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Flavin reductase (NADPH) (FR) (EC 1.5.1.30) (Biliverdin reductase B) (BVR-B) (EC 1.3.1.24) (Biliverdin-IX beta-reductase) (Green heme-binding protein) (GHBP) (NADPH-dependent diaphorase) (NADPH-flavin reductase) (FLR)

 BLVRB_HUMAN             Reviewed;         206 AA.
P30043; A6NKD8; B2R5C6; P32078; P53005; Q32LZ2;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 175.
RecName: Full=Flavin reductase (NADPH);
Short=FR;
EC=1.5.1.30 {ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:18241201};
AltName: Full=Biliverdin reductase B;
Short=BVR-B;
EC=1.3.1.24 {ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:18241201, ECO:0000269|PubMed:7929092};
AltName: Full=Biliverdin-IX beta-reductase;
AltName: Full=Green heme-binding protein;
Short=GHBP;
AltName: Full=NADPH-dependent diaphorase;
AltName: Full=NADPH-flavin reductase;
Short=FLR;
Name=BLVRB; Synonyms=FLR;
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 PROTEIN SEQUENCE OF 2-34; 63-87 AND
98-206.
TISSUE=Erythrocyte, and Reticulocyte;
PubMed=8117274; DOI=10.1006/bbrc.1994.1165;
Chikuba K., Yubisui T., Shirabe K., Takeshita M.;
"Cloning and nucleotide sequence of a cDNA of the human erythrocyte
NADPH-flavin reductase.";
Biochem. Biophys. Res. Commun. 198:1170-1176(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8799475; DOI=10.1248/bpb.19.796;
Komuro A., Tobe T., Hashimoto K., Nakano Y., Yamaguchi T.,
Nakajima H., Tomita M.;
"Molecular cloning and expression of human liver biliverdin-IXbeta
reductase.";
Biol. Pharm. Bull. 19:796-804(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
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 VARIANT GLN-46.
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
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).
[8]
PROTEIN SEQUENCE OF 2-205.
TISSUE=Liver;
PubMed=8280170; DOI=10.1006/bbrc.1993.2649;
Yamaguchi T., Komuro A., Nakano Y., Tomita M., Nakajima H.;
"Complete amino acid sequence of biliverdin-IX beta reductase from
human liver.";
Biochem. Biophys. Res. Commun. 197:1518-1523(1993).
[9]
PROTEIN SEQUENCE OF 2-21, SUBUNIT, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=7929092;
Yamaguchi T., Komoda Y., Nakajima H.;
"Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from
human liver. Purification and characterization.";
J. Biol. Chem. 269:24343-24348(1994).
[10]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[11]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Erythrocyte;
PubMed=8313871; DOI=10.1002/elps.11501401183;
Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C.,
Balant L., Hochstrasser D.F.;
"Plasma and red blood cell protein maps: update 1993.";
Electrophoresis 14:1223-1231(1993).
[12]
PROTEIN SEQUENCE OF 40-92; 64-78; 106-124 AND 146-170, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[13]
IDENTITY OF FR AND BVR-B.
PubMed=8687377; DOI=10.1042/bj3160385;
Shalloe F., Elliott G., Ennis O., Mantle T.J.;
"Evidence that biliverdin-IX beta reductase and flavin reductase are
identical.";
Biochem. J. 316:385-387(1996).
[14]
FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10620517; DOI=10.1042/bj3450393;
Cunningham O., Gore M.G., Mantle T.J.;
"Initial-rate kinetics of the flavin reductase reaction catalysed by
human biliverdin-IXbeta reductase (BVR-B).";
Biochem. J. 345:393-399(2000).
[15]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-153.
PubMed=18241201; DOI=10.1042/BJ20071495;
Smith L.J., Browne S., Mulholland A.J., Mantle T.J.;
"Computational and experimental studies on the catalytic mechanism of
biliverdin-IXbeta reductase.";
Biochem. J. 411:475-484(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND 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).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEXES WITH
MESOBILIVERDIN; BILIVERDIN; FLAVIN MONONUCLEOTIDE; LUMICHROME AND
NADP, AND SUBUNIT.
PubMed=11224564; DOI=10.1038/84948;
Pereira P.J., Macedo-Ribeiro S., Parraga A., Perez-Luque R.,
Cunningham O., Darcy K., Mantle T.J., Coll M.;
"Structure of human biliverdin IXbeta reductase, an early fetal
bilirubin IXbeta producing enzyme.";
Nat. Struct. Biol. 8:215-220(2001).
-!- FUNCTION: Broad specificity oxidoreductase that catalyzes the
NADPH-dependent reduction of a variety of flavins, such as
riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ
(pyrroloquinoline quinone). Contributes to heme catabolism and
metabolizes linear tetrapyrroles. Can also reduce the complexed
Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the
liver, converts biliverdin to bilirubin.
{ECO:0000269|PubMed:10620517}.
-!- CATALYTIC ACTIVITY: Reduced riboflavin + NADP(+) = riboflavin +
NADPH. {ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:18241201}.
-!- CATALYTIC ACTIVITY: Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H.
{ECO:0000269|PubMed:10620517, ECO:0000269|PubMed:18241201,
ECO:0000269|PubMed:7929092}.
-!- ENZYME REGULATION: Mesobiliverdin acts as competitve inhibitor for
flavin reduction, indicating that flavin and tetrapyrrole
substrates compete for the same site.
{ECO:0000269|PubMed:10620517}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=36 uM for NADP {ECO:0000269|PubMed:10620517,
ECO:0000269|PubMed:7929092};
KM=5.6 mM for NADH {ECO:0000269|PubMed:10620517,
ECO:0000269|PubMed:7929092};
KM=0.3 uM for biliverdin IX-beta {ECO:0000269|PubMed:10620517,
ECO:0000269|PubMed:7929092};
KM=52 uM for FMN {ECO:0000269|PubMed:10620517,
ECO:0000269|PubMed:7929092};
KM=125 uM for FAD {ECO:0000269|PubMed:10620517,
ECO:0000269|PubMed:7929092};
KM=53 uM for riboflavin {ECO:0000269|PubMed:10620517,
ECO:0000269|PubMed:7929092};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11224564,
ECO:0000269|PubMed:7929092}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7929092}.
-!- TISSUE SPECIFICITY: Predominantly expressed in liver and
erythrocytes. At lower levels in heart, lung, adrenal gland and
cerebrum. {ECO:0000269|PubMed:7929092}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/blvrb/";
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EMBL; D26308; BAA05370.1; -; mRNA.
EMBL; D32143; BAA06874.1; -; mRNA.
EMBL; AK312137; BAG35073.1; -; mRNA.
EMBL; AY340485; AAP88933.1; -; Genomic_DNA.
EMBL; AC010271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471126; EAW56969.1; -; Genomic_DNA.
EMBL; BC109371; AAI09372.1; -; mRNA.
CCDS; CCDS33029.1; -.
PIR; JC2070; JC2070.
RefSeq; NP_000704.1; NM_000713.2.
UniGene; Hs.515785; -.
PDB; 1HDO; X-ray; 1.15 A; A=2-205.
PDB; 1HE2; X-ray; 1.20 A; A=2-205.
PDB; 1HE3; X-ray; 1.40 A; A=2-205.
PDB; 1HE4; X-ray; 1.40 A; A=2-205.
PDB; 1HE5; X-ray; 1.50 A; A=2-205.
PDBsum; 1HDO; -.
PDBsum; 1HE2; -.
PDBsum; 1HE3; -.
PDBsum; 1HE4; -.
PDBsum; 1HE5; -.
ProteinModelPortal; P30043; -.
SMR; P30043; -.
BioGrid; 107114; 13.
IntAct; P30043; 6.
MINT; MINT-5001335; -.
STRING; 9606.ENSP00000263368; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB02073; Biliverdine Ix Alpha.
DrugBank; DB04363; Mesobiliverdin Iv Alpha.
DrugBank; DB00157; NADH.
DrugBank; DB00140; Riboflavin.
DrugBank; DB03247; Riboflavin Monophosphate.
iPTMnet; P30043; -.
PhosphoSitePlus; P30043; -.
BioMuta; BLVRB; -.
DMDM; 1706870; -.
DOSAC-COBS-2DPAGE; P30043; -.
REPRODUCTION-2DPAGE; IPI00783862; -.
SWISS-2DPAGE; P30043; -.
UCD-2DPAGE; P30043; -.
EPD; P30043; -.
PaxDb; P30043; -.
PeptideAtlas; P30043; -.
PRIDE; P30043; -.
TopDownProteomics; P30043; -.
Ensembl; ENST00000263368; ENSP00000263368; ENSG00000090013.
GeneID; 645; -.
KEGG; hsa:645; -.
