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

Bifunctional cytochrome P450/NADPH--P450 reductase 2 (CYP102A3) (Fatty acid hydroxylase CypB) (Flavocytochrome P450 102A3) [Includes: Cytochrome P450 102A3 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)]

 CYPB_BACSU              Reviewed;        1054 AA.
O08336;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
22-NOV-2017, entry version 140.
RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase 2 {ECO:0000305};
AltName: Full=CYP102A3 {ECO:0000303|PubMed:15122913};
AltName: Full=Fatty acid hydroxylase CypB {ECO:0000305};
AltName: Full=Flavocytochrome P450 102A3 {ECO:0000305};
Includes:
RecName: Full=Cytochrome P450 102A3 {ECO:0000305};
EC=1.14.14.1 {ECO:0000269|PubMed:14741768, ECO:0000269|PubMed:15122913};
Includes:
RecName: Full=NADPH--cytochrome P450 reductase;
EC=1.6.2.4 {ECO:0000269|PubMed:14741768, ECO:0000269|PubMed:15122913};
Name=cypB {ECO:0000312|EMBL:CAB14658.1};
Synonyms=cyp102A3 {ECO:0000303|PubMed:11574077,
ECO:0000303|PubMed:15122913}, yrhJ {ECO:0000303|PubMed:11574077,
ECO:0000303|PubMed:15122913}; OrderedLocusNames=BSU27160;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9308178; DOI=10.1099/00221287-143-9-2939;
Sorokin A., Bolotin A., Purnelle B., Hilbert H., Lauber J.,
Duesterhoeft A., Ehrlich S.D.;
"Sequence of the Bacillus subtilis genome region in the vicinity of
the lev operon reveals two new extracytoplasmic function RNA
polymerase sigma factors SigV and SigZ.";
Microbiology 143:2939-2943(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
INDUCTION.
PubMed=11574077; DOI=10.1093/oxfordjournals.jbchem.a003020;
Lee T.-R., Hsu H.-P., Shaw G.-C.;
"Transcriptional regulation of the Bacillus subtilis bscR-CYP102A3
operon by the BscR repressor and differential induction of cytochrome
CYP102A3 expression by oleic acid and palmitate.";
J. Biochem. 130:569-574(2001).
[4]
INDUCTION.
STRAIN=168 / 1A1;
PubMed=11734890; DOI=10.1007/s002030100350;
Gustafsson M.C., Palmer C.N., Wolf C.R., von Wachenfeldt C.;
"Fatty-acid-displaced transcriptional repressor, a conserved regulator
of cytochrome P450 102 transcription in Bacillus species.";
Arch. Microbiol. 176:459-464(2001).
[5]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=168 / 1A1;
PubMed=15122913; DOI=10.1021/bi035904m;
Gustafsson M.C., Roitel O., Marshall K.R., Noble M.A., Chapman S.K.,
Pessegueiro A., Fulco A.J., Cheesman M.R., von Wachenfeldt C.,
Munro A.W.;
"Expression, purification, and characterization of Bacillus subtilis
cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of
P450 BM3 from Bacillus megaterium.";
Biochemistry 43:5474-5487(2004).
[6]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND MUTAGENESIS
OF PHE-89 AND SER-190.
STRAIN=168 / ATCC 33234 / DSM 402 / NCIMB 10106;
PubMed=14741768; DOI=10.1016/j.jbiotec.2003.11.001;
Lentz O., Urlacher V., Schmid R.D.;
"Substrate specificity of native and mutated cytochrome P450
(CYP102A3) from Bacillus subtilis.";
J. Biotechnol. 108:41-49(2004).
[7]
PROTEIN ENGINEERING.
STRAIN=168 / ATCC 33234 / DSM 402 / NCIMB 10106;
PubMed=16381045; DOI=10.1002/cbic.200500266;
Lentz O., Feenstra A., Habicher T., Hauer B., Schmid R.D.,
Urlacher V.B.;
"Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus
subtilis by using a new versatile assay system.";
ChemBioChem 7:345-350(2006).
[8]
INDUCTION.
STRAIN=168 / 1604;
PubMed=17434969; DOI=10.1128/JB.00130-07;
Jervis A.J., Thackray P.D., Houston C.W., Horsburgh M.J., Moir A.;
"SigM-responsive genes of Bacillus subtilis and their promoters.";
J. Bacteriol. 189:4534-4538(2007).
-!- FUNCTION: Functions as a fatty acid monooxygenase. Catalyzes
hydroxylation of a range of medium to long-chain fatty acids, with
a preference for long-chain unsaturated and branched-chain fatty
acids over saturated fatty acids. Hydroxylation of myristic acid
occurs mainly at the omega-2 and omega-3 positions, in
approximately equal proportions. Also displays a NADPH-dependent
reductase activity in the C-terminal domain, which allows electron
transfer from NADPH to the heme iron of the cytochrome P450 N-
