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

NADP nitrous oxide-forming nitric oxide reductase (NOR) (EC 1.7.1.14) (CYPLVA1) (Cytochrome P450 55A1) (Cytochrome P450 DNIR) (Cytochrome P450nor) (Fungal nitric oxide reductase)

 NOR_FUSOX               Reviewed;         403 AA.
P23295;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 111.
RecName: Full=NADP nitrous oxide-forming nitric oxide reductase;
Short=NOR;
EC=1.7.1.14;
AltName: Full=CYPLVA1;
AltName: Full=Cytochrome P450 55A1;
AltName: Full=Cytochrome P450 DNIR;
AltName: Full=Cytochrome P450nor;
AltName: Full=Fungal nitric oxide reductase;
Name=CYP55A1; Synonyms=CYP55;
Fusarium oxysporum (Fusarium vascular wilt).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
Fusarium; Fusarium oxysporum species complex.
NCBI_TaxID=5507;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND INDUCTION.
STRAIN=MT-811;
PubMed=2037602;
Kizawa H., Tomura D., Oda M., Fukamizu A., Hoshino T., Gotoh O.,
Yasui T., Shoun H.;
"Nucleotide sequence of the unique nitrate/nitrite-inducible
cytochrome P-450 cDNA from Fusarium oxysporum.";
J. Biol. Chem. 266:10632-10637(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MT-811;
PubMed=7798191;
Tomura D., Obika K., Fukamizu A., Shoun H.;
"Nitric oxide reductase cytochrome P-450 gene, CYP 55, of the fungus
Fusarium oxysporum containing a potential binding-site for FNR, the
transcription factor involved in the regulation of anaerobic growth of
Escherichia coli.";
J. Biochem. 116:88-94(1994).
[3]
PROTEIN SEQUENCE OF 2-11, AND ACETYLATION AT ALA-2.
PubMed=9010754; DOI=10.1093/oxfordjournals.jbchem.a021525;
Nakahara K., Shoun H.;
"N-terminal processing and amino acid sequence of two isoforms of
nitric oxide reductase cytochrome P450nor from Fusarium oxysporum.";
J. Biochem. 120:1082-1087(1996).
[4]
CATALYTIC ACTIVITY, ENZYME REGULATION, AND FUNCTION.
PubMed=2040619;
Shoun H., Tanimoto T.;
"Denitrification by the fungus Fusarium oxysporum and involvement of
cytochrome P-450 in the respiratory nitrite reduction.";
J. Biol. Chem. 266:11078-11082(1991).
[5]
CATALYTIC ACTIVITY.
PubMed=7829493; DOI=10.1074/jbc.270.4.1617;
Shiro Y., Fujii M., Iizuka T., Adachi S., Tsukamoto K., Nakahara K.,
Shoun H.;
"Spectroscopic and kinetic studies on reaction of cytochrome P450nor
with nitric oxide. Implication for its nitric oxide reduction
mechanism.";
J. Biol. Chem. 270:1617-1623(1995).
[6]
FUNCTION, AND MUTAGENESIS OF ARG-64; SER-73; SER-75; GLY-76; LYS-77;
GLN-78 AND ARG-174.
PubMed=12105197; DOI=10.1074/jbc.M203923200;
Zhang L., Kudo T., Takaya N., Shoun H.;
"The B' helix determines cytochrome P450nor specificity for the
electron donors NADH and NADPH.";
J. Biol. Chem. 277:33842-33847(2002).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=9334748; DOI=10.1038/nsb1097-827;
Park S.-Y., Shimizu H., Adachi S., Nakagawa A., Tanaka I.,
Nakahara K., Shoun H., Obayashi E., Nakamura H., Iizuka T., Shiro Y.;
"Crystal structure of nitric oxide reductase from denitrifying fungus
Fusarium oxysporum.";
Nat. Struct. Biol. 4:827-832(1997).
[8]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-403 IN COMPLEX WITH HEME,
CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-286 AND ASP-393.
PubMed=10671516; DOI=10.1074/jbc.275.7.4816;
Shimizu H., Obayashi E., Gomi Y., Arakawa H., Park S.-Y., Nakamura H.,
Adachi S., Shoun H., Shiro Y.;
"Proton delivery in NO reduction by fungal nitric-oxide reductase.
Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO
complexes of wild-type and mutant enzymes.";
J. Biol. Chem. 275:4816-4826(2000).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-402 IN COMPLEX WITH HEME OF
WILD TYPE; MUTANT VAL-286 AND MUTANT THR-286, AND MUTAGENESIS OF
SER-286.
PubMed=11051564; DOI=10.1016/S0162-0134(00)00103-3;
Shimizu H., Park S., Lee D., Shoun H., Shiro Y.;
"Crystal structures of cytochrome P450nor and its mutants
(Ser286-->Val, Thr) in the ferric resting state at cryogenic
temperature: a comparative analysis with monooxygenase cytochrome
P450s.";
J. Inorg. Biochem. 81:191-205(2000).
[10]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-402 IN COMPLEX WITH HEME.
PubMed=11132616; DOI=10.1016/S0162-0134(00)00161-6;
Obayashi E., Shimizu H., Park S.Y., Shoun H., Shiro Y.;
"Mutation effects of a conserved threonine (Thr243) of cytochrome
P450nor on its structure and function.";
J. Inorg. Biochem. 82:103-111(2000).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH HEME.
PubMed=11076941; DOI=10.1074/jbc.M007244200;
Kudo T., Takaya N., Park S.Y., Shiro Y., Shoun H.;
"A positively charged cluster formed in the heme-distal pocket of
cytochrome P450nor is essential for interaction with NADH.";
J. Biol. Chem. 276:5020-5026(2001).
[12]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH HEME.
PubMed=11258878; DOI=10.1021/bi002225s;
Lee D.-S., Park S.-Y., Yamane K., Obayashi E., Hori H., Shiro Y.;
"Structural characterization of n-butyl-isocyanide complexes of
cytochromes P450nor and P450cam.";
Biochemistry 40:2669-2677(2001).
[13]
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH HEME.
PubMed=11752781;
Shimizu H., Park S.-Y., Shiro Y., Adachi S.;
"X-ray structure of nitric oxide reductase (cytochrome P450nor) at
atomic resolution.";
Acta Crystallogr. D 58:81-89(2002).
[14]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH HEME, AND
CATALYTIC ACTIVITY.
PubMed=15313618; DOI=10.1016/j.jmb.2004.07.009;
Oshima R., Fushinobu S., Su F., Zhang L., Takaya N., Shoun H.;
"Structural evidence for direct hydride transfer from NADH to
cytochrome P450nor.";
J. Mol. Biol. 342:207-217(2004).
-!- FUNCTION: Nitric oxide reductase which is involved in a
dissimilatory reduction of nitrite. Acts as a nitric oxide
reductase. Is able to reduce nitrate and nitrite to a gaseous form
of N(2)O when oxygen supply is limited or discontinued. May
function as a detoxification mechanism.
{ECO:0000269|PubMed:12105197, ECO:0000269|PubMed:2040619}.
-!- CATALYTIC ACTIVITY: Nitrous oxide + NAD(P)(+) + H(2)O = 2 nitric
oxide + NAD(P)H. {ECO:0000269|PubMed:10671516,
ECO:0000269|PubMed:15313618, ECO:0000269|PubMed:2040619,
ECO:0000269|PubMed:7829493}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- ENZYME REGULATION: Cyanide, CO, and oxygen strongly inhibit
catalytic activity. {ECO:0000269|PubMed:2040619}.
-!- INDUCTION: By nitrate/nitrite. {ECO:0000269|PubMed:2037602}.
-!- SIMILARITY: 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; M63340; AAA33337.1; -; mRNA.
EMBL; D14517; BAA03390.1; -; Genomic_DNA.
PIR; JC5150; JC5150.
PIR; JC5151; JC5151.
PDB; 1CL6; X-ray; 1.70 A; A=2-403.
PDB; 1CMJ; X-ray; 1.70 A; A=2-403.
PDB; 1CMN; X-ray; 1.70 A; A=2-403.
PDB; 1EHE; X-ray; 1.70 A; A=2-403.
PDB; 1EHF; X-ray; 1.70 A; A=2-403.
PDB; 1EHG; X-ray; 1.70 A; A=2-403.
PDB; 1F24; X-ray; 1.40 A; A=2-403.
PDB; 1F25; X-ray; 1.40 A; A=2-403.
