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Cytochrome P450 26B1 (EC 1.14.13.-) (Cytochrome P450 26A2) (Cytochrome P450 retinoic acid-inactivating 2) (Cytochrome P450RAI-2) (Retinoic acid-metabolizing cytochrome)

 CP26B_HUMAN             Reviewed;         512 AA.
Q9NR63; B2R8M7; B7Z2K6; B7Z2P4; B7Z3B8; E4W5W7; Q32MC0; Q53TW1;
Q9NP41;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
07-NOV-2018, entry version 157.
RecName: Full=Cytochrome P450 26B1;
EC=1.14.13.- {ECO:0000269|PubMed:10823918, ECO:0000269|PubMed:26937021};
AltName: Full=Cytochrome P450 26A2;
AltName: Full=Cytochrome P450 retinoic acid-inactivating 2;
Short=Cytochrome P450RAI-2;
AltName: Full=Retinoic acid-metabolizing cytochrome;
Name=CYP26B1; Synonyms=CYP26A2, P450RAI2;
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), FUNCTION, CATALYTIC ACTIVITY,
TISSUE SPECIFICITY, AND INDUCTION.
TISSUE=Retina;
PubMed=10823918; DOI=10.1073/pnas.120161397;
White J.A., Ramshaw H., Taimi M., Stangle W., Zhang A., Everingham S.,
Creighton S., Tam S.-P., Jones G., Petkovich M.;
"Identification of the human cytochrome P450, P450RAI-2, which is
predominantly expressed in the adult cerebellum and is responsible for
all-trans-retinoic acid metabolism.";
Proc. Natl. Acad. Sci. U.S.A. 97:6403-6408(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT SER-264.
TISSUE=Vascular smooth muscle;
Savenstrand H., Kumawat A., Karlsson M., Eriksson L.A., Sirsjo A.,
Strid A.;
"A spliced version of the human cytochrome P450 26B1 has an
alternative function in retinoic acid metabolism.";
Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
VARIANT SER-264.
TISSUE=Brain, Cerebellum, and Hippocampus;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-181; VAL-185;
HIS-191; ASN-227; SER-264; LYS-380; GLY-420; CYS-473 AND ILE-479.
SeattleSNPs variation discovery resource;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
FUNCTION, AND VARIANTS RHFCA PRO-146 AND LEU-363.
PubMed=22019272; DOI=10.1016/j.ajhg.2011.09.015;
Laue K., Pogoda H.M., Daniel P.B., van Haeringen A., Alanay Y.,
von Ameln S., Rachwalski M., Morgan T., Gray M.J., Breuning M.H.,
Sawyer G.M., Sutherland-Smith A.J., Nikkels P.G., Kubisch C.,
Bloch W., Wollnik B., Hammerschmidt M., Robertson S.P.;
"Craniosynostosis and multiple skeletal anomalies in humans and
zebrafish result from a defect in the localized degradation of
retinoic acid.";
Am. J. Hum. Genet. 89:595-606(2011).
[8]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
VARIANT ARG-64.
PubMed=26937021; DOI=10.1124/jpet.116.232637;
Foti R.S., Isoherranen N., Zelter A., Dickmann L.J., Buttrick B.R.,
Diaz P., Douguet D.;
"Identification of tazarotenic acid as the first xenobiotic substrate
of human retinoic acid hydroxylase CYP26A1 and CYP26B1.";
J. Pharmacol. Exp. Ther. 357:281-292(2016).
-!- FUNCTION: Involved in the metabolism of retinoic acid (RA),
rendering this classical morphogen inactive through oxidation.
Involved in the specific inactivation of all-trans-retinoic acid
(all-trans-RA), with a preference for the following substrates:
all-trans-RA > 9-cis-RA > 13-cis-RA. Generates several
hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH-
RA. Essential for postnatal survival. Plays a central role in germ
cell development: acts by degrading RA in the developing testis,
preventing STRA8 expression, thereby leading to delay of meiosis.
Required for the maintenance of the undifferentiated state of male
germ cells during embryonic development in Sertoli cells, inducing
arrest in G0 phase of the cell cycle and preventing meiotic entry.
Plays a role in skeletal development, both at the level of
patterning and in the ossification of bone and the establishment
of some synovial joints. {ECO:0000269|PubMed:10823918,
ECO:0000269|PubMed:22019272}.
