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

Bacterioferritin (BFR) (EC 1.16.3.1) (Cytochrome b-1) (Cytochrome b-557)

 BFR_ECOLI               Reviewed;         158 AA.
P0ABD3; O68931; P11056; Q2M701;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 1.
31-JAN-2018, entry version 100.
RecName: Full=Bacterioferritin;
Short=BFR;
EC=1.16.3.1;
AltName: Full=Cytochrome b-1;
AltName: Full=Cytochrome b-557;
Name=bfr; OrderedLocusNames=b3336, JW3298;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=2661540; DOI=10.1128/jb.171.7.3940-3947.1989;
Andrews S.C., Harrison P.M., Guest J.R.;
"Cloning, sequencing, and mapping of the bacterioferritin gene (bfr)
of Escherichia coli K-12.";
J. Bacteriol. 171:3940-3947(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ECOR 30;
Noorani S.M., Lindahl L., Zengel J.M.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 1-87.
STRAIN=K12;
PubMed=2644932; DOI=10.1016/S0006-291X(89)80075-0;
Andrews S.C., Smith J.M.A., Guest J.R., Harrison P.M.;
"Amino acid sequence of the bacterioferritin (cytochrome b1) of
Escherichia coli-K12.";
Biochem. Biophys. Res. Commun. 158:489-496(1989).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-158.
STRAIN=K12;
PubMed=7959070; DOI=10.1016/0378-1119(94)90851-6;
Whitchurch C.B., Mattick J.S.;
"Escherichia coli contains a set of genes homologous to those involved
in protein secretion, DNA uptake and the assembly of type-4 fimbriae
in other bacteria.";
Gene 150:9-15(1994).
[7]
HEME-BINDING, MASS SPECTROMETRY, AND MUTAGENESIS OF MET-31; MET-52 AND
MET-86.
STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
PubMed=7559480; DOI=10.1074/jbc.270.40.23268;
Andrews S.C., Le Brun N.E., Barynin V., Thomson A.J., Moore G.R.,
Guest J.R., Harrison P.M.;
"Site-directed replacement of the coaxial heme ligands of
bacterioferritin generates heme-free variants.";
J. Biol. Chem. 270:23268-23274(1995).
[8]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=10769150; DOI=10.1021/bi992631f;
Yang X., Le Brun N.E., Thomson A.J., Moore G.R., Chasteen N.D.;
"The iron oxidation and hydrolysis chemistry of Escherichia coli
bacterioferritin.";
Biochemistry 39:4915-4923(2000).
[10]
FUNCTION, ROLE OF THE FERROXIDASE CENTER IN CORE FORMATION, CATALYTIC
ACTIVITY, ENZYME REGULATION, AND MUTAGENESIS OF GLU-18; GLU-127 AND
HIS-130.
PubMed=14636073; DOI=10.1021/bi035253u;
Baaghil S., Lewin A., Moore G.R., Le Brun N.E.;
"Core formation in Escherichia coli bacterioferritin requires a
functional ferroxidase center.";
Biochemistry 42:14047-14056(2003).
[11]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH HEME AND
MANGANESE IONS.
PubMed=7664064; DOI=10.1038/nsb0794-453;
Frolow F., Kalb A.J., Yariv J.;
"Structure of a unique twofold symmetric haem-binding site.";
Nat. Struct. Biol. 1:453-460(1994).
[12]
X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) IN COMPLEX WITH HEME AND
MANGANESE IONS, AND SUBUNIT.
PubMed=9867433; DOI=10.1107/S0907444997006811;
Dautant A., Meyer J.-B., Yariv J., Precigoux G., Sweet R.M.,
Kalb A.J., Frolow F.;
"Structure of a monoclinic crystal form of cyctochrome b1
(bacterioferritin) from E. coli.";
Acta Crystallogr. D 54:16-24(1998).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH HEME; IRON AND
ZINC IONS.
STRAIN=B / BL21;
PubMed=17077480; DOI=10.1107/S1744309106039583;
van Eerde A., Wolterink-van Loo S., van der Oost J., Dijkstra B.W.;
"Fortuitous structure determination of 'as-isolated' Escherichia coli
bacterioferritin in a novel crystal form.";
Acta Crystallogr. F 62:1061-1066(2006).
[14]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANTS PHE-35 AND PHE-133 IN
COMPLEX WITH HEME AND IRON IONS, CATALYTIC ACTIVITY, AND ENZYME
REGULATION.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=19705876; DOI=10.1021/bi900869x;
Lawson T.L., Crow A., Lewin A., Yasmin S., Moore G.R., Le Brun N.E.;
"Monitoring the iron status of the ferroxidase center of Escherichia
coli bacterioferritin using fluorescence spectroscopy.";
Biochemistry 48:9031-9039(2009).
