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

3-alpha-hydroxysteroid dehydrogenase (3-alpha-HSD) (EC 1.1.1.50) (Hydroxyprostaglandin dehydrogenase)

 DIDH_RAT                Reviewed;         322 AA.
P23457; Q5BKC8; Q6LDE6; Q6LDE7;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
05-DEC-2018, entry version 153.
RecName: Full=3-alpha-hydroxysteroid dehydrogenase;
Short=3-alpha-HSD;
EC=1.1.1.50;
AltName: Full=Hydroxyprostaglandin dehydrogenase;
Name=Akr1c9;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=1840601;
Pawlowski J.E., Huizinga M., Penning T.M.;
"Cloning and sequencing of the cDNA for rat liver 3 alpha-
hydroxysteroid/dihydrodiol dehydrogenase.";
J. Biol. Chem. 266:8820-8825(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=1714456;
Stolz A., Rahimi-Kiani M., Ameis D., Chan E., Ronk M., Shively J.E.;
"Molecular structure of rat hepatic 3 alpha-hydroxysteroid
dehydrogenase. A member of the oxidoreductase gene family.";
J. Biol. Chem. 266:15253-15257(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1922097; DOI=10.1210/mend-5-6-823;
Cheng K.-C., White P.C., Qin K.-N.;
"Molecular cloning and expression of rat liver 3 alpha-hydroxysteroid
dehydrogenase.";
Mol. Endocrinol. 5:823-828(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7515872; DOI=10.1093/oxfordjournals.jbchem.a124323;
Usui E., Okuda K., Kato Y., Noshiro M.;
"Rat hepatic 3 alpha-hydroxysteroid dehydrogenase: expression of cDNA
and physiological function in bile acid biosynthetic pathway.";
J. Biochem. 115:230-237(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley;
PubMed=10619355; DOI=10.1016/S0960-0760(99)00122-3;
Lin H.K., Hung C.F., Moore M., Penning T.M.;
"Genomic structure of rat 3alpha-hydroxysteroid/dihydrodiol
dehydrogenase (3alpha-HSD/DD, AKR1C9).";
J. Steroid Biochem. Mol. Biol. 71:29-39(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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]
PROTEIN SEQUENCE OF 2-16; 121-135; 152-166 AND 203-217.
TISSUE=Liver;
PubMed=7998972;
Del Bello B., Maellaro E., Sugherini L., Santucci A., Comporti M.,
Casini A.F.;
"Purification of NADPH-dependent dehydroascorbate reductase from rat
liver and its identification with 3 alpha-hydroxysteroid
dehydrogenase.";
Biochem. J. 304:385-390(1994).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 112-169 AND 238-322.
PubMed=1793046; DOI=10.1007/BF01993305;
Pawlowski J., Huizinga M., Penning T.M.;
"Isolation and partial characterization of a full-length cDNA clone
for 3 alpha-hydroxysteroid dehydrogenase: a potential target enzyme
for nonsteroidal anti-inflammatory drugs.";
Agents Actions 34:289-293(1991).
[9]
PROTEIN SEQUENCE OF 162-171; 208-223 AND 232-246.
PubMed=2026597;
Penning T.M., Abrams W.R., Pawlowski J.E.;
"Affinity labeling of 3 alpha-hydroxysteroid dehydrogenase with 3
alpha-bromoacetoxyandrosterone and 11 alpha-bromoacetoxyprogesterone.
Isolation and sequence of active site peptides containing reactive
cysteines; sequence confirmation using nucleotide sequence from a cDNA
clone.";
J. Biol. Chem. 266:8826-8834(1991).
[10]
TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=7626489; DOI=10.1016/0960-0760(95)00019-V;
Khanna M., Qin K.-N., Cheng K.-C.;
"Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and
molecular cloning of multiple cDNAs encoding structurally related
proteins in humans.";
J. Steroid Biochem. Mol. Biol. 53:41-46(1995).
[11]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
TISSUE=Liver;
PubMed=8146147; DOI=10.1073/pnas.91.7.2517;
Hoog S.S., Pawlowski J.E., Alzari P.M., Penning T.M., Lewis M.;
"Three-dimensional structure of rat liver 3 alpha-
hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto
reductase superfamily.";
Proc. Natl. Acad. Sci. U.S.A. 91:2517-2521(1994).
