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

3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1 1 1 35) (17-beta-hydroxysteroid dehydrogenase 10) (17-beta-HSD 10) (EC 1 1 1 51) (3-hydroxy-2-methylbutyryl-CoA dehydrogenase) (EC 1 1 1 178) (3-hydroxyacyl-CoA dehydrogenase type II) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Scully protein) (Type II HADH)

 HCD2_DROME              Reviewed;         255 AA.
O18404; G7H840; Q059C3; Q8MRC1;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
12-SEP-2018, entry version 157.
RecName: Full=3-hydroxyacyl-CoA dehydrogenase type-2;
EC=1.1.1.35;
AltName: Full=17-beta-hydroxysteroid dehydrogenase 10;
Short=17-beta-HSD 10;
EC=1.1.1.51;
AltName: Full=3-hydroxy-2-methylbutyryl-CoA dehydrogenase;
EC=1.1.1.178;
AltName: Full=3-hydroxyacyl-CoA dehydrogenase type II;
AltName: Full=Mitochondrial ribonuclease P protein 2;
Short=Mitochondrial RNase P protein 2;
AltName: Full=Scully protein;
AltName: Full=Type II HADH;
Name=scu; ORFNames=CG7113;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-33
AND PHE-120.
STRAIN=Canton-S;
PubMed=9585418; DOI=10.1083/jcb.141.4.1009;
Torroja L., Ortuno-Sahagun D., Ferrus A., Haemmerle B., Barbas J.A.;
"Scully, an essential gene of Drosophila, is homologous to mammalian
mitochondrial type II L-3-hydroxyacyl-CoA dehydrogenase/amyloid-beta
peptide-binding protein.";
J. Cell Biol. 141:1009-1018(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
Stapleton M., Booth B., Carlson J.W., Frise E., Kapadia B., Park S.,
Wan K.H., Yu C., Celniker S.E.;
Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12917011; DOI=10.1042/BJ20030877;
Shafqat N., Marschall H.U., Filling C., Nordling E., Wu X.Q.,
Bjork L., Thyberg J., Martensson E., Salim S., Jornvall H.,
Oppermann U.;
"Expanded substrate screenings of human and Drosophila type 10 17beta-
hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in
bile acid and steroid hormone metabolism: characterization of
multifunctional 3alpha/7alpha/7beta/17beta/20beta/21-HSD.";
Biochem. J. 376:49-60(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=16979555; DOI=10.1016/j.cub.2006.07.062;
Cermelli S., Guo Y., Gross S.P., Welte M.A.;
"The lipid-droplet proteome reveals that droplets are a protein-
storage depot.";
Curr. Biol. 16:1783-1795(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY
20-HYDROXYECDYSONE.
PubMed=17924685; DOI=10.1021/pr0705183;
Sun Y., An S., Henrich V.C., Sun X., Song Q.;
"Proteomic identification of PKC-mediated expression of 20E-induced
protein in Drosophila melanogaster.";
J. Proteome Res. 6:4478-4488(2007).
-!- FUNCTION: May function in mitochondrial tRNA maturation. Catalyzes
the beta-oxidation at position 17 of androgens and estrogens, and
has 3-alpha-hydroxysteroid dehydrogenase activity with
androsterone. Catalyzes the third step in the beta-oxidation of
fatty acids. Carries out oxidative conversions of 7-beta-
hydroxylated bile acids. Also exhibits 20-beta-OH and 21-OH
dehydrogenase activities with C21 steroids. Required for cell
survival during embryonic development. May play a role in germline
formation. {ECO:0000269|PubMed:12917011,
ECO:0000269|PubMed:9585418}.
-!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
+ NADH. {ECO:0000269|PubMed:12917011}.
-!- CATALYTIC ACTIVITY: (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA +
NAD(+) = 2-methylacetoacetyl-CoA + NADH.
{ECO:0000269|PubMed:12917011}.
-!- CATALYTIC ACTIVITY: Testosterone + NAD(P)(+) = androst-4-ene-3,17-
dione + NAD(P)H. {ECO:0000269|PubMed:12917011}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=33.7 uM for acetoacetyl-CoA (in the presence of 0.2 mM NADH,
at pH 6.4 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
KM=101 uM for beta-hydroxybutyryl-CoA (in the presence of 1 mM
NAD, at pH 9.3 and 25 degrees Celsius)
{ECO:0000269|PubMed:12917011};
KM=37.3 uM for androsterone (in the presence of 1 mM NAD, at pH
9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
KM=12.3 uM for 5-alpha-dihydrotestosterone (in the presence of
0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)
{ECO:0000269|PubMed:12917011};
KM=11.1 uM for 17-beta-estradiol (in the presence of 0.2 mM
NADH, at pH 9.3 and 25 degrees Celsius)
{ECO:0000269|PubMed:12917011};
KM=9 uM for 5-alpha-pregnan-20-beta-ol-3-one (in the presence of
1 mM NAD, at pH 9.3 and 25 degrees Celsius)
{ECO:0000269|PubMed:12917011};
KM=3 uM for isoursodeoxycholic acid (in the presence of 1 mM
NAD, at pH 9.3 and 25 degrees Celsius)
{ECO:0000269|PubMed:12917011};
KM=32.5 uM for NADH (in the presence of acetoacetyl-CoA, at pH
7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
KM=64.4 uM for NAD (in the presence of beta-hydroxybutyryl-CoA,
at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
KM=124 uM for NAD (in the presence of aldosterone, at pH 9.3 and
25 degrees Celsius) {ECO:0000269|PubMed:12917011};
pH dependence:
Optimum pH is 9.3 for the dehydrogenase reaction, and 6.4 for
the reductase reaction. {ECO:0000269|PubMed:12917011};
-!- SUBUNIT: Multimer. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Note=Localizes
to the lipid droplet fraction in early embryos.
{ECO:0000269|PubMed:16979555}.
-!- TISSUE SPECIFICITY: Found in many tissues including CNS, imaginal
disks and salivary glands. Highest expression in both embryonic
gonadal primordia and mature ovaries and testes.
{ECO:0000269|PubMed:9585418}.
-!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development.
In adults, expression is higher in females than in males.
{ECO:0000269|PubMed:9585418}.
-!- INDUCTION: By 20-hydroxyecdysone. {ECO:0000269|PubMed:17924685}.
-!- DISRUPTION PHENOTYPE: Embryonic and pupal lethal. Male mutants
show small testes and degenerating spermatocytes with a large
accumulation of small fat-containing vesicles in the cytoplasm and
almost no mitochondria. Null mutant photoreceptors fail to
differentiate normally, are unable to form proper rhabdomeres and
present smaller mitochondria with fewer, but swollen crestae, than
wild-type cells. {ECO:0000269|PubMed:9585418}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AET07646.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={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; Y15102; CAA75377.1; -; mRNA.
EMBL; AE014298; AAF48797.1; -; Genomic_DNA.
EMBL; AY121672; AAM51999.1; -; mRNA.
EMBL; BT029045; ABJ16978.1; -; mRNA.
EMBL; BT132763; AET07646.1; ALT_INIT; mRNA.
RefSeq; NP_523396.1; NM_078672.5.
UniGene; Dm.7957; -.
ProteinModelPortal; O18404; -.
SMR; O18404; -.
BioGrid; 59109; 78.
DIP; DIP-17092N; -.
IntAct; O18404; 6.
STRING; 7227.FBpp0074285; -.
SwissLipids; SLP:000000795; -.
PaxDb; O18404; -.
PRIDE; O18404; -.
EnsemblMetazoa; FBtr0074511; FBpp0074285; FBgn0021765.
GeneID; 32789; -.
KEGG; dme:Dmel_CG7113; -.
CTD; 32789; -.
FlyBase; FBgn0021765; scu.
eggNOG; KOG1199; Eukaryota.
eggNOG; ENOG410XNNW; LUCA.
GeneTree; ENSGT00920000148965; -.
InParanoid; O18404; -.
KO; K08683; -.
OMA; LMGLVNC; -.
OrthoDB; EOG091G0G9O; -.
PhylomeDB; O18404; -.
Reactome; R-DME-70895; Branched-chain amino acid catabolism.
ChiTaRS; scu; fly.
GenomeRNAi; 32789; -.
PRO; PR:O18404; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0021765; Expressed in 37 organ(s), highest expression level in arthropod fat body.
ExpressionAtlas; O18404; baseline and differential.
Genevisible; O18404; DM.
GO; GO:0005829; C:cytosol; NAS:FlyBase.
GO; GO:0030678; C:mitochondrial ribonuclