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Cytochrome P450 2A6 (EC 1.14.13.-) (1,4-cineole 2-exo-monooxygenase) (CYPIIA6) (Coumarin 7-hydroxylase) (Cytochrome P450 IIA3) (Cytochrome P450(I))

 CP2A6_HUMAN             Reviewed;         494 AA.
P11509; A7YAE5; B2R7F6; P00190; P10890; Q16803; Q4VAT9; Q4VAU0;
Q4VAU1; Q9H1Z7; Q9UCU0; Q9UK48;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
20-DEC-2017, entry version 205.
RecName: Full=Cytochrome P450 2A6;
EC=1.14.13.-;
AltName: Full=1,4-cineole 2-exo-monooxygenase;
AltName: Full=CYPIIA6;
AltName: Full=Coumarin 7-hydroxylase;
AltName: Full=Cytochrome P450 IIA3;
AltName: Full=Cytochrome P450(I);
Name=CYP2A6; Synonyms=CYP2A3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-29 AND TYR-392.
TISSUE=Liver;
PubMed=2726448; DOI=10.1093/nar/17.8.2907;
Miles J.S., Bickmore W., Brook J.D., McLaren A.W., Meehan R.,
Wolf C.R.;
"Close linkage of the human cytochrome P450IIA and P450IIB gene
subfamilies: implications for the assignment of substrate
specificity.";
Nucleic Acids Res. 17:2907-2917(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIS-160 AND TYR-392.
TISSUE=Hepatocyte;
PubMed=2748347; DOI=10.1093/nar/17.12.4888;
Yamano S., Nagata K., Yamazoe Y., Kato R., Gelboin H.V.,
Gonzalez F.J.;
"cDNA and deduced amino acid sequences of human P450 IIA3 (CYP2A3).";
Nucleic Acids Res. 17:4888-4888(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-160 AND TYR-392, AND
CHARACTERIZATION OF VARIANT HIS-160.
TISSUE=Hepatocyte;
PubMed=2322567; DOI=10.1021/bi00457a031;
Yamano S., Tatsuno J., Gonzalez F.J.;
"The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human
liver microsomes.";
Biochemistry 29:1322-1329(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TYR-392.
TISSUE=Liver;
Zhuge J., Qian Y., Xie H., Yu Y.;
"Sequence of a new human cytochrome P450-2A6 cDNA.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-392.
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-160; CYS-203;
MET-365; TYR-392; ASP-418 AND ASP-419.
NIEHS SNPs program;
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TYR-392.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-160; TYR-392
AND ARG-476.
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).
[10]
PROTEIN SEQUENCE OF 1-20, FUNCTION, SUBCELLULAR LOCATION, INDUCTION,
AND TISSUE SPECIFICITY.
PubMed=1889415; DOI=10.1111/j.1432-1033.1991.tb16212.x;
Maurice M., Emiliani S., Dalet-Beluche I., Derancourt J., Lange R.;
"Isolation and characterization of a cytochrome P450 of the IIA
subfamily from human liver microsomes.";
Eur. J. Biochem. 200:511-517(1991).
[11]
PROTEIN SEQUENCE OF 1-13, FUNCTION, SUBCELLULAR LOCATION, INDUCTION,
AND TISSUE SPECIFICITY.
PubMed=1944238;
Yun C.H., Shimada T., Guengerich F.P.;
"Purification and characterization of human liver microsomal
cytochrome P-450 2A6.";
Mol. Pharmacol. 40:679-685(1991).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-164, AND VARIANT CYP2A6*6
GLN-128.
PubMed=11278503; DOI=10.1074/jbc.M009432200;
Kitagawa K., Kunugita N., Kitagawa M., Kawamoto T.;
"CYP2A6*6, a novel polymorphism in cytochrome p450 2A6, has a single
amino acid substitution (R128Q) that inactivates enzymatic activity.";
J. Biol. Chem. 276:17830-17835(2001).
[13]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 163-494, AND VARIANT
TYR-392.
PubMed=3856261; DOI=10.1073/pnas.82.4.983;
Phillips I.R., Shephard E.A., Ashworth A., Rabin B.R.;
"Isolation and sequence of a human cytochrome P-450 cDNA clone.";
Proc. Natl. Acad. Sci. U.S.A. 82:983-987(1985).