[12]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=8718859; DOI=10.1021/bi9604688;
Bennett M.J., Schlegel B.P., Jez J.M., Penning T.M., Lewis M.;
"Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase
complexed with NADP+.";
Biochemistry 35:10702-10711(1996).
[13]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH NADP AND
TESTOSTERONE.
PubMed=9261071; DOI=10.1016/S0969-2126(97)00234-7;
Bennett M.J., Albert R.H., Jez J.M., Ma H., Penning T.M., Lewis M.;
"Steroid recognition and regulation of hormone action: crystal
structure of testosterone and NADP+ bound to 3 alpha-
hydroxysteroid/dihydrodiol dehydrogenase.";
Structure 5:799-812(1997).
-!- FUNCTION: Besides being a 3-alpha-hydroxysteroid dehydrogenase,
the enzyme can accomplish diverse functions: as quinone reductase,
as an aromatic alcohol dehydrogenase, as dihydrodiol
dehydrogenase, and as 9-, 11-, and 15-hydroxyprostaglandin
dehydrogenase.
-!- CATALYTIC ACTIVITY:
Reaction=a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+)
+ NADPH; Xref=Rhea:RHEA:34783, ChEBI:CHEBI:15378,
ChEBI:CHEBI:36835, ChEBI:CHEBI:47788, ChEBI:CHEBI:57783,
ChEBI:CHEBI:58349; EC=1.1.1.50;
-!- CATALYTIC ACTIVITY:
Reaction=a 3alpha-hydroxysteroid + NAD(+) = a 3-oxosteroid + H(+)
+ NADH; Xref=Rhea:RHEA:34779, ChEBI:CHEBI:15378,
ChEBI:CHEBI:36835, ChEBI:CHEBI:47788, ChEBI:CHEBI:57540,
ChEBI:CHEBI:57945; EC=1.1.1.50;
-!- ACTIVITY REGULATION: Potently inhibited by the nonsteroidal anti-
inflammatory drugs (NSAID).
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9261071}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: In brain, highest levels found in olfactory
bulb. Moderate levels present in cerebellum, cerebral cortex,
hypothalamus and pituitary. Low levels present in amygdala, brain
stem, caudate putamen, cingulate cortex, hippocampus, midbrain,
and thalamus. {ECO:0000269|PubMed:7626489}.
-!- SIMILARITY: Belongs to the aldo/keto reductase family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M64393; AAA40605.1; -; mRNA.
EMBL; M61937; AAA41077.1; -; mRNA.
EMBL; D17310; BAA04132.1; -; mRNA.
EMBL; S57790; AAB19918.1; -; mRNA.
EMBL; AF180334; AAF25813.1; -; Genomic_DNA.
EMBL; AF180326; AAF25813.1; JOINED; Genomic_DNA.
EMBL; AF180327; AAF25813.1; JOINED; Genomic_DNA.
EMBL; AF180328; AAF25813.1; JOINED; Genomic_DNA.
EMBL; AF180329; AAF25813.1; JOINED; Genomic_DNA.
EMBL; AF180330; AAF25813.1; JOINED; Genomic_DNA.
EMBL; AF180331; AAF25813.1; JOINED; Genomic_DNA.
EMBL; AF180332; AAF25813.1; JOINED; Genomic_DNA.
EMBL; AF180333; AAF25813.1; JOINED; Genomic_DNA.
EMBL; BC091123; AAH91123.1; -; mRNA.
EMBL; S35751; AAB21512.1; -; mRNA.
EMBL; S35752; AAB21513.1; -; mRNA.
PIR; A39350; A39350.
PIR; PC2175; PC2175.
RefSeq; NP_612556.1; NM_138547.3.
UniGene; Rn.10021; -.
UniGene; Rn.206655; -.
PDB; 1AFS; X-ray; 2.50 A; A/B=1-322.
