IN COMPLEXES WITH
DOUBLE-STRANDED DNA CONTAINING 1-METHYLADENINE OR 3-METHYLCYTOSINE.
PubMed=20223766; DOI=10.1093/nar/gkq129;
Lu L., Yi C., Jian X., Zheng G., He C.;
"Structure determination of DNA methylation lesions N1-meA and N3-meC
in duplex DNA using a cross-linked protein-DNA system.";
Nucleic Acids Res. 38:4415-4425(2010).
-!- FUNCTION: Dioxygenase that repairs alkylated DNA and RNA
containing 1-methyladenine and 3-methylcytosine by oxidative
demethylation. Can also repair alkylated DNA containing 1-
ethenoadenine (in vitro). Has strong preference for double-
stranded DNA. Has low efficiency with single-stranded substrates.
Requires molecular oxygen, alpha-ketoglutarate and iron.
{ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:12594517,
ECO:0000269|PubMed:16174769, ECO:0000269|PubMed:18432238,
ECO:0000269|PubMed:18519673}.
-!- CATALYTIC ACTIVITY: DNA-base-CH(3) + 2-oxoglutarate + O(2) = DNA-
base + formaldehyde + succinate + CO(2).
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
ECO:0000269|PubMed:18432238, ECO:0000269|PubMed:18519673};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00805, ECO:0000269|PubMed:18432238,
ECO:0000269|PubMed:18519673};
-!- ACTIVITY REGULATION: Activated by ascorbate and magnesium ions.
{ECO:0000269|PubMed:12486230, ECO:0000269|PubMed:18519673}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12486230,
ECO:0000269|PubMed:12594517}. Note=Detected in replication foci
during S-phase.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6NS38-1; Sequence=Displayed;
Name=2;
IsoId=Q6NS38-2; Sequence=VSP_042923;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in colon, small intestine, ovary,
testis, prostate, skeletal muscle, heart, liver and urinary
bladder. {ECO:0000269|PubMed:12486230,
ECO:0000269|PubMed:16174769}.
-!- SIMILARITY: Belongs to the alkB 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; AY754389; AAV28301.1; -; mRNA.
EMBL; AB277859; BAF56576.1; -; mRNA.
EMBL; AC011596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC070489; AAH70489.1; -; mRNA.
CCDS; CCDS31897.1; -. [Q6NS38-1]
CCDS; CCDS55883.1; -. [Q6NS38-2]
RefSeq; NP_001001655.1; NM_001001655.2. [Q6NS38-1]
RefSeq; NP_001138846.1; NM_001145374.1. [Q6NS38-1]
RefSeq; NP_001138847.1; NM_001145375.1. [Q6NS38-1]
RefSeq; NP_001192108.1; NM_001205179.1. [Q6NS38-2]
RefSeq; NP_001192109.1; NM_001205180.1. [Q6NS38-2]
RefSeq; XP_005253892.1; XM_005253835.4. [Q6NS38-1]
RefSeq; XP_005253893.1; XM_005253836.1. [Q6NS38-2]
UniGene; Hs.374458; -.
PDB; 3BTX; X-ray; 2.00 A; A=56-258.
PDB; 3BTY; X-ray; 2.35 A; A=56-258.
PDB; 3BTZ; X-ray; 3.00 A; A=57-258.
PDB; 3BU0; X-ray; 2.50 A; A=56-258.
PDB; 3BUC; X-ray; 2.59 A; A=56-258.
PDB; 3H8O; X-ray; 2.50 A; A=56-261.
PDB; 3H8R; X-ray; 1.77 A; A=56-261.
PDB; 3H8X; X-ray; 2.50 A; A=56-261.
PDB; 3RZG; X-ray; 1.62 A; A=56-261.
PDB; 3RZH; X-ray; 2.25 A; A=56-261.
PDB; 3RZJ; X-ray; 2.50 A; A=56-261.
PDB; 3RZK; X-ray; 2.78 A; A=56-261.
PDB; 3RZL; X-ray; 2.60 A; A/D=56-261.
PDB; 3RZM; X-ray; 3.06 A; A=56-260.
PDB; 3S57; X-ray; 1.60 A; A=56-258.
PDB; 3S5A; X-ray; 1.70 A; A=56-258.
PDB; 4MG2; X-ray; 2.30 A; A=56-258.
PDB; 4MGT; X-ray; 2.60 A; A=56-258.
PDBsum; 3BTX; -.
PDBsum; 3BTY; -.
PDBsum; 3BTZ; -.
PDBsum; 3BU0; -.
PDBsum; 3BUC; -.
PDBsum; 3H8O; -.
PDBsum; 3H8R; -.
PDBsum; 3H8X; -.
PDBsum; 3RZG; -.
PDBsum; 3RZH; -.
PDBsum; 3RZJ; -.
PDBsum; 3RZK; -.
PDBsum; 3RZL; -.
PDBsum; 3RZM; -.
PDBsum; 3S57; -.
PDBsum; 3S5A; -.
PDBsum; 4MG2; -.
PDBsum; 4MGT; -.
ProteinModelPortal; Q6NS38; -.