[14]
CATALYTIC ACTIVITY, FUNCTION AS 1,4-CINEOLE 2-EXO-MONOOXYGENASE, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11695850; DOI=10.1080/00498250110065595;
Miyazawa M., Shindo M., Shimada T.;
"Roles of cytochrome P450 3A enzymes in the 2-hydroxylation of 1,4-
cineole, a monoterpene cyclic ether, by rat and human liver
microsomes.";
Xenobiotica 31:713-723(2001).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-494 IN COMPLEX WITH
COUMARIN; HEME AND THE INHIBITOR METHOXSALEN, FUNCTION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16086027; DOI=10.1038/nsmb971;
Yano J.K., Hsu M.H., Griffin K.J., Stout C.D., Johnson E.F.;
"Structures of human microsomal cytochrome P450 2A6 complexed with
coumarin and methoxsalen.";
Nat. Struct. Mol. Biol. 12:822-823(2005).
[17]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 29-494 IN COMPLEX WITH
PHENACETIN AND HEME, AND FUNCTION.
PubMed=17125252; DOI=10.1021/jm060519r;
Yano J.K., Denton T.T., Cerny M.A., Zhang X., Johnson E.F.,
Cashman J.R.;
"Synthetic inhibitors of cytochrome P-450 2A6: inhibitory activity,
difference spectra, mechanism of inhibition, and protein
cocrystallization.";
J. Med. Chem. 49:6987-7001(2006).
[18]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 29-494 IN COMPLEX WITH
PHENACETIN AND HEME, FUNCTION, CHARACTERIZATION OF VARIANTS LEU-110
AND MET-365, AND MUTAGENESIS OF ILE-208; SER-213; ILE-300; GLY-301;
SER-369 AND ARG-372.
PubMed=18779312; DOI=10.1124/dmd.108.023770;
DeVore N.M., Smith B.D., Urban M.J., Scott E.E.;
"Key residues controlling phenacetin metabolism by human cytochrome
P450 2A enzymes.";
Drug Metab. Dispos. 36:2582-2590(2008).
[19]
CHARACTERIZATION OF VARIANT CYP2A6*2 HIS-160.
PubMed=9409631; DOI=10.1016/S0278-6915(97)00066-5;
Hadidi H., Zahlsen K., Idle J.R., Cholerton S.;
"A single amino acid substitution (Leu160His) in cytochrome P450
CYP2A6 causes switching from 7-hydroxylation to 3-hydroxylation of
coumarin.";
Food Chem. Toxicol. 35:903-907(1997).
[20]
VARIANT CYP2A6*5 VAL-479.
PubMed=10544257; DOI=10.1016/S0014-5793(99)01364-2;
Oscarson M., McLellan R.A., Gullsten H., Agundez J.A., Benitez J.,
Rautio A., Raunio H., Pelkonen O., Ingelman-Sundberg M.;
"Identification and characterisation of novel polymorphisms in the
CYP2A locus: implications for nicotine metabolism.";
FEBS Lett. 460:321-327(1999).
[21]
VARIANTS CYP2A6*7 THR-471 AND CYP2A6*8 LEU-485.
PubMed=11237731; DOI=10.1006/bbrc.2001.4422;
Ariyoshi N., Sawamura Y., Kamataki T.;
"A novel single nucleotide polymorphism altering stability and
activity of CYP2a6.";
Biochem. Biophys. Res. Commun. 281:810-814(2001).
[22]
VARIANTS CYP2A6*13 ARG-5; CYP2A6*14 ASN-29; CYP2A6*15 GLU-194 AND
CYP2A6*16 SER-203.
PubMed=15618701; DOI=10.2133/dmpk.17.482;
Kiyotani K., Fujieda M., Yamazaki H., Shimada T., Guengerich F.P.,
Parkinson A., Nakagawa K., Ishizaki T., Kamataki T.;
"Twenty one novel single nucleotide polymorphisms (SNPs) of the CYP2A6
gene in Japanese and Caucasians.";
Drug Metab. Pharmacokinet. 17:482-487(2002).
[23]
VARIANTS ASP-419 AND THR-471.