-!- FUNCTION: Has also a significant activity in oxidation of
tazarotenic acid and may therefore metabolize that xenobiotic in
vivo. {ECO:0000269|PubMed:26937021}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.01 uM for tazarotenic acid (measured in vitro by the
production of tazarotenic acid-sulfoxide)
{ECO:0000269|PubMed:26937021};
KM=0.56 uM for tazarotenic acid (measured in vitro by the
production of hydroxytazarotenic acid production)
{ECO:0000269|PubMed:26937021};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Microsome membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9NR63-1; Sequence=Displayed;
Name=2;
IsoId=Q9NR63-2; Sequence=VSP_042968;
Name=3;
IsoId=Q9NR63-3; Sequence=VSP_042967;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in brain, particularly in the
cerebellum and pons. {ECO:0000269|PubMed:10823918}.
-!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:10823918}.
-!- DISEASE: Radiohumeral fusions with other skeletal and craniofacial
anomalies (RHFCA) [MIM:614416]: A disease characterized by
craniofacial malformations, occipital encephalocele, radiohumeral
fusions, oligodactyly, advanced osseous maturation, and calvarial
mineralization defects. {ECO:0000269|PubMed:22019272}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAH12154.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/cyp26b1/";
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EMBL; AF252297; AAF76003.1; -; mRNA.
EMBL; FJ467289; ACR19332.1; -; mRNA.
EMBL; AK294814; BAH11892.1; -; mRNA.
EMBL; AK294933; BAH11930.1; -; mRNA.
EMBL; AK295683; BAH12154.1; ALT_INIT; mRNA.
EMBL; AK313433; BAG36224.1; -; mRNA.
EMBL; AC007002; AAY14690.1; -; Genomic_DNA.
EMBL; BC069443; AAH69443.1; -; mRNA.
EMBL; BC109205; AAI09206.1; -; mRNA.
CCDS; CCDS1919.1; -. [Q9NR63-1]
CCDS; CCDS62934.1; -. [Q9NR63-2]
RefSeq; NP_001264671.1; NM_001277742.1. [Q9NR63-2]
RefSeq; NP_063938.1; NM_019885.3. [Q9NR63-1]
UniGene; Hs.91546; -.
ProteinModelPortal; Q9NR63; -.
SMR; Q9NR63; -.
BioGrid; 121153; 8.
STRING; 9606.ENSP00000001146; -.
BindingDB; Q9NR63; -.
ChEMBL; CHEMBL3713687; -.
SwissLipids; SLP:000001876; -.
iPTMnet; Q9NR63; -.
PhosphoSitePlus; Q9NR63; -.
DMDM; 20137526; -.
MaxQB; Q9NR63; -.
PaxDb; Q9NR63; -.
PeptideAtlas; Q9NR63; -.
PRIDE; Q9NR63; -.
ProteomicsDB; 82286; -.
ProteomicsDB; 82287; -. [Q9NR63-2]
ProteomicsDB; 82288; -. [Q9NR63-3]
Ensembl; ENST00000001146; ENSP00000001146; ENSG00000003137. [Q9NR63-1]
Ensembl; ENST00000546307; ENSP00000443304; ENSG00000003137. [Q9NR63-2]
GeneID; 56603; -.
KEGG; hsa:56603; -.
UCSC; uc002sih.3; human. [Q9NR63-1]
CTD; 56603; -.
DisGeNET; 56603; -.
EuPathDB; HostDB:ENSG00000003137.8; -.
GeneCards; CYP26B1; -.
HGNC; HGNC:20581; CYP26B1.
HPA; HPA012567; -.
MalaCards; CYP26B1; -.
MIM; 605207; gene.
MIM; 614416; phenotype.
neXtProt; NX_Q9NR63; -.
OpenTargets; ENSG00000003137; -.
Orphanet; 293925; Lethal occipital encephalocele-skeletal dysplasia syndrome.
PharmGKB; PA134879191; -.
eggNOG; KOG0157; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00800000124060; -.
HOGENOM; HOG000220829; -.
HOVERGEN; HBG051099; -.
InParanoid; Q9NR63; -.
KO; K12664; -.
OMA; KEGRFHY; -.
OrthoDB; EOG091G0K6Z; -.
PhylomeDB; Q9NR63; -.
TreeFam; TF105093; -.
Reactome; R-HSA-211916; Vitamins.
Reactome; R-HSA-5365859; RA biosynthesis pathway.
Reactome; R-HSA-5579015; Defective CYP26B1 causes Radiohumeral fusions with other skeletal and craniofacial anomalies (RHFCA).
SABIO-RK; Q9NR63; -.
ChiTaRS; CYP26B1; human.
GeneWiki; CYP26B1; -.
GenomeRNAi; 56603; -.
PRO; PR:Q9NR63; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000003137; Expressed in 183 organ(s), highest expression level in cerebellar vermis.
CleanEx; HS_CYP26B1; -.