terminal domain. {ECO:0000269|PubMed:14741768,
ECO:0000269|PubMed:15122913}.
-!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000269|PubMed:14741768, ECO:0000269|PubMed:15122913}.
-!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
reduced hemoprotein. {ECO:0000269|PubMed:14741768,
ECO:0000269|PubMed:15122913}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:15122913};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000269|PubMed:15122913};
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:15122913};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=165 uM for lauric acid {ECO:0000269|PubMed:15122913};
KM=542 uM for myristic acid {ECO:0000269|PubMed:15122913};
KM=337 uM for palmitic acid {ECO:0000269|PubMed:15122913};
KM=68.5 uM for stearic acid {ECO:0000269|PubMed:15122913};
KM=28.7 uM for phytanic acid {ECO:0000269|PubMed:15122913};
KM=68.3 uM for 15-methylpalmitic acid
{ECO:0000269|PubMed:15122913};
KM=79 uM for arachidonic acid {ECO:0000269|PubMed:15122913};
KM=5.1 uM for NADPH {ECO:0000269|PubMed:15122913};
KM=2.43 mM for NADH {ECO:0000269|PubMed:15122913};
KM=10.9 uM for cytochrome c (in the reductase assay)
{ECO:0000269|PubMed:15122913};
KM=285 uM for ferricyanide (in the reductase assay)
{ECO:0000269|PubMed:15122913};
Note=kcat is 104 min(-1) for lauric acid hydroxylation. kcat is
5556 min(-1) for myristic acid hydroxylation. kcat is 676 min(-
1) for palmitic acid hydroxylation. kcat is 374 min(-1) for
stearic acid hydroxylation. kcat is 794 min(-1) for phytanic
acid hydroxylation. kcat is 3845 min(-1) for 15-methylpalmitic
acid hydroxylation. kcat is 1690 min(-1) for arachidonic acid
hydroxylation. kcat is 3520 min(-1) for the reduction of
cytochrome c. kcat is 37050 min(-1) for the reduction of
ferricyanide. {ECO:0000269|PubMed:15122913};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- INDUCTION: Negatively regulated by the transcriptional repressor
FatR (PubMed:11574077, PubMed:11734890). Is induced by fatty acids
such as oleate, linoleate and phytanate, that bind and displace
the FatR repressor (PubMed:11734890). Is also induced by
palmitate, likely via another mechanism (PubMed:11574077).
Transcribed under partial control of SigM ECF sigma factor
(PubMed:17434969). {ECO:0000269|PubMed:11574077,
ECO:0000269|PubMed:11734890, ECO:0000269|PubMed:17434969}.
-!- SIMILARITY: In the N-terminal section; belongs to the cytochrome
P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U93874; AAB80867.1; -; Genomic_DNA.
EMBL; AL009126; CAB14658.1; -; Genomic_DNA.
PIR; A69975; A69975.
RefSeq; NP_390594.1; NC_000964.3.
RefSeq; WP_003246174.1; NZ_JNCM01000036.1.
ProteinModelPortal; O08336; -.
SMR; O08336; -.
STRING; 224308.Bsubs1_010100014841; -.
PaxDb; O08336; -.
EnsemblBacteria; CAB14658; CAB14658; BSU27160.
GeneID; 937585; -.
KEGG; bsu:BSU27160; -.
PATRIC; fig|224308.179.peg.2949; -.
eggNOG; ENOG4107EER; Bacteria.
eggNOG; COG0369; LUCA.
HOGENOM; HOG000093545; -.
InParanoid; O08336; -.
KO; K14338; -.
OMA; EDYPACE; -.
PhylomeDB; O08336; -.
BioCyc; BSUB:BSU27160-MONOMER; -.
SABIO-RK; O08336; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
GO; GO:0019395; P:fatty acid oxidation; IDA:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
Gene3D; 3.40.50.360; -; 1.
InterPro; IPR023206; Bifunctional_P450_P450_red.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR036396; Cyt_P450_sf.
InterPro; IPR003097; FAD-binding_1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
Pfam; PF00067; p450; 1.
PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SUPFAM; SSF48264; SSF48264; 1.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Electron transport; FAD; Flavoprotein;
FMN; Heme; Iron; Metal-binding; Monooxygenase; Multifunctional enzyme;
NADP; Oxidoreductase; Reference proteome; Transport.
CHAIN 1 1054 Bifunctional cytochrome P450/NADPH--P450
reductase 2.
/FTId=PRO_0000052207.
DOMAIN 486 625 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 663 896 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 492 497 FMN. {ECO:0000250|UniProtKB:P14779}.