PubMed=12721789; DOI=10.1007/s10038-003-0021-7;
Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C.,
Nakamura Y.;
"Catalog of 680 variations among eight cytochrome p450 (CYP) genes,
nine esterase genes, and two other genes in the Japanese population.";
J. Hum. Genet. 48:249-270(2003).
[24]
VARIANTS ARG-5; ASN-29; LEU-118; GLN-128; PRO-224; MET-365; ASP-418;
ASP-419; THR-471; ARG-476 AND LEU-485.
PubMed=15469410; DOI=10.1517/14622416.5.7.895;
Solus J.F., Arietta B.J., Harris J.R., Sexton D.P., Steward J.Q.,
McMunn C., Ihrie P., Mehall J.M., Edwards T.L., Dawson E.P.;
"Genetic variation in eleven phase I drug metabolism genes in an
ethnically diverse population.";
Pharmacogenomics 5:895-931(2004).
[25]
VARIANTS LEU-110; LEU-118; LEU-128; ALA-131; ASP-418; ASP-419 AND
TYR-438.
PubMed=18360915; DOI=10.1002/humu.20698;
Mwenifumbo J.C., Al Koudsi N., Ho M.K., Zhou Q., Hoffmann E.B.,
Sellers E.M., Tyndale R.F.;
"Novel and established CYP2A6 alleles impair in vivo nicotine
metabolism in a population of Black African descent.";
Hum. Mutat. 29:679-688(2008).
[26]
VARIANTS CYS-203; SER-203 AND MET-365, AND CHARACTERIZATION OF VARIANT
CYS-203.
PubMed=18216723; DOI=10.1097/FPC.0b013e3282f3606e;
Ho M.K., Mwenifumbo J.C., Zhao B., Gillam E.M., Tyndale R.F.;
"A novel CYP2A6 allele, CYP2A6*23, impairs enzyme function in vitro
and in vivo and decreases smoking in a population of Black-African
descent.";
Pharmacogenet. Genomics 18:67-75(2008).
-!- FUNCTION: Exhibits a high coumarin 7-hydroxylase activity. Can act
in the hydroxylation of the anti-cancer drugs cyclophosphamide and
ifosphamide. Competent in the metabolic activation of aflatoxin
B1. Constitutes the major nicotine C-oxidase. Acts as a 1,4-
cineole 2-exo-monooxygenase. Possesses low phenacetin O-
deethylation activity. {ECO:0000269|PubMed:11695850,
ECO:0000269|PubMed:16086027, ECO:0000269|PubMed:17125252,
ECO:0000269|PubMed:18779312, ECO:0000269|PubMed:1889415,
ECO:0000269|PubMed:1944238}.
-!- CATALYTIC ACTIVITY: 1,4-cineole + NADPH + O(2) = 2-exo-hydroxy-
1,4-cineole + NADP(+) + H(2)O. {ECO:0000269|PubMed:11695850}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.23 uM for coumarin {ECO:0000269|PubMed:11695850,
ECO:0000269|PubMed:16086027};
KM=530 uM for 1,4-cineole {ECO:0000269|PubMed:11695850,
ECO:0000269|PubMed:16086027};
Vmax=3.5 nmol/min/nmol enzyme toward 2-exo-hydroxy-1,4-cineole
{ECO:0000269|PubMed:11695850, ECO:0000269|PubMed:16086027};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane; Peripheral membrane protein.
-!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:1889415,
ECO:0000269|PubMed:1944238}.
-!- INDUCTION: By phenobarbital and dexamethasone.
{ECO:0000269|PubMed:1889415, ECO:0000269|PubMed:1944238}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA52147.1; Type=Miscellaneous discrepancy; Note=Numerous conflicts and frameshifts.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Cytochrome P450 Allele Nomenclature Committee;
Note=CYP2A6 alleles;
URL="http://www.cypalleles.ki.se/cyp2a6.htm";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cyp2a6/";
-!- WEB RESOURCE: Name=Wikipedia; Note=CYP2A6 entry;
URL="https://en.wikipedia.org/wiki/CYP2A6";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CYP2A6ID40240ch19q13.html";
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EMBL; X13897; CAA32097.1; -; mRNA.
EMBL; X13929; CAA32117.1; -; mRNA.
EMBL; X13930; CAA32118.1; -; mRNA.