SMR; Q6NS38; -.
BioGrid; 125741; 12.
IntAct; Q6NS38; 7.
STRING; 9606.ENSP00000343021; -.
DrugBank; DB00126; Vitamin C.
iPTMnet; Q6NS38; -.
PhosphoSitePlus; Q6NS38; -.
BioMuta; ALKBH2; -.
DMDM; 74736661; -.
EPD; Q6NS38; -.
MaxQB; Q6NS38; -.
PaxDb; Q6NS38; -.
PeptideAtlas; Q6NS38; -.
PRIDE; Q6NS38; -.
ProteomicsDB; 66621; -.
ProteomicsDB; 66622; -. [Q6NS38-2]
DNASU; 121642; -.
Ensembl; ENST00000343075; ENSP00000343021; ENSG00000189046. [Q6NS38-1]
Ensembl; ENST00000429722; ENSP00000398181; ENSG00000189046. [Q6NS38-1]
Ensembl; ENST00000440112; ENSP00000399820; ENSG00000189046. [Q6NS38-2]
Ensembl; ENST00000619381; ENSP00000478765; ENSG00000189046. [Q6NS38-2]
GeneID; 121642; -.
KEGG; hsa:121642; -.
UCSC; uc001tnx.3; human. [Q6NS38-1]
CTD; 121642; -.
DisGeNET; 121642; -.
EuPathDB; HostDB:ENSG00000189046.10; -.
GeneCards; ALKBH2; -.
HGNC; HGNC:32487; ALKBH2.
HPA; CAB011198; -.
HPA; HPA045392; -.
HPA; HPA051976; -.
MIM; 610602; gene.
neXtProt; NX_Q6NS38; -.
OpenTargets; ENSG00000189046; -.
PharmGKB; PA143485292; -.
eggNOG; ENOG410IIVX; Eukaryota.
eggNOG; COG3145; LUCA.
GeneTree; ENSGT00530000063618; -.
HOGENOM; HOG000263606; -.
HOVERGEN; HBG080832; -.
InParanoid; Q6NS38; -.
KO; K10859; -.
OMA; QATYGDT; -.
OrthoDB; EOG091G0S0P; -.
PhylomeDB; Q6NS38; -.
TreeFam; TF331732; -.
BRENDA; 1.14.11.33; 2681.
Reactome; R-HSA-112122; ALKBH2 mediated reversal of alkylation damage.
ChiTaRS; ALKBH2; human.
EvolutionaryTrace; Q6NS38; -.
GenomeRNAi; 121642; -.
PRO; PR:Q6NS38; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000189046; Expressed in 167 organ(s), highest expression level in prostate gland.
CleanEx; HS_ALKBH2; -.
ExpressionAtlas; Q6NS38; baseline and differential.
Genevisible; Q6NS38; HS.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0103053; F:1-ethyladenine demethylase activity; IEA:UniProtKB-EC.
GO; GO:0051747; F:cytosine C-5 DNA demethylase activity; IDA:UniProtKB.
GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; IDA:UniProtKB.
GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:UniProtKB.
GO; GO:0080111; P:DNA demethylation; TAS:BHF-UCL.
GO; GO:0070989; P:oxidative demethylation; TAS:BHF-UCL.
GO; GO:0035511; P:oxidative DNA demethylation; IDA:UniProtKB.
Gene3D; 2.60.120.590; -; 1.
InterPro; IPR027450; AlkB-like.
InterPro; IPR037151; AlkB-like_sf.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
PROSITE; PS51471; FE2OG_OXY; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Dioxygenase;
DNA damage; DNA repair; Iron; Magnesium; Metal-binding; Nucleus;
Oxidoreductase; Polymorphism; Reference proteome.
CHAIN 1 261 DNA oxidative demethylase ALKBH2.
/FTId=PRO_0000239275.
DOMAIN 152 257 Fe2OG dioxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
REGION 102 104 Substrate binding.
{ECO:0000269|PubMed:18432238}.
REGION 122 124 Substrate binding.
{ECO:0000269|PubMed:18432238}.
REGION 159 161 Alpha-ketoglutarate binding.
{ECO:0000269|PubMed:18432238}.
REGION 248 254 Alpha-ketoglutarate binding.
{ECO:0000269|PubMed:18432238}.
METAL 171 171 Iron; catalytic.
{ECO:0000269|PubMed:18432238}.
METAL 173 173 Iron; catalytic.
{ECO:0000269|PubMed:18432238}.
METAL 236 236 Iron; catalytic.
{ECO:0000269|PubMed:18432238}.
BINDING 174 174 Substrate. {ECO:0000269|PubMed:18432238}.
VAR_SEQ 95 261 ALARVQVFGKWHSVPRKQATYGDAGLTYTFSGLTLSPKPWI
PVLERIRDHVSGVTGQTFNFVLINRYKDGCDHIGEHRDDER
ELAPGSPIASVSFGACRDFVFRHKDSRGKSPSRRVAVVRLP
LAHGSLLMMNHPTNTHWYHSLPVRKKVLAPRVNLTFRKILL
TKK -> IKMAVTTSGSTEMMKENWPLGAPLPLSPSVPAET
LSSGIRIPVGKAPPGGWRWSGCRWPTGAY (in isoform
2). {ECO:0000303|PubMed:17979886}.