[15]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF METAL-FREE APOPROTEIN AND IN
COMPLEXES WITH ZN(2+); FE(2+); FE(3+) AND HEME, COFACTOR, INTERNAL
SURFACE IRON-BINDING SITE, MUTAGENESIS OF HIS-46 AND ASP-50, AND
MECHANISM OF IRON MINERALIZATION.
STRAIN=K12 / JM109 / ATCC 53323;
PubMed=19391621; DOI=10.1021/ja8093444;
Crow A., Lawson T.L., Lewin A., Moore G.R., Le Brun N.E.;
"Structural basis for iron mineralization by bacterioferritin.";
J. Am. Chem. Soc. 131:6808-6813(2009).
[16]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ARG-128/ARG-135 DIMER
IN COMPLEX WITH HEME AND ZINC IONS.
PubMed=19439409; DOI=10.1074/jbc.M901747200;
Wong S.G., Tom-Yew S.A., Lewin A., Le Brun N.E., Moore G.R.,
Murphy M.E., Mauk A.G.;
"Structural and mechanistic studies of a stabilized subunit dimer
variant of Escherichia coli bacterioferritin identify residues
required for core formation.";
J. Biol. Chem. 284:18873-18881(2009).
[17]
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH HEME AND ZINC
IONS.
STRAIN=B / BL21;
PubMed=18946693; DOI=10.1007/s00775-008-0438-8;
Willies S.C., Isupov M.N., Garman E.F., Littlechild J.A.;
"The binding of haem and zinc in the 1.9 A X-ray structure of
Escherichia coli bacterioferritin.";
J. Biol. Inorg. Chem. 14:201-207(2009).
[18]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH HEME.
PubMed=21215826; DOI=10.1016/j.bbapap.2010.12.017;
Antonyuk S.V., Hough M.A.;
"Monitoring and validating active site redox states in protein
crystals.";
Biochim. Biophys. Acta 1814:778-784(2011).
-!- FUNCTION: Iron-storage protein, whose ferroxidase center binds
Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates
in the subsequent Fe(3+) oxide mineral core formation within the
central cavity of the protein complex. The mineralized iron core
can contain as many as 2700 iron atoms/24-meric molecule.
{ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073}.
-!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
{ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073,
ECO:0000269|PubMed:19705876}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:19391621};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
{ECO:0000269|PubMed:19391621};
-!- COFACTOR:
Name=Fe cation; Xref=ChEBI:CHEBI:24875;
Evidence={ECO:0000269|PubMed:19391621};
Note=Binds 2 iron ions per subunit. The catalytic dinuclear iron-
binding site within each subunit is known as the ferroxidase
center. In BFR, the ferroxidase center appears to function as a
true di-iron catalytic cofactor, rather than as a pore for the
transfer of iron into the central cavity, as found for eukaryotic
ferritins. {ECO:0000269|PubMed:19391621};
-!- ENZYME REGULATION: Iron oxidation is inhibited by Zn(2+), which
binds at the ferroxidase center with a higher affinity that
Fe(2+). The occupation of the ferroxidase center by Zn(2+) also
severely restricts the ability of BFR to form an iron core.
{ECO:0000269|PubMed:10769150, ECO:0000269|PubMed:14636073,
ECO:0000269|PubMed:19705876}.
-!- SUBUNIT: Homooligomer of 24 subunits, arranged as 12 dimers, that
are packed together to form an approximately spherical molecule
with a central cavity, in which large amounts of iron can be
deposited as a ferric-oxy-hydroxide mineral core.
{ECO:0000269|PubMed:17077480, ECO:0000269|PubMed:18946693,
ECO:0000269|PubMed:19439409, ECO:0000269|PubMed:19705876,
ECO:0000269|PubMed:21215826, ECO:0000269|PubMed:7664064,
ECO:0000269|PubMed:9867433}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-907496, EBI-907496;
-!- MASS SPECTROMETRY: Mass=18496; Mass_error=2; Method=Electrospray;
Range=1-158; Evidence={ECO:0000269|PubMed:7559480};
-!- MISCELLANEOUS: The internal surface iron site that binds iron 3 is
important for the mineralization phase but not for Fe(2+) binding
and oxidation at the ferroxidase center.
-!- SIMILARITY: Belongs to the bacterioferritin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M27176; AAC13987.1; -; mRNA.
EMBL; AF058450; AAC14288.1; -; Genomic_DNA.
EMBL; U18997; AAA58133.1; -; Genomic_DNA.
EMBL; U00096; AAC76361.1; -; Genomic_DNA.
EMBL; AP009048; BAE77955.1; -; Genomic_DNA.
EMBL; L28106; AAC36929.1; -; Genomic_DNA.