EMBL; M33318; AAA52067.1; -; mRNA.
EMBL; AF182275; AAF13600.1; -; mRNA.
EMBL; AK312964; BAG35803.1; -; mRNA.
EMBL; EU135979; ABV02584.1; -; Genomic_DNA.
EMBL; FJ440681; ACK44068.1; -; Genomic_DNA.
EMBL; AC008537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471126; EAW57012.1; -; Genomic_DNA.
EMBL; BC096253; AAH96253.3; -; mRNA.
EMBL; BC096254; AAH96254.1; -; mRNA.
EMBL; BC096255; AAH96255.1; -; mRNA.
EMBL; BC096256; AAH96256.1; -; mRNA.
EMBL; AF326721; AAG45229.1; -; Genomic_DNA.
EMBL; K03192; AAA52147.1; ALT_SEQ; mRNA.
CCDS; CCDS12568.1; -.
PIR; A00190; O4HUPB.
PIR; S04698; O4HUA6.
RefSeq; NP_000753.3; NM_000762.5.
UniGene; Hs.250615; -.
PDB; 1Z10; X-ray; 1.90 A; A/B/C/D=29-494.
PDB; 1Z11; X-ray; 2.05 A; A/B/C/D=29-494.
PDB; 2FDU; X-ray; 1.85 A; A/B/C/D=29-494.
PDB; 2FDV; X-ray; 1.65 A; A/B/C/D=29-494.
PDB; 2FDW; X-ray; 2.05 A; A/B/C/D=29-494.
PDB; 2FDY; X-ray; 1.95 A; A/B/C/D=29-494.
PDB; 3EBS; X-ray; 2.15 A; A/B/C/D=29-494.
PDB; 3T3Q; X-ray; 2.10 A; A/B/C/D=29-494.
PDB; 3T3R; X-ray; 2.40 A; A/B/C/D=29-494.
PDB; 4EJJ; X-ray; 2.30 A; A/B/C/D=29-494.
PDB; 4RUI; X-ray; 2.61 A; A/B/C/D/E/F=29-494.
PDBsum; 1Z10; -.
PDBsum; 1Z11; -.
PDBsum; 2FDU; -.
PDBsum; 2FDV; -.
PDBsum; 2FDW; -.
PDBsum; 2FDY; -.
PDBsum; 3EBS; -.
PDBsum; 3T3Q; -.
PDBsum; 3T3R; -.
PDBsum; 4EJJ; -.
PDBsum; 4RUI; -.
ProteinModelPortal; P11509; -.
SMR; P11509; -.
BioGrid; 107927; 4.
STRING; 9606.ENSP00000301141; -.
BindingDB; P11509; -.
ChEMBL; CHEMBL5282; -.
DrugBank; DB07621; (5-(PYRIDIN-3-YL)FURAN-2-YL)METHANAMINE.
DrugBank; DB04665; 2H-1-BENZOPYRAN-2-ONE.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB01118; Amiodarone.
DrugBank; DB00381; Amlodipine.
DrugBank; DB01351; Amobarbital.
DrugBank; DB00182; Amphetamine.
DrugBank; DB01435; Antipyrine.
DrugBank; DB01274; Arformoterol.
DrugBank; DB00972; Azelastine.
DrugBank; DB00207; Azithromycin.
DrugBank; DB00921; Buprenorphine.
DrugBank; DB01156; Bupropion.
DrugBank; DB00356; Chlorzoxazone.
DrugBank; DB00568; Cinnarizine.
DrugBank; DB00604; Cisapride.
DrugBank; DB00636; Clofibrate.
DrugBank; DB00882; Clomifene.
DrugBank; DB00257; Clotrimazole.
DrugBank; DB00363; Clozapine.
DrugBank; DB00531; Cyclophosphamide.
DrugBank; DB06292; Dapagliflozin.
DrugBank; DB01151; Desipramine.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB01191; Dexfenfluramine.
DrugBank; DB00255; Diethylstilbestrol.
DrugBank; DB00470; Dronabinol.
DrugBank; DB00216; Eletriptan.
DrugBank; DB04953; Ezogabine.
DrugBank; DB04841; Flunarizine.
DrugBank; DB01544; Flunitrazepam.
DrugBank; DB00544; Fluorouracil.
DrugBank; DB00690; Flurazepam.
DrugBank; DB01213; Fomepizole.
DrugBank; DB00983; Formoterol.
DrugBank; DB01159; Halothane.
DrugBank; DB01181; Ifosfamide.
DrugBank; DB00951; Isoniazid.
DrugBank; DB01026; Ketoconazole.
DrugBank; DB01006; Letrozole.
DrugBank; DB00281; Lidocaine.
DrugBank; DB04871; Lorcaserin.
DrugBank; DB01043; Memantine.
DrugBank; DB00170; Menadione.
DrugBank; DB00763; Methimazole.
DrugBank; DB00553; Methoxsalen.
DrugBank; DB01028; Methoxyflurane.
DrugBank; DB01011; Metyrapone.
DrugBank; DB01110; Miconazole.
DrugBank; DB00471; Montelukast.
DrugBank; DB07617; N-METHYL(5-(PYRIDIN-3-YL)FURAN-2-YL)METHANAMINE.
DrugBank; DB00238; Nevirapine.
DrugBank; DB00184; Nicotine.
DrugBank; DB01115; Nifedipine.
DrugBank; DB06712; Nilvadipine.
DrugBank; DB01059; Norfloxacin.
DrugBank; DB00312; Pentobarbital.
DrugBank; DB03783; Phenacetin.
DrugBank; DB01174; Phenobarbital.
DrugBank; DB01085; Pilocarpine.
DrugBank; DB04977; Plitidepsin.
DrugBank; DB00860; Prednisolone.
DrugBank; DB00396; Progesterone.
DrugBank; DB00818; Propofol.
DrugBank; DB01045; Rifampicin.
DrugBank; DB00412; Rosiglitazone.
DrugBank; DB01037; Selegiline.
DrugBank; DB01236; Sevoflurane.
DrugBank; DB06729; Sulfaphenazole.
DrugBank; DB00675; Tamoxifen.
DrugBank; DB00752; Tranylcypromine.
DrugBank; DB00755; Tretinoin.
DrugBank; DB01361; Troleandomycin.
DrugBank; DB00313; Valproic Acid.
DrugBank; DB09068; Vortioxetine.
DrugBank; DB00495; Zidovudine.
GuidetoPHARMACOLOGY; 1321; -.
iPTMnet; P11509; -.
PhosphoSitePlus; P11509; -.
BioMuta; CYP2A6; -.
DMDM; 308153612; -.
PaxDb; P11509; -.
PeptideAtlas; P11509; -.
PRIDE; P11509; -.
DNASU; 1548; -.
Ensembl; ENST00000301141; ENSP00000301141; ENSG00000255974.
GeneID; 1548; -.
KEGG; hsa:1548; -.
UCSC; uc002opl.4; human.
CTD; 1548; -.
DisGeNET; 1548; -.
EuPathDB; HostDB:ENSG00000255974.6; -.
GeneCards; CYP2A6; -.
HGNC; HGNC:2610; CYP2A6.
HPA; HPA046713; -.
HPA; HPA047262; -.
MalaCards; CYP2A6; -.
MIM; 122720; gene+phenotype.
neXtProt; NX_P11509; -.
PharmGKB; PA121; -.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
HOVERGEN; HBG015789; -.
InParanoid; P11509; -.
KO; K17683; -.
PhylomeDB; P11509; -.
TreeFam; TF352043; -.
BioCyc; MetaCyc:HS10343-MONOMER; -.
BRENDA; 1.14.14.1; 2681.
Reactome; R-HSA-211981; Xenobiotics.
Reactome; R-HSA-211999; CYP2E1 reactions.
SABIO-RK; P11509; -.
EvolutionaryTrace; P11509; -.
GeneWiki; CYP2A6; -.
GenomeRNAi; 1548; -.
PRO; PR:P11509; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000255974; -.
ExpressionAtlas; P11509; baseline and differential.
Genevisible; P11509; HS.
GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
GO; GO:0008389; F:coumarin 7-hydroxylase activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
GO; GO:0046226; P:coumarin catabolic process; IDA:BHF-UCL.
GO; GO:0009804; P:coumarin metabolic process; IDA:BHF-UCL.