CTD; 645; -.
DisGeNET; 645; -.
EuPathDB; HostDB:ENSG00000090013.9; -.
GeneCards; BLVRB; -.
HGNC; HGNC:1063; BLVRB.
HPA; HPA041698; -.
HPA; HPA041937; -.
MIM; 600941; gene.
neXtProt; NX_P30043; -.
OpenTargets; ENSG00000090013; -.
PharmGKB; PA25374; -.
eggNOG; ENOG410IXV9; Eukaryota.
eggNOG; ENOG4111JAS; LUCA.
GeneTree; ENSGT00390000014810; -.
HOGENOM; HOG000262432; -.
HOVERGEN; HBG050695; -.
InParanoid; P30043; -.
KO; K05901; -.
OMA; TEIRPAW; -.
OrthoDB; EOG091G0PLW; -.
PhylomeDB; P30043; -.
TreeFam; TF324063; -.
BRENDA; 1.3.1.24; 2681.
BRENDA; 1.5.1.30; 2681.
Reactome; R-HSA-189483; Heme degradation.
EvolutionaryTrace; P30043; -.
GenomeRNAi; 645; -.
PRO; PR:P30043; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000090013; -.
CleanEx; HS_BLVRB; -.
ExpressionAtlas; P30043; baseline and differential.
Genevisible; P30043; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
GO; GO:0004074; F:biliverdin reductase activity; IDA:UniProtKB.
GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IDA:UniProtKB.
GO; GO:0042167; P:heme catabolic process; IDA:UniProtKB.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF13460; NAD_binding_10; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
NADP; Oxidoreductase; Phosphoprotein; Polymorphism;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1286669,
ECO:0000269|PubMed:7929092,
ECO:0000269|PubMed:8117274,
ECO:0000269|PubMed:8280170,
ECO:0000269|PubMed:8313871}.
CHAIN 2 206 Flavin reductase (NADPH).
/FTId=PRO_0000064948.
NP_BIND 10 15 NADP.
NP_BIND 54 55 NADP.
NP_BIND 75 78 NADP.
BINDING 35 35 NADP.
BINDING 132 132 NADP.
BINDING 153 153 Substrate.
BINDING 154 154 NADP; via amide nitrogen.
MOD_RES 42 42 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 46 46 R -> Q (in dbSNP:rs11547746).
{ECO:0000269|Ref.4}.
/FTId=VAR_019168.
MUTAGEN 153 153 H->A: Reduced affinity for biliverdin.
{ECO:0000269|PubMed:18241201}.
CONFLICT 16 16 G -> C (in Ref. 9; AA sequence).
{ECO:0000305}.
STRAND 5 10 {ECO:0000244|PDB:1HDO}.
HELIX 14 25 {ECO:0000244|PDB:1HDO}.
STRAND 29 35 {ECO:0000244|PDB:1HDO}.
HELIX 37 39 {ECO:0000244|PDB:1HDO}.
STRAND 42 44 {ECO:0000244|PDB:1HDO}.
STRAND 48 53 {ECO:0000244|PDB:1HDO}.
HELIX 58 65 {ECO:0000244|PDB:1HDO}.
STRAND 69 73 {ECO:0000244|PDB:1HDO}.
HELIX 86 101 {ECO:0000244|PDB:1HDO}.
STRAND 105 109 {ECO:0000244|PDB:1HDO}.
HELIX 112 114 {ECO:0000244|PDB:1HDO}.
HELIX 118 120 {ECO:0000244|PDB:1HE2}.
HELIX 123 125 {ECO:0000244|PDB:1HDO}.
HELIX 126 141 {ECO:0000244|PDB:1HDO}.
STRAND 144 149 {ECO:0000244|PDB:1HDO}.
STRAND 152 155 {ECO:0000244|PDB:1HDO}.
STRAND 164 169 {ECO:0000244|PDB:1HDO}.
STRAND 174 177 {ECO:0000244|PDB:1HDO}.
HELIX 178 187 {ECO:0000244|PDB:1HDO}.
HELIX 188 190 {ECO:0000244|PDB:1HE2}.
TURN 193 196 {ECO:0000244|PDB:1HDO}.
STRAND 198 202 {ECO:0000244|PDB:1HDO}.
SEQUENCE 206 AA; 22119 MW; 3057E6D69A9F9F9F CRC64;
MAVKKIAIFG ATGQTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPRPAHV VVGDVLQAAD
VDKTVAGQDA VIVLLGTRND LSPTTVMSEG ARNIVAAMKA HGVDKVVACT SAFLLWDPTK
VPPRLQAVTD DHIRMHKVLR ESGLKYVAVM PPHIGDQPLT GAYTVTLDGR GPSRVISKHD
LGHFMLRCLT TDEYDGHSTY PSHQYQ


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CSB-PA002722GA01HU Rabbit anti-human biliverdin reductase B (flavin reductase (NADPH)) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA002722GA01HU Rabbit anti-human biliverdin reductase B (flavin reductase (NADPH)) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
EIAAB05623 Adipocyte protein P27,AP27,Carbonyl reductase [NADPH] 2,Cbr2,LCR,Lung carbonyl reductase,Mouse,Mus musculus,NADPH-dependent carbonyl reductase 2
EIAAB05620 15-hydroxyprostaglandin dehydrogenase [NADP+],Carbonyl reductase [NADPH] 1,Cbr,Cbr1,Mouse,Mus musculus,NADPH-dependent carbonyl reductase 1,Prostaglandin 9-ketoreductase,Prostaglandin-E(2) 9-reductase
EIAAB05619 15-hydroxyprostaglandin dehydrogenase [NADP+],Bos taurus,Bovine,Carbonyl reductase [NADPH] 1,CBR1,NADPH-dependent carbonyl reductase 1,Prostaglandin 9-ketoreductase,Prostaglandin-E(2) 9-reductase
EIAAB10841 2,4-dienoyl-CoA reductase [NADPH],2,4-dienoyl-CoA reductase, mitochondrial,4-enoyl-CoA reductase [NADPH],DECR,DECR1,Homo sapiens,Human
EIAAB10839 2,4-dienoyl-CoA reductase [NADPH],2,4-dienoyl-CoA reductase, mitochondrial,4-enoyl-CoA reductase [NADPH],Decr,Decr1,Rat,Rattus norvegicus
EIAAB05621 15-hydroxyprostaglandin dehydrogenase [NADP+],20-beta-hydroxysteroid dehydrogenase,Carbonyl reductase [NADPH] 1,CBR,CBR1,NADPH-dependent carbonyl reductase 1,Oryctolagus cuniculus,Prostaglandin 9-keto
EIAAB05618 15-hydroxyprostaglandin dehydrogenase [NADP+],20-beta-hydroxysteroid dehydrogenase,Carbonyl reductase [NADPH] 1,Cbr,Cbr1,NADPH-dependent carbonyl reductase 1,Prostaglandin 9-ketoreductase,Prostaglandi
EIAAB05616 15-hydroxyprostaglandin dehydrogenase [NADP+],20-beta-hydroxysteroid dehydrogenase,Carbonyl reductase [NADPH] 1,CBR,CBR1,CRN,NADPH-dependent carbonyl reductase 1,Pig,Prostaglandin 9-ketoreductase,Pros
EIAAB05622 Carbonyl reductase [NADPH] 2,CBR2,LCR,Lung carbonyl reductase,NADPH-dependent carbonyl reductase 2,Pig,Sus scrofa
EIAAB10840 2,4-dienoyl-CoA reductase [NADPH],2,4-dienoyl-CoA reductase, mitochondrial,4-enoyl-CoA reductase [NADPH],Decr1,Mouse,Mus musculus
EIAAB05624 Carbonyl reductase [NADPH] 3,CBR3,Homo sapiens,Human,NADPH-dependent carbonyl reductase 3
EIAAB05617 15-hydroxyprostaglandin dehydrogenase [NADP+],Carbonyl reductase [NADPH] 1,CBR,CBR1,CRN,Homo sapiens,Human,NADPH-dependent carbonyl reductase 1,Prostaglandin 9-ketoreductase,Prostaglandin-E(2) 9-reduc
BLVRB_MOUSE Mouse ELISA Kit FOR Flavin reductase (NADPH) 96T
BLVRB_BOVIN Bovine ELISA Kit FOR Flavin reductase (NADPH) 96T
BLVRB_MOUSE ELISA Kit FOR Flavin reductase (NADPH); organism: Mouse; gene name: Blvrb 96T
EIAAB44144 NADPH-dependent thioredoxin reductase,Rat,Rattus norvegicus,Thioredoxin reductase 1, cytoplasmic,Thioredoxin reductase TR1,TR,Trxr1,Txnrd1


 

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