PDB; 1F26; X-ray; 1.40 A; A=2-403.
PDB; 1GED; X-ray; 2.00 A; A=1-403.
PDB; 1GEI; X-ray; 1.60 A; A=1-403.
PDB; 1GEJ; X-ray; 1.50 A; A=1-403.
PDB; 1JFB; X-ray; 1.00 A; A=1-403.
PDB; 1JFC; X-ray; 1.05 A; A=1-403.
PDB; 1ROM; X-ray; 2.00 A; A=1-403.
PDB; 1ULW; X-ray; 2.00 A; A=2-403.
PDB; 1XQD; X-ray; 1.80 A; A=1-403.
PDB; 2ROM; X-ray; 2.00 A; A=1-403.
PDBsum; 1CL6; -.
PDBsum; 1CMJ; -.
PDBsum; 1CMN; -.
PDBsum; 1EHE; -.
PDBsum; 1EHF; -.
PDBsum; 1EHG; -.
PDBsum; 1F24; -.
PDBsum; 1F25; -.
PDBsum; 1F26; -.
PDBsum; 1GED; -.
PDBsum; 1GEI; -.
PDBsum; 1GEJ; -.
PDBsum; 1JFB; -.
PDBsum; 1JFC; -.
PDBsum; 1ROM; -.
PDBsum; 1ULW; -.
PDBsum; 1XQD; -.
PDBsum; 2ROM; -.
ProteinModelPortal; P23295; -.
SMR; P23295; -.
iPTMnet; P23295; -.
KEGG; ag:AAA33337; -.
KO; K15877; -.
BioCyc; MetaCyc:MONOMER-16203; -.
BRENDA; 1.7.1.14; 2351.
BRENDA; 1.7.2.5; 2351.
SABIO-RK; P23295; -.
EvolutionaryTrace; P23295; -.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR002397; Cyt_P450_B.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 2.
PRINTS; PR00359; BP450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
Metal-binding; Monooxygenase; NAD; NADP; Oxidoreductase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9010754}.
CHAIN 2 403 NADP nitrous oxide-forming nitric oxide
reductase.
/FTId=PRO_0000052039.
METAL 352 352 Iron (heme axial ligand).
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:9010754}.
MUTAGEN 64 64 R->E: Impairs interaction with NADH.
{ECO:0000269|PubMed:12105197}.
MUTAGEN 73 73 S->A: Decreases the NADPH-dependent
activity. {ECO:0000269|PubMed:12105197}.
MUTAGEN 75 75 S->A: Decreases the NADPH-dependent
activity. {ECO:0000269|PubMed:12105197}.
MUTAGEN 75 75 S->G: Improves the NADPH-dependent
activity. {ECO:0000269|PubMed:12105197}.
MUTAGEN 76 76 G->A: Decreases the NADPH-dependent
activity. {ECO:0000269|PubMed:12105197}.
MUTAGEN 77 77 K->A: Decreases the NADPH-dependent
activity. {ECO:0000269|PubMed:12105197}.
MUTAGEN 78 78 Q->A: Decreases the NADPH-dependent
activity. {ECO:0000269|PubMed:12105197}.
MUTAGEN 174 174 R->E: Impairs interaction with NADH.
{ECO:0000269|PubMed:12105197}.
MUTAGEN 286 286 S->V,T: Impairs catalytic activity.
{ECO:0000269|PubMed:10671516,
ECO:0000269|PubMed:11051564}.
MUTAGEN 393 393 D->V,L: Impairs catalytic activity.
{ECO:0000269|PubMed:10671516}.
STRAND 7 9 {ECO:0000244|PDB:1JFB}.
STRAND 13 17 {ECO:0000244|PDB:1GED}.
HELIX 21 28 {ECO:0000244|PDB:1JFB}.
STRAND 30 35 {ECO:0000244|PDB:1JFB}.
STRAND 41 45 {ECO:0000244|PDB:1JFB}.
HELIX 48 56 {ECO:0000244|PDB:1JFB}.
STRAND 64 66 {ECO:0000244|PDB:2ROM}.
HELIX 74 79 {ECO:0000244|PDB:1JFB}.
HELIX 86 88 {ECO:0000244|PDB:1JFB}.
HELIX 93 98 {ECO:0000244|PDB:1JFB}.
TURN 99 101 {ECO:0000244|PDB:1JFB}.