/FTId=VSP_042923.
VARIANT 203 203 R -> H (in dbSNP:rs33962311).
/FTId=VAR_048223.
MUTAGEN 173 173 D->A: Loss of activity.
{ECO:0000269|PubMed:16174769}.
MUTAGEN 236 236 H->A: Reduced activity.
{ECO:0000269|PubMed:16174769}.
CONFLICT 43 43 R -> G (in Ref. 1; AAV28301).
{ECO:0000305}.
STRAND 58 62 {ECO:0000244|PDB:3S57}.
STRAND 65 71 {ECO:0000244|PDB:3S57}.
HELIX 75 88 {ECO:0000244|PDB:3S57}.
HELIX 94 97 {ECO:0000244|PDB:3S57}.
STRAND 98 101 {ECO:0000244|PDB:3S57}.
STRAND 104 107 {ECO:0000244|PDB:3S57}.
STRAND 109 116 {ECO:0000244|PDB:3S57}.
STRAND 122 124 {ECO:0000244|PDB:3S57}.
STRAND 127 129 {ECO:0000244|PDB:3S57}.
HELIX 136 149 {ECO:0000244|PDB:3S57}.
STRAND 154 163 {ECO:0000244|PDB:3S57}.
STRAND 168 171 {ECO:0000244|PDB:3S57}.
STRAND 176 178 {ECO:0000244|PDB:3RZG}.
STRAND 184 191 {ECO:0000244|PDB:3S57}.
STRAND 193 199 {ECO:0000244|PDB:3S57}.
HELIX 200 202 {ECO:0000244|PDB:3S57}.
STRAND 204 206 {ECO:0000244|PDB:3S57}.
STRAND 214 218 {ECO:0000244|PDB:3S57}.
STRAND 222 227 {ECO:0000244|PDB:3S57}.
HELIX 230 233 {ECO:0000244|PDB:3S57}.
STRAND 234 238 {ECO:0000244|PDB:3S57}.
STRAND 248 254 {ECO:0000244|PDB:3S57}.
SEQUENCE 261 AA; 29322 MW; A376E13F92621A01 CRC64;
MDRFLVKGAQ GGLLRKQEEQ EPTGEEPAVL GGDKESTRKR PRREAPGNGG HSAGPSWRHI
RAEGLDCSYT VLFGKAEADE IFQELEKEVE YFTGALARVQ VFGKWHSVPR KQATYGDAGL
TYTFSGLTLS PKPWIPVLER IRDHVSGVTG QTFNFVLINR YKDGCDHIGE HRDDERELAP
GSPIASVSFG ACRDFVFRHK DSRGKSPSRR VAVVRLPLAH GSLLMMNHPT NTHWYHSLPV
RKKVLAPRVN LTFRKILLTK K


Related products :

Catalog number Product name Quantity
CSB-EL001608BO Bovine Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit 96T
CSB-EL001608MO Mouse Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit 96T
CSB-EL001608HU Human Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit 96T
CSB-EL001608BO Bovine Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit SpeciesBovine 96T
CSB-EL001608HU Human Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit SpeciesHuman 96T
CSB-EL001608MO Mouse Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2(ALKBH2) ELISA kit SpeciesMouse 96T
ALKB2_BOVIN ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2; organism: Bovine; gene name: ALKBH2 96T
ALKB3_RAT Rat ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 96T
ALKBH3-970H Protein: Recombinant Human Alpha-Ketoglutarate-Dependent Dioxygenase AlkB Homolog 3, His-tagged 100ug
ALKBH3-970H Protein Recombinant Human Alpha-Ketoglutarate-Dependent Dioxygenase AlkB Homolog 3, His-tagged 100ug
ALKB3_MOUSE Mouse ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3 96T
ALKB2_MOUSE Mouse ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2 96T
CSB-EL001609RA Rat Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit 96T
CSB-EL001609MO Mouse Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit 96T
CSB-EL001609BO Bovine Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit 96T
CSB-EL001609RA Rat Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit SpeciesRat 96T
CSB-EL001609HU Human Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit 96T
CSB-EL001609BO Bovine Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit SpeciesBovine 96T
CSB-EL001609HU Human Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit SpeciesHuman 96T
CSB-EL001609MO Mouse Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3(ALKBH3) ELISA kit SpeciesMouse 96T
ALKB3_BOVIN ELISA Kit FOR Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3; organism: Bovine; gene name: ALKBH3 96T
ALKB1_HUMAN Human ELISA Kit FOR Alkylated DNA repair protein alkB homolog 1 96T
ALKB8_HUMAN Human ELISA Kit FOR Alkylated DNA repair protein alkB homolog 8 96T
CSB-EL001614HU Human Alkylated DNA repair protein alkB homolog 8(ALKBH8) ELISA kit 96T
CSB-EL001607HU Human Alkylated DNA repair protein alkB homolog 1(ALKBH1) ELISA kit 96T


 

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