PDB; 1LWI; X-ray; 2.70 A; A/B=1-322.
PDB; 1RAL; X-ray; 3.00 A; A=1-308.
PDBsum; 1AFS; -.
PDBsum; 1LWI; -.
PDBsum; 1RAL; -.
ProteinModelPortal; P23457; -.
SMR; P23457; -.
STRING; 10116.ENSRNOP00000023835; -.
ChEMBL; CHEMBL1075221; -.
iPTMnet; P23457; -.
PhosphoSitePlus; P23457; -.
PaxDb; P23457; -.
PRIDE; P23457; -.
Ensembl; ENSRNOT00000023835; ENSRNOP00000023835; ENSRNOG00000017672.
GeneID; 191574; -.
KEGG; rno:191574; -.
UCSC; RGD:708361; rat.
CTD; 105387; -.
RGD; 708361; LOC191574.
eggNOG; KOG1577; Eukaryota.
eggNOG; COG0656; LUCA.
GeneTree; ENSGT00940000153677; -.
HOGENOM; HOG000250272; -.
HOVERGEN; HBG000020; -.
InParanoid; P23457; -.
OMA; AWYYGTE; -.
OrthoDB; EOG091G0D69; -.
PhylomeDB; P23457; -.
TreeFam; TF106492; -.
BioCyc; MetaCyc:MONOMER-14305; -.
BRENDA; 1.1.1.213; 5301.
BRENDA; 1.6.5.10; 5301.
Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-RNO-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
Reactome; R-RNO-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-RNO-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
Reactome; R-RNO-5365859; RA biosynthesis pathway.
Reactome; R-RNO-975634; Retinoid metabolism and transport.
SABIO-RK; P23457; -.
EvolutionaryTrace; P23457; -.
PRO; PR:P23457; -.
Proteomes; UP000002494; Chromosome 17.
Bgee; ENSRNOG00000017672; Expressed in 9 organ(s), highest expression level in liver.
Genevisible; P23457; RN.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IBA:GO_Central.
GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
GO; GO:0047042; F:androsterone dehydrogenase (B-specific) activity; IEA:UniProtKB-EC.
GO; GO:0047023; F:androsterone dehydrogenase activity; IBA:GO_Central.
GO; GO:0047086; F:ketosteroid monooxygenase activity; IBA:GO_Central.
GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
GO; GO:0016229; F:steroid dehydrogenase activity; IMP:RGD.
GO; GO:0044597; P:daunorubicin metabolic process; IBA:GO_Central.
GO; GO:0044598; P:doxorubicin metabolic process; IBA:GO_Central.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0042448; P:progesterone metabolic process; IBA:GO_Central.
GO; GO:0006693; P:prostaglandin metabolic process; IBA:GO_Central.
GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
CDD; cd06660; Aldo_ket_red; 1.
Gene3D; 3.20.20.100; -; 1.
InterPro; IPR018170; Aldo/ket_reductase_CS.
InterPro; IPR020471; Aldo/keto_reductase.
InterPro; IPR023210; NADP_OxRdtase_dom.
InterPro; IPR036812; NADP_OxRdtase_dom_sf.
PANTHER; PTHR11732; PTHR11732; 1.
Pfam; PF00248; Aldo_ket_red; 1.
PIRSF; PIRSF000097; AKR; 1.
PRINTS; PR00069; ALDKETRDTASE.
SUPFAM; SSF51430; SSF51430; 1.
PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
NAD; NADP; Oxidoreductase; Reference proteome.
CHAIN 1 322 3-alpha-hydroxysteroid dehydrogenase.
/FTId=PRO_0000124654.
NP_BIND 20 24 NADP. {ECO:0000269|PubMed:9261071}.
NP_BIND 166 167 NADP. {ECO:0000269|PubMed:9261071}.
NP_BIND 216 221 NADP. {ECO:0000269|PubMed:9261071}.
NP_BIND 270 280 NADP. {ECO:0000269|PubMed:9261071}.
ACT_SITE 55 55 Proton donor.