GO; GO:0017144; P:drug metabolic process; IDA:BHF-UCL.
GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
GO; GO:0042738; P:exogenous drug catabolic process; IDA:BHF-UCL.
GO; GO:0008202; P:steroid metabolic process; IMP:BHF-UCL.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR008067; Cyt_P450_E_grp-I_CYP2A-like.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR01684; EP450ICYP2A.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum; Heme; Iron;
Membrane; Metal-binding; Microsome; Monooxygenase; NADP;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 494 Cytochrome P450 2A6.
/FTId=PRO_0000051668.
METAL 439 439 Iron (heme axial ligand).
BINDING 107 107 Substrate. {ECO:0000305}.
BINDING 297 297 Substrate.
MOD_RES 131 131 Phosphoserine.
{ECO:0000250|UniProtKB:P00176}.
MOD_RES 379 379 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q64458}.
VARIANT 5 5 G -> R (in allele CYP2A6*13;
dbSNP:rs28399434).
{ECO:0000269|PubMed:15469410,
ECO:0000269|PubMed:15618701}.
/FTId=VAR_018330.
VARIANT 29 29 S -> N (in allele CYP2A6*14;
dbSNP:rs28399435).
{ECO:0000269|PubMed:15469410,
ECO:0000269|PubMed:15618701,
ECO:0000269|PubMed:2726448}.
/FTId=VAR_018331.
VARIANT 110 110 V -> L (in allele CYP2A6*24; increases
phenacetin O-deethylation activity 4
fold; dbSNP:rs72549435).
{ECO:0000269|PubMed:18360915,
ECO:0000269|PubMed:18779312}.
/FTId=VAR_055035.
VARIANT 118 118 F -> L (in allele CYP2A6*25 and allele
CYP2A6*26; dbSNP:rs28399440).
{ECO:0000269|PubMed:15469410,
ECO:0000269|PubMed:18360915}.
/FTId=VAR_024711.
VARIANT 128 128 R -> L (in allele CYP2A6*26).
{ECO:0000269|PubMed:18360915}.
/FTId=VAR_055036.
VARIANT 128 128 R -> Q (in allele CYP2A6*6; loss of
activity; dbSNP:rs4986891).
{ECO:0000269|PubMed:11278503,
ECO:0000269|PubMed:15469410}.
/FTId=VAR_011577.
VARIANT 131 131 S -> A (in allele CYP2A6*26;
dbSNP:rs59552350).
{ECO:0000269|PubMed:18360915}.
/FTId=VAR_055037.
VARIANT 160 160 L -> H (in allele CYP2A6*2; unable to
catalyze 7-hydroxylation of coumarin;
causes switching from coumarin 7-
hydroxylation to 3-hydroxylation;
dbSNP:rs1801272).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2322567,
ECO:0000269|PubMed:2748347,
ECO:0000269|PubMed:9409631,
ECO:0000269|Ref.6}.
/FTId=VAR_001249.
VARIANT 194 194 K -> E (in allele CYP2A6*15).
{ECO:0000269|PubMed:15618701}.
/FTId=VAR_018332.
VARIANT 203 203 R -> C (in allele CYP2A6*23; greatly
reduced activity toward nicotine C-
oxidation as well as reduced coumarin 7-
hydroxylation; dbSNP:rs56256500).
{ECO:0000269|PubMed:18216723,
ECO:0000269|Ref.6}.
/FTId=VAR_055034.
VARIANT 203 203 R -> S (in allele CYP2A6*16;
dbSNP:rs56256500).
{ECO:0000269|PubMed:15618701,
ECO:0000269|PubMed:18216723}.
/FTId=VAR_018333.
VARIANT 224 224 S -> P (in dbSNP:rs28399447).
{ECO:0000269|PubMed:15469410}.
/FTId=VAR_024712.
VARIANT 292 292 V -> M (in dbSNP:rs2644906).
/FTId=VAR_059149.
VARIANT 294 294 T -> S (in dbSNP:rs4997557).
/FTId=VAR_048448.
VARIANT 365 365 V -> M (in allele CYP2A6*17; increases
phenacetin O-deethylation activity 2
fold; dbSNP:rs28399454).