ExpressionAtlas; Q9NR63; baseline and differential.
Genevisible; Q9NR63; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; NAS:BHF-UCL.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; IDA:BHF-UCL.
GO; GO:0001972; F:retinoic acid binding; IDA:BHF-UCL.
GO; GO:0060349; P:bone morphogenesis; IMP:UniProtKB.
GO; GO:0001709; P:cell fate determination; ISS:BHF-UCL.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0070268; P:cornification; IEA:Ensembl.
GO; GO:0030326; P:embryonic limb morphogenesis; ISS:BHF-UCL.
GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl.
GO; GO:0001768; P:establishment of T cell polarity; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0007140; P:male meiotic nuclear division; ISS:BHF-UCL.
GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; TAS:BHF-UCL.
GO; GO:0055114; P:oxidation-reduction process; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:2001037; P:positive regulation of tongue muscle cell differentiation; IEA:Ensembl.
GO; GO:0009954; P:proximal/distal pattern formation; ISS:BHF-UCL.
GO; GO:0045580; P:regulation of T cell differentiation; IEA:Ensembl.
GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
GO; GO:0034653; P:retinoic acid catabolic process; IDA:BHF-UCL.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; ISS:BHF-UCL.
GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
GO; GO:0043587; P:tongue morphogenesis; IEA:Ensembl.
GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome.
GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002403; Cyt_P450_E_grp-IV.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00465; EP450IV.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Craniosynostosis;
Disease mutation; Endoplasmic reticulum; Heme; Iron; Membrane;
Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Polymorphism;
Reference proteome.
CHAIN 1 512 Cytochrome P450 26B1.
/FTId=PRO_0000051985.
METAL 441 441 Iron (heme axial ligand). {ECO:0000255}.
VAR_SEQ 1 67 MLFEGLDLVSALATLAACLVSVTLLLAVSQQLWQLRWAATR
DKSCKLPIPKGSMGFPLIGETGHWLL -> MKNKTCVLVCV
SVFGGERGQVTVPRVGVRRPSLAGPLQKCTLRETRVWLP
(in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042967.
VAR_SEQ 69 143 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_042968.
VARIANT 64 64 H -> R. {ECO:0000269|PubMed:26937021}.
/FTId=VAR_075982.
VARIANT 146 146 S -> P (in RHFCA; dbSNP:rs281875232).
{ECO:0000269|PubMed:22019272}.
/FTId=VAR_067923.
VARIANT 181 181 V -> M (in dbSNP:rs142999899).
{ECO:0000269|Ref.4}.
/FTId=VAR_038722.
VARIANT 185 185 A -> V (in dbSNP:rs765423228).
{ECO:0000269|Ref.4}.
/FTId=VAR_038723.
VARIANT 191 191 R -> H (in dbSNP:rs76025186).
{ECO:0000269|Ref.4}.
/FTId=VAR_038724.
VARIANT 227 227 D -> N (in dbSNP:rs143738797).
{ECO:0000269|Ref.4}.
/FTId=VAR_038725.
VARIANT 264 264 L -> S (in dbSNP:rs2241057).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.2, ECO:0000269|Ref.4}.
/FTId=VAR_024383.
VARIANT 363 363 R -> L (in RHFCA; dbSNP:rs281875231).
{ECO:0000269|PubMed:22019272}.
/FTId=VAR_067924.
VARIANT 380 380 E -> K (in dbSNP:rs2286965).
{ECO:0000269|Ref.4}.
/FTId=VAR_038726.
VARIANT 420 420 A -> G (in dbSNP:rs7568553).
{ECO:0000269|Ref.4}.
/FTId=VAR_038727.
VARIANT 473 473 R -> C (in dbSNP:rs61751056).
{ECO:0000269|Ref.4}.
/FTId=VAR_038728.
VARIANT 479 479 V -> I (in dbSNP:rs148075682).
{ECO:0000269|Ref.4}.
/FTId=VAR_038729.
CONFLICT 265 265 D -> G (in Ref. 3; BAH11930).
{ECO:0000305}.