BINDING 50 50 NADP. {ECO:0000269|PubMed:9261071}.
BINDING 117 117 Substrate.
BINDING 190 190 NADP. {ECO:0000269|PubMed:9261071}.
BINDING 227 227 Substrate.
SITE 84 84 Lowers pKa of active site Tyr.
{ECO:0000250}.
MOD_RES 1 1 Blocked amino end (Met).
CONFLICT 108 108 L -> Q (in Ref. 3; AAB19918).
{ECO:0000305}.
CONFLICT 273 274 NA -> KP (in Ref. 3; AAB19918).
{ECO:0000305}.
CONFLICT 280 280 L -> P (in Ref. 3; AAB19918).
{ECO:0000305}.
HELIX 3 5 {ECO:0000244|PDB:1AFS}.
STRAND 7 9 {ECO:0000244|PDB:1AFS}.
TURN 11 13 {ECO:0000244|PDB:1RAL}.
STRAND 15 22 {ECO:0000244|PDB:1AFS}.
TURN 28 30 {ECO:0000244|PDB:1RAL}.
HELIX 33 43 {ECO:0000244|PDB:1AFS}.
STRAND 48 50 {ECO:0000244|PDB:1AFS}.
TURN 53 56 {ECO:0000244|PDB:1AFS}.
HELIX 58 70 {ECO:0000244|PDB:1AFS}.
HELIX 76 78 {ECO:0000244|PDB:1AFS}.
STRAND 80 85 {ECO:0000244|PDB:1AFS}.
HELIX 87 89 {ECO:0000244|PDB:1AFS}.
HELIX 92 94 {ECO:0000244|PDB:1AFS}.
HELIX 95 106 {ECO:0000244|PDB:1AFS}.
STRAND 109 117 {ECO:0000244|PDB:1AFS}.
STRAND 124 129 {ECO:0000244|PDB:1AFS}.
STRAND 131 137 {ECO:0000244|PDB:1RAL}.
HELIX 144 156 {ECO:0000244|PDB:1AFS}.
STRAND 159 167 {ECO:0000244|PDB:1AFS}.
HELIX 170 177 {ECO:0000244|PDB:1AFS}.
STRAND 187 192 {ECO:0000244|PDB:1AFS}.
HELIX 200 209 {ECO:0000244|PDB:1AFS}.
STRAND 212 217 {ECO:0000244|PDB:1AFS}.
TURN 225 227 {ECO:0000244|PDB:1AFS}.
HELIX 235 237 {ECO:0000244|PDB:1AFS}.
HELIX 239 247 {ECO:0000244|PDB:1AFS}.
HELIX 252 262 {ECO:0000244|PDB:1AFS}.
STRAND 266 269 {ECO:0000244|PDB:1AFS}.
HELIX 274 280 {ECO:0000244|PDB:1AFS}.
TURN 281 284 {ECO:0000244|PDB:1AFS}.
HELIX 290 297 {ECO:0000244|PDB:1AFS}.
HELIX 309 311 {ECO:0000244|PDB:1AFS}.