PIR; JV0032; FREC.
RefSeq; NP_417795.1; NC_000913.3.
RefSeq; WP_000675504.1; NZ_LN832404.1.
PDB; 1BCF; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 1BFR; X-ray; 2.94 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-158.
PDB; 2HTN; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-158.
PDB; 2VXI; X-ray; 1.91 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 2Y3Q; X-ray; 1.55 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1J; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1L; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1M; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1N; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1O; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1P; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E1Q; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 3E2C; X-ray; 1.80 A; A/B=1-158.
PDB; 3GHQ; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 4CVP; X-ray; 2.11 A; A=1-158.
PDB; 4CVR; X-ray; 1.10 A; A=1-158.
PDB; 4CVS; X-ray; 1.39 A; A=1-158.
PDB; 4CVT; X-ray; 1.79 A; A=1-158.
PDB; 4U3G; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 4XKS; X-ray; 1.57 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 4XKT; X-ray; 1.82 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDB; 4XKU; X-ray; 1.78 A; A/B/C/D/E/F/G/H/I/J/K/L=1-158.
PDBsum; 1BCF; -.
PDBsum; 1BFR; -.
PDBsum; 2HTN; -.
PDBsum; 2VXI; -.
PDBsum; 2Y3Q; -.
PDBsum; 3E1J; -.
PDBsum; 3E1L; -.
PDBsum; 3E1M; -.
PDBsum; 3E1N; -.
PDBsum; 3E1O; -.
PDBsum; 3E1P; -.
PDBsum; 3E1Q; -.
PDBsum; 3E2C; -.
PDBsum; 3GHQ; -.
PDBsum; 4CVP; -.
PDBsum; 4CVR; -.
PDBsum; 4CVS; -.
PDBsum; 4CVT; -.
PDBsum; 4U3G; -.
PDBsum; 4XKS; -.
PDBsum; 4XKT; -.
PDBsum; 4XKU; -.
ProteinModelPortal; P0ABD3; -.
SMR; P0ABD3; -.
BioGrid; 4262466; 15.
DIP; DIP-36167N; -.
IntAct; P0ABD3; 3.
STRING; 316385.ECDH10B_3511; -.
EPD; P0ABD3; -.
PaxDb; P0ABD3; -.
PRIDE; P0ABD3; -.
EnsemblBacteria; AAC76361; AAC76361; b3336.
EnsemblBacteria; BAE77955; BAE77955; BAE77955.
GeneID; 947839; -.
KEGG; ecj:JW3298; -.
KEGG; eco:b3336; -.
PATRIC; fig|1411691.4.peg.3395; -.
EchoBASE; EB0111; -.
EcoGene; EG10113; bfr.
eggNOG; ENOG4108UQY; Bacteria.
eggNOG; COG2193; LUCA.
HOGENOM; HOG000262383; -.
InParanoid; P0ABD3; -.
KO; K03594; -.
PhylomeDB; P0ABD3; -.
BioCyc; EcoCyc:EG10113-MONOMER; -.
BioCyc; MetaCyc:EG10113-MONOMER; -.
BRENDA; 1.16.3.1; 2026.
EvolutionaryTrace; P0ABD3; -.
PRO; PR:P0ABD3; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; IDA:EcoCyc.
GO; GO:0020037; F:heme binding; IDA:EcoCyc.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
GO; GO:0016491; F:oxidoreductase activity; NAS:EcoliWiki.
GO; GO:0006880; P:intracellular sequestering of iron ion; IDA:EcoCyc.
GO; GO:0006826; P:iron ion transport; IEA:InterPro.
CDD; cd00907; Bacterioferritin; 1.
Gene3D; 1.20.1260.10; -; 1.
InterPro; IPR002024; Bacterioferritin.
InterPro; IPR012347; Ferritin-like.
InterPro; IPR009040; Ferritin-like_diiron.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR008331; Ferritin_DPS_dom.
Pfam; PF00210; Ferritin; 1.
PIRSF; PIRSF002560; Bacterioferritin; 1.
PRINTS; PR00601; BACFERRITIN.
SUPFAM; SSF47240; SSF47240; 1.
TIGRFAMs; TIGR00754; bfr; 1.
PROSITE; PS00549; BACTERIOFERRITIN; 1.
PROSITE; PS50905; FERRITIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Heme;
Iron; Iron storage; Metal-binding; Oxidoreductase; Reference proteome.
CHAIN 1 158 Bacterioferritin.
/FTId=PRO_0000192592.
DOMAIN 1 145 Ferritin-like diiron.
{ECO:0000255|PROSITE-ProRule:PRU00085}.