NP_BIND 539 542 FMN. {ECO:0000250|UniProtKB:P14779}.
NP_BIND 573 575 FMN. {ECO:0000250|UniProtKB:P14779}.
NP_BIND 581 583 FMN. {ECO:0000250|UniProtKB:P14779}.
REGION 1 475 Cytochrome P450.
{ECO:0000305|PubMed:15122913}.
REGION 22 31 Fatty acid binding.
{ECO:0000250|UniProtKB:P14779}.
REGION 77 89 Fatty acid binding.
{ECO:0000250|UniProtKB:P14779}.
REGION 331 333 Fatty acid binding.
{ECO:0000250|UniProtKB:P14779}.
REGION 476 1053 NADPH--P450 reductase.
{ECO:0000305|PubMed:15122913}.
METAL 403 403 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P14779}.
BINDING 183 183 Fatty acid.
{ECO:0000250|UniProtKB:P14779}.
BINDING 266 266 Fatty acid.
{ECO:0000250|UniProtKB:P14779}.
BINDING 440 440 Fatty acid.
{ECO:0000250|UniProtKB:P14779}.
SITE 271 271 Important for catalytic activity.
{ECO:0000250|UniProtKB:P14779}.
MUTAGEN 89 89 F->V: Hydroxylates shorter substrates
with higher conversion rates than wild-
type, and in contrast to wild-type, is
also able to convert medium-chain alkanes
and aromatic compounds; when associated
with Q-190.
{ECO:0000269|PubMed:14741768}.
MUTAGEN 190 190 S->Q: Hydroxylates shorter substrates
with higher conversion rates than wild-
type, and in contrast to wild-type, is
also able to convert medium-chain alkanes
and aromatic compounds; when associated
with V-89. {ECO:0000269|PubMed:14741768}.
SEQUENCE 1054 AA; 118676 MW; 705F8E27866CA110 CRC64;
MKQASAIPQP KTYGPLKNLP HLEKEQLSQS LWRIADELGP IFRFDFPGVS SVFVSGHNLV
AEVCDEKRFD KNLGKGLQKV REFGGDGLFT SWTHEPNWQK AHRILLPSFS QKAMKGYHSM
MLDIATQLIQ KWSRLNPNEE IDVADDMTRL TLDTIGLCGF NYRFNSFYRD SQHPFITSML
RALKEAMNQS KRLGLQDKMM VKTKLQFQKD IEVMNSLVDR MIAERKANPD ENIKDLLSLM
LYAKDPVTGE TLDDENIRYQ IITFLIAGHE TTSGLLSFAI YCLLTHPEKL KKAQEEADRV
LTDDTPEYKQ IQQLKYIRMV LNETLRLYPT APAFSLYAKE DTVLGGEYPI SKGQPVTVLI
PKLHRDQNAW GPDAEDFRPE RFEDPSSIPH HAYKPFGNGQ RACIGMQFAL QEATMVLGLV
LKHFELINHT GYELKIKEAL TIKPDDFKIT VKPRKTAAIN VQRKEQADIK AETKPKETKP
KHGTPLLVLF GSNLGTAEGI AGELAAQGRQ MGFTAETAPL DDYIGKLPEE GAVVIVTASY
NGAPPDNAAG FVEWLKELEE GQLKGVSYAV FGCGNRSWAS TYQRIPRLID DMMKAKGASR
LTAIGEGDAA DDFESHRESW ENRFWKETMD AFDINEIAQK EDRPSLSITF LSEATETPVA
KAYGAFEGIV LENRELQTAA STRSTRHIEL EIPAGKTYKE GDHIGILPKN SRELVQRVLS
RFGLQSNHVI KVSGSAHMAH LPMDRPIKVV DLLSSYVELQ EPASRLQLRE LASYTVCPPH
QKELEQLVSD DGIYKEQVLA KRLTMLDFLE DYPACEMPFE RFLALLPSLK PRYYSISSSP
KVHANIVSMT VGVVKASAWS GRGEYRGVAS NYLAELNTGD AAACFIRTPQ SGFQMPNDPE
TPMIMVGPGT GIAPFRGFIQ ARSVLKKEGS TLGEALLYFG CRRPDHDDLY REELDQAEQD
GLVTIRRCYS RVENEPKGYV QHLLKQDTQK LMTLIEKGAH IYVCGDGSQM APDVERTLRL
AYEAEKAASQ EESAVWLQKL QDQRRYVKDV WTGM


Related products :

Catalog number Product name Quantity
EIAAB08920 CYP2C8,CYPIIC8,Cytochrome P450 2C8,Cytochrome P450 form 1,Cytochrome P450 IIC2,Cytochrome P450 MP-12,Cytochrome P450 MP-20,Homo sapiens,Human,S-mephenytoin 4-hydroxylase
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
E1557h ELISA kit 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
E1557h ELISA 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
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
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
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
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
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
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
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
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
E1557r ELISA kit 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T
E1557p ELISA kit 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 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
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
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
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
U1557b CLIA 21-OHase,Bos taurus,Bovine,CYP21,CYP21A1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Steroid 21-hydroxylase 96T
E1557p ELISA 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
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


 

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