{ECO:0000269|PubMed:15469410,
ECO:0000269|PubMed:18216723,
ECO:0000269|PubMed:18779312,
ECO:0000269|Ref.6}.
/FTId=VAR_024713.
VARIANT 392 392 F -> Y (in dbSNP:rs1809810).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2322567,
ECO:0000269|PubMed:2726448,
ECO:0000269|PubMed:2748347,
ECO:0000269|PubMed:3856261,
ECO:0000269|Ref.4, ECO:0000269|Ref.6,
ECO:0000269|Ref.8}.
/FTId=VAR_055033.
VARIANT 418 418 N -> D (in allele CYP2A6*28;
dbSNP:rs28399463).
{ECO:0000269|PubMed:15469410,
ECO:0000269|PubMed:18360915,
ECO:0000269|Ref.6}.
/FTId=VAR_024714.
VARIANT 419 419 E -> D (in allele CYP2A6*28;
dbSNP:rs8192730).
{ECO:0000269|PubMed:12721789,
ECO:0000269|PubMed:15469410,
ECO:0000269|PubMed:18360915,
ECO:0000269|Ref.6}.
/FTId=VAR_018375.
VARIANT 438 438 N -> Y (in allele CYP2A6*24).
{ECO:0000269|PubMed:18360915}.
/FTId=VAR_055038.
VARIANT 471 471 I -> T (in allele CYP2A6*7;
dbSNP:rs5031016).
{ECO:0000269|PubMed:11237731,
ECO:0000269|PubMed:12721789,
ECO:0000269|PubMed:15469410}.
/FTId=VAR_011578.
VARIANT 476 476 K -> R (in dbSNP:rs6413474).
{ECO:0000269|PubMed:15469410,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_024715.
VARIANT 479 479 G -> V (in allele CYP2A6*5; loss of
activity; dbSNP:rs5031017).
{ECO:0000269|PubMed:10544257}.
/FTId=VAR_008356.
VARIANT 485 485 R -> L (in allele CYP2A6*8;
dbSNP:rs28399468).
{ECO:0000269|PubMed:11237731,
ECO:0000269|PubMed:15469410}.
/FTId=VAR_011579.
MUTAGEN 208 208 I->S: Increases phenacetin O-deethylation
activity 10 fold; when associated with F-
300 and A-301. Increases phenacetin O-
deethylation activity 38 fold; when
associated with F-300; A-301 and G-369.
{ECO:0000269|PubMed:18779312}.
MUTAGEN 213 213 S->A: No effect on phenacetin O-
deethylation activity.
{ECO:0000269|PubMed:18779312}.
MUTAGEN 300 300 I->F: Increases phenacetin O-deethylation
activity 3 fold. Increases phenacetin O-
deethylation activity 8 fold; when
associated with A-301. Increases
phenacetin O-deethylation activity 10
fold; when associated with S-208 and A-
301. Increases phenacetin O-deethylation
activity 12 fold; when associated with A-
301 and G-369. Increases phenacetin O-
deethylation activity 38 fold; when
associated with S-208; A-301 and G-369.
{ECO:0000269|PubMed:18779312}.
MUTAGEN 301 301 G->A: Slightly decreases phenacetin O-
deethylation activity. Increases
phenacetin O-deethylation activity 8
fold; when associated with F-300.
Increases phenacetin O-deethylation
activity 10 fold; when associated with S-
208 and F-300. Increases phenacetin O-
deethylation activity 12 fold; when
associated with F-300 and G-369.
Increases phenacetin O-deethylation
activity 38 fold; when associated with S-
208; F-300 and G-369.
{ECO:0000269|PubMed:18779312}.
MUTAGEN 369 369 S->G: Increases phenacetin O-deethylation
activity 3 fold. Increases phenacetin O-
deethylation activity 38 fold; when
associated with S-208; F-300 and A-301.
{ECO:0000269|PubMed:18779312}.
MUTAGEN 372 372 R->H: Increases phenacetin O-deethylation
activity 2 fold.
{ECO:0000269|PubMed:18779312}.
CONFLICT 3 7 Missing (in Ref. 1; CAA32097).
{ECO:0000305}.
CONFLICT 255 255 N -> K (in Ref. 1; CAA32097).
{ECO:0000305}.
CONFLICT 326 326 K -> Q (in Ref. 1; CAA32097).