HELIX 102 105 {ECO:0000244|PDB:1JFB}.
HELIX 107 131 {ECO:0000244|PDB:1JFB}.
STRAND 134 136 {ECO:0000244|PDB:1ULW}.
HELIX 140 143 {ECO:0000244|PDB:1JFB}.
TURN 144 146 {ECO:0000244|PDB:1JFB}.
HELIX 147 157 {ECO:0000244|PDB:1JFB}.
HELIX 161 163 {ECO:0000244|PDB:1JFB}.
HELIX 164 175 {ECO:0000244|PDB:1JFB}.
STRAND 177 179 {ECO:0000244|PDB:1CL6}.
HELIX 181 204 {ECO:0000244|PDB:1JFB}.
HELIX 210 217 {ECO:0000244|PDB:1JFB}.
TURN 218 222 {ECO:0000244|PDB:1JFB}.
HELIX 226 257 {ECO:0000244|PDB:1JFB}.
HELIX 259 267 {ECO:0000244|PDB:1JFB}.
HELIX 269 271 {ECO:0000244|PDB:1JFB}.
HELIX 272 282 {ECO:0000244|PDB:1JFB}.
STRAND 291 296 {ECO:0000244|PDB:1JFB}.
STRAND 298 300 {ECO:0000244|PDB:1JFB}.
STRAND 303 305 {ECO:0000244|PDB:1JFB}.
STRAND 310 313 {ECO:0000244|PDB:1JFB}.
HELIX 315 318 {ECO:0000244|PDB:1JFB}.
TURN 322 324 {ECO:0000244|PDB:1JFB}.
STRAND 325 327 {ECO:0000244|PDB:1JFB}.
HELIX 348 350 {ECO:0000244|PDB:1JFB}.
HELIX 355 372 {ECO:0000244|PDB:1JFB}.
STRAND 377 380 {ECO:0000244|PDB:1JFB}.
HELIX 382 384 {ECO:0000244|PDB:1JFB}.
STRAND 396 398 {ECO:0000244|PDB:1JFB}.
STRAND 400 402 {ECO:0000244|PDB:1JFB}.
SEQUENCE 403 AA; 44372 MW; 7FDD97D8E0FB9215 CRC64;
MASGAPSFPF SRASGPEPPA EFAKLRATNP VSQVKLFDGS LAWLVTKHKD VCFVATSEKL
SKVRTRQGFP ELSASGKQAA KAKPTFVDMD PPEHMHQRSM VEPTFTPEAV KNLQPYIQRT
VDDLLEQMKQ KGCANGPVDL VKEFALPVPS YIIYTLLGVP FNDLEYLTQQ NAIRTNGSST
AREASAANQE LLDYLAILVE QRLVEPKDDI ISKLCTEQVK PGNIDKSDAV QIAFLLLVAG
NATMVNMIAL GVATLAQHPD QLAQLKANPS LAPQFVEELC RYHTASALAI KRTAKEDVMI
GDKLVRANEG IIASNQSANR DEEVFENPDE FNMNRKWPPQ DPLGFGFGDH RCIAEHLAKA
ELTTVFSTLY QKFPDLKVAV PLGKINYTPL NRDVGIVDLP VIF


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
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
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
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
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
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
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
EIAAB08904 CYP2B4,CYPIIB4,Cytochrome P450 2B4,Cytochrome P450 isozyme 2,Cytochrome P450 LM2,Cytochrome P450 type B0,Cytochrome P450 type B1,Oryctolagus cuniculus,Rabbit
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
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
EIAAB08843 CYP1A1,CYPIA1,Cytochrome P450 1A1,Cytochrome P450 form 6,Cytochrome P450-C,Cytochrome P450-P1,Homo sapiens,Human
EIAAB08847 CYP1A2,CYPIA2,Cytochrome P450 1A2,Cytochrome P450 isozyme 4,Cytochrome P450 LM4,Cytochrome P450-PM4,Oryctolagus cuniculus,Rabbit
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
EIAAB08924 Cyp2c13,Cyp2c-13,CYPIIC13,Cytochrome P450 2C13, male-specific,Cytochrome P-450g,Cytochrome P450-G,Cytochrome P450-UT-5,Rat,Rattus norvegicus
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
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
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
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


 

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