METAL 18 18 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 46 46 Iron 3. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 50 50 Iron 3. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 51 51 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 51 51 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 52 52 Iron (heme axial ligand); shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 54 54 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 94 94 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 127 127 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 127 127 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
METAL 130 130 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085,
ECO:0000269|PubMed:17077480}.
VARIANT 5 7 TKV -> VKI (in strain: ECOR 30).
VARIANT 38 38 K -> M (in strain: ECOR 30).
VARIANT 57 57 R -> K (in strain: ECOR 30).
VARIANT 68 68 L -> I (in strain: ECOR 30).
VARIANT 78 78 N -> G (in strain: ECOR 30).
VARIANT 88 88 R -> Q (in strain: ECOR 30).
VARIANT 92 92 A -> R (in strain: ECOR 30).
VARIANT 96 96 D -> E (in strain: ECOR 30).
VARIANT 100 100 N -> D (in strain: ECOR 30).
VARIANT 106 106 G -> A (in strain: ECOR 30).
VARIANT 125 125 R -> A (in strain: ECOR 30).
VARIANT 142 144 QKM -> GKI (in strain: ECOR 30).
VARIANT 152 158 AQIREEG -> SQIKVKD (in strain: ECOR 30).
MUTAGEN 18 18 E->A: Highly decreased Fe(2+) oxidation
activity. Is also severely restricted in
its ability to lay down an iron core.
{ECO:0000269|PubMed:14636073}.
MUTAGEN 31 31 M->H,L: No loss of heme binding.
{ECO:0000269|PubMed:7559480}.
MUTAGEN 46 46 H->A: Fe(2+)-binding and single turnover
oxidation at the ferroxidase center occur
normally but iron mineralization within
the cavity is significantly impaired.
{ECO:0000269|PubMed:19391621}.
MUTAGEN 50 50 D->A: Fe(2+)-binding and single turnover
oxidation at the ferroxidase center occur
normally but iron mineralization within
the cavity is significantly impaired.
{ECO:0000269|PubMed:19391621}.
MUTAGEN 52 52 M->H,L: Loss of heme binding. Is still
capable of accumulating iron.
{ECO:0000269|PubMed:7559480}.
MUTAGEN 86 86 M->L: No loss of heme binding.
{ECO:0000269|PubMed:7559480}.
MUTAGEN 127 127 E->Q: Decreased Fe(2+) oxidation
activity. Is also affected in its ability
to lay down an iron core.
{ECO:0000269|PubMed:14636073}.
MUTAGEN 130 130 H->E: Decreased Fe(2+) oxidation
activity. Is also severely restricted in
its ability to lay down an iron core.
{ECO:0000269|PubMed:14636073}.
CONFLICT 53 53 K -> M (in Ref. 5; AA sequence).
{ECO:0000305}.
HELIX 5 34 {ECO:0000244|PDB:4CVR}.
HELIX 38 64 {ECO:0000244|PDB:4CVR}.
HELIX 83 110 {ECO:0000244|PDB:4CVR}.
HELIX 114 144 {ECO:0000244|PDB:4CVR}.
HELIX 146 152 {ECO:0000244|PDB:4CVR}.
SEQUENCE 158 AA; 18495 MW; A6C86CE1CD8F865A CRC64;
MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID EMKHADRYIE
RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN LREAIGYADS VHDYVSRDMM
IEILRDEEGH IDWLETELDL IQKMGLQNYL QAQIREEG


Related products :

Catalog number Product name Quantity
EIAAB10220 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Homo sapiens,Human,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,
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
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 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
EIAAB10224 Cyba,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,Rat,Rattus norvegic
EIAAB10222 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,Pig,Superoxide-gene
EIAAB10221 Bos taurus,Bovine,CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,S
EIAAB10219 Cyba,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Mouse,Mus musculus,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,
EIAAB10223 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,Oryctolagus cuniculus,p22 phagocyte B-cytochrome,p22phox,p22-ph
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
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
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
EIAAB08851 Cyp1a2,Cyp1a-2,CYPIA2,Cytochrome P-448,Cytochrome P450 1A2,Cytochrome P-450d,Cytochrome P450-D,Rat,Rattus norvegicus
EIAAB08879 CYP26A2,CYP26B1,Cytochrome P450 26A2,Cytochrome P450 26B1,Cytochrome P450 retinoic acid-inactivating 2,Cytochrome P450RAI-2,Homo sapiens,Human,P450RAI2,Retinoic acid-metabolizing cytochrome
EIAAB08922 Cyp2c,Cyp2c11,Cyp2c-11,CYPIIC11,Cytochrome P450 2C11,Cytochrome P-450(M-1),Cytochrome P450H,Cytochrome P450-UT-2,Cytochrome P450-UT-A,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 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
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
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
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
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
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


 

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