{ECO:0000305}.
TURN 41 43 {ECO:0000244|PDB:2FDV}.
HELIX 46 48 {ECO:0000244|PDB:2FDV}.
HELIX 51 53 {ECO:0000244|PDB:2FDU}.
HELIX 54 65 {ECO:0000244|PDB:2FDV}.
STRAND 67 73 {ECO:0000244|PDB:2FDV}.
STRAND 76 81 {ECO:0000244|PDB:2FDV}.
HELIX 84 91 {ECO:0000244|PDB:2FDV}.
TURN 92 98 {ECO:0000244|PDB:2FDV}.
HELIX 105 111 {ECO:0000244|PDB:2FDV}.
STRAND 115 118 {ECO:0000244|PDB:2FDV}.
HELIX 121 137 {ECO:0000244|PDB:2FDV}.
TURN 138 141 {ECO:0000244|PDB:2FDV}.
HELIX 143 162 {ECO:0000244|PDB:2FDV}.
TURN 163 165 {ECO:0000244|PDB:2FDV}.
HELIX 171 187 {ECO:0000244|PDB:2FDV}.
HELIX 196 212 {ECO:0000244|PDB:2FDV}.
HELIX 215 227 {ECO:0000244|PDB:2FDV}.
STRAND 230 232 {ECO:0000244|PDB:2FDY}.
HELIX 233 256 {ECO:0000244|PDB:2FDV}.
HELIX 267 277 {ECO:0000244|PDB:2FDV}.
TURN 278 280 {ECO:0000244|PDB:2FDV}.
HELIX 288 319 {ECO:0000244|PDB:2FDV}.
HELIX 321 334 {ECO:0000244|PDB:2FDV}.
STRAND 337 339 {ECO:0000244|PDB:2FDV}.
HELIX 343 348 {ECO:0000244|PDB:2FDV}.
HELIX 350 363 {ECO:0000244|PDB:2FDV}.
STRAND 378 380 {ECO:0000244|PDB:2FDV}.
STRAND 383 385 {ECO:0000244|PDB:2FDV}.
STRAND 390 393 {ECO:0000244|PDB:2FDV}.
HELIX 395 399 {ECO:0000244|PDB:2FDV}.
TURN 402 404 {ECO:0000244|PDB:2FDV}.
STRAND 405 407 {ECO:0000244|PDB:4RUI}.
HELIX 413 416 {ECO:0000244|PDB:2FDV}.
STRAND 419 421 {ECO:0000244|PDB:3T3Q}.
HELIX 442 459 {ECO:0000244|PDB:2FDV}.
STRAND 460 466 {ECO:0000244|PDB:2FDV}.
HELIX 468 470 {ECO:0000244|PDB:2FDV}.
STRAND 476 483 {ECO:0000244|PDB:2FDV}.
STRAND 489 493 {ECO:0000244|PDB:2FDV}.
SEQUENCE 494 AA; 56501 MW; 8C05CBF0EFC698AF CRC64;
MLASGMLLVA LLVCLTVMVL MSVWQQRKSK GKLPPGPTPL PFIGNYLQLN TEQMYNSLMK
ISERYGPVFT IHLGPRRVVV LCGHDAVREA LVDQAEEFSG RGEQATFDWV FKGYGVVFSN
GERAKQLRRF SIATLRDFGV GKRGIEERIQ EEAGFLIDAL RGTGGANIDP TFFLSRTVSN
VISSIVFGDR FDYKDKEFLS LLRMMLGIFQ FTSTSTGQLY EMFSSVMKHL PGPQQQAFQL
LQGLEDFIAK KVEHNQRTLD PNSPRDFIDS FLIRMQEEEK NPNTEFYLKN LVMTTLNLFI
GGTETVSTTL RYGFLLLMKH PEVEAKVHEE IDRVIGKNRQ PKFEDRAKMP YMEAVIHEIQ
RFGDVIPMSL ARRVKKDTKF RDFFLPKGTE VFPMLGSVLR DPSFFSNPQD FNPQHFLNEK
GQFKKSDAFV PFSIGKRNCF GEGLARMELF LFFTTVMQNF RLKSSQSPKD IDVSPKHVGF
ATIPRNYTMS FLPR


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