SEQUENCE 512 AA; 57513 MW; A06D1D9944E6726F CRC64;
MLFEGLDLVS ALATLAACLV SVTLLLAVSQ QLWQLRWAAT RDKSCKLPIP KGSMGFPLIG
ETGHWLLQGS GFQSSRREKY GNVFKTHLLG RPLIRVTGAE NVRKILMGEH HLVSTEWPRS
TRMLLGPNTV SNSIGDIHRN KRKVFSKIFS HEALESYLPK IQLVIQDTLR AWSSHPEAIN
VYQEAQKLTF RMAIRVLLGF SIPEEDLGHL FEVYQQFVDN VFSLPVDLPF SGYRRGIQAR
QILQKGLEKA IREKLQCTQG KDYLDALDLL IESSKEHGKE MTMQELKDGT LELIFAAYAT
TASASTSLIM QLLKHPTVLE KLRDELRAHG ILHSGGCPCE GTLRLDTLSG LRYLDCVIKE
VMRLFTPISG GYRTVLQTFE LDGFQIPKGW SVMYSIRDTH DTAPVFKDVN VFDPDRFSQA
RSEDKDGRFH YLPFGGGVRT CLGKHLAKLF LKVLAVELAS TSRFELATRT FPRITLVPVL
HPVDGLSVKF FGLDSNQNEI LPETEAMLSA TV


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U1557h CLIA 21-OHase,CYP21,CYP21A2,CYP21B,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Cytochrome P450-C21B,Homo sapiens,Human,Steroid 21-hydroxylase 96T
EIAAB08901 Cyp2b1,Cyp2b-1,CYPIIB1,Cytochrome P450 2B1,Cytochrome P450b,Cytochrome P450-B,Cytochrome P450-LM2,Cytochrome P450-PB1,Cytochrome P450-PB2,Rat,Rattus norvegicus
EIAAB08923 Cyp2c12,Cyp2c-12,Cyp2c40,CYPIIC12,Cytochrome P450 15-beta,Cytochrome P450 2C12, female-specific,Cytochrome P450I,Cytochrome P450-UT-1,Cytochrome P450-UT-I,Rat,Rattus norvegicus
EIAAB08974 Albendazole monooxygenase,Albendazole sulfoxidase,CYP3A3,CYP3A4,CYPIIIA3,CYPIIIA4,Cytochrome P450 3A3,Cytochrome P450 3A4,Cytochrome P450 HLp,Cytochrome P450 NF-25,Cytochrome P450-PCN1,Homo sapiens,Hu
U0988Rb CLIA 4-nitrophenol 2-hydroxylase,CYP2E,CYP2E1,CYPIIE1,Cytochrome P450 2E1,Cytochrome P450 isozyme 3A,Cytochrome P450 LM3A,Cytochrome P450-ALC,Oryctolagus cuniculus,Rabbit 96T
E0988Rb ELISA 4-nitrophenol 2-hydroxylase,CYP2E,CYP2E1,CYPIIE1,Cytochrome P450 2E1,Cytochrome P450 isozyme 3A,Cytochrome P450 LM3A,Cytochrome P450-ALC,Oryctolagus cuniculus,Rabbit 96T
E0988Rb ELISA kit 4-nitrophenol 2-hydroxylase,CYP2E,CYP2E1,CYPIIE1,Cytochrome P450 2E1,Cytochrome P450 isozyme 3A,Cytochrome P450 LM3A,Cytochrome P450-ALC,Oryctolagus cuniculus,Rabbit 96T
EIAAB08934 Cyp2d1,Cyp2d-1,Cyp2d9,CYPIID1,Cytochrome P450 2D1,Cytochrome P450-CMF1A,Cytochrome P450-DB1,Cytochrome P450-UT-7,Debrisoquine 4-hydroxylase,Rat,Rattus norvegicus
EIAAB08989 Cyp4a11,Cyp4a2,Cyp4a-2,CYPIVA2,Cytochrome P450 4A2,Cytochrome P-450 K-2,Cytochrome P450 K-5,Cytochrome P450-LA-omega 2,Lauric acid omega-hydroxylase,Rat,Rattus norvegicus
EIAAB08904 CYP2B4,CYPIIB4,Cytochrome P450 2B4,Cytochrome P450 isozyme 2,Cytochrome P450 LM2,Cytochrome P450 type B0,Cytochrome P450 type B1,Oryctolagus cuniculus,Rabbit
E1557m ELISA 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
E1557m ELISA kit 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
U1557m CLIA 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
EIAAB08908 Cyp2b10,Cyp2b-10,Cyp2b20,CYPIIB10,CYPIIB20,Cytochrome P450 2B10,Cytochrome P450 2B20,Cytochrome P450 clone PF3_46,Cytochrome P450-16-alpha,Mouse,Mus musculus,P24,Testosterone 16-alpha hydroxylase
E1557r ELISA 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T
U1557r CLIA 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T
E1557b ELISA 21-OHase,Bos taurus,Bovine,CYP21,CYP21A1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Steroid 21-hydroxylase 96T
E1557b ELISA kit 21-OHase,Bos taurus,Bovine,CYP21,CYP21A1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Steroid 21-hydroxylase 96T
U1557p CLIA 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T


 

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