SEQUENCE 322 AA; 37028 MW; 592EFC584726A4F6 CRC64;
MDSISLRVAL NDGNFIPVLG FGTTVPEKVA KDEVIKATKI AIDNGFRHFD SAYLYEVEEE
VGQAIRSKIE DGTVKREDIF YTSKLWSTFH RPELVRTCLE KTLKSTQLDY VDLYIIHFPM
ALQPGDIFFP RDEHGKLLFE TVDICDTWEA MEKCKDAGLA KSIGVSNFNC RQLERILNKP
GLKYKPVCNQ VECHLYLNQS KMLDYCKSKD IILVSYCTLG SSRDKTWVDQ KSPVLLDDPV
LCAIAKKYKQ TPALVALRYQ LQRGVVPLIR SFNAKRIKEL TQVFEFQLAS EDMKALDGLN
RNFRYNNAKY FDDHPNHPFT DE


Related products :

Catalog number Product name Quantity
EIAAB11263 3-alpha-HSD,3-alpha-hydroxysteroid dehydrogenase,Akr1c9,Hydroxyprostaglandin dehydrogenase,Rat,Rattus norvegicus
EIAAB11092 17-beta-HSD 1,17-beta-hydroxysteroid dehydrogenase type 1,20 alpha-hydroxysteroid dehydrogenase,20-alpha-HSD,E17KSR,E2DH,EDH17B1,EDH17B2,EDHB17,Estradiol 17-beta-dehydrogenase 1,Homo sapiens,HSD17B1,H
EIAAB11105 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,20 alpha-hydroxysteroid dehydrogenase,20-alpha-HSD,E2DH,EDH17B2,Estradiol 17-beta-dehydrogenase 2,Homo sapiens,HSD17B2,Human,Microsomal 17-bet
AKR1C3 AKR1C1 Gene aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase)
CSB-EL001542HU Human aldo-keto reductase family 1, member C1 (dihydrodiol dehydrogenase 1; 20-alpha (3-alpha)-hydroxysteroid dehydrogenase) (AKR1C1) ELISA kit, Species Human, Sample Type serum, plasma 96T
AKR1C4 AKR1C2 Gene aldo-keto reductase family 1, member C2 (dihydrodiol dehydrogenase 2; bile acid binding protein; 3-alpha hydroxysteroid dehydrogenase, type III)
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
AKR1E2 AKR1C4 Gene aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol dehydrogenase 4)
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
EIAAB30480 20-alpha-HSD,20-alpha-hydroxysteroid dehydrogenase,AKR1C5,Oryctolagus cuniculus,Prostaglandin-E(2) 9-reductase,Rabbit
10-611-183001 3 alpha-Hydroxysteroid Dehydrogenase (3 alpha-HSDH (Bacteria)) - 500 Units
10-611-183001 3 alpha-Hydroxysteroid Dehydrogenase (3 alpha-HSDH (Bacteria)) - 100 Units
10-611-183001 3 alpha-Hydroxysteroid Dehydrogenase (3 alpha-HSDH (Bacteria)) - 25 Units
EIAAB28643 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial,BCKDE1A,BCKDH E1-alpha,BCKDHA,Bos taurus,Bovine,Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
EIAAB28644 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial,BCKDE1A,BCKDH E1-alpha,Bckdha,Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain,Mouse,Mus musculus
EIAAB28642 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial,BCKDE1A,BCKDH E1-alpha,Bckdha,Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain,Rat,Rattus norvegicus
EIAAB28641 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial,BCKDE1A,BCKDH E1-alpha,BCKDHA,Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain,Homo sapiens,Human
EIAAB11152 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,Homo sapiens,HSD11B2,HSD11K,Human,NAD-dependent 11-beta-hydroxysteroid dehydrogenase
EIAAB11149 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,HSD11B2,NAD-dependent 11-beta-hydroxysteroid dehydrogenase,Oryctolagus cuniculus,Rabbit
EIAAB11151 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,Hsd11b2,Hsd11k,Mouse,Mus musculus,NAD-dependent 11-beta-hydroxysteroid dehydrogenase
EIAAB11148 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Corticosteroid 11-beta-dehydrogenase isozyme 2,Hsd11b2,Hsd11k,NAD-dependent 11-beta-hydroxysteroid dehydrogenase,Rat,Rattus norvegicus
EIAAB11150 11-beta-HSD2,11-beta-hydroxysteroid dehydrogenase type 2,11-DH2,Bos taurus,Bovine,Corticosteroid 11-beta-dehydrogenase isozyme 2,HSD11B2,NAD-dependent 11-beta-hydroxysteroid dehydrogenase
EIAAB11106 17-beta-HSD 3,17-beta-hydroxysteroid dehydrogenase type 3,EDH17B3,Homo sapiens,HSD17B3,Human,Testicular 17-beta-hydroxysteroid dehydrogenase,Testosterone 17-beta-dehydrogenase 3
77758 IgG,3 ALPHA HYDROXYSTEROID DEHYDROGENASE 1 ml


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | 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 | 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 | 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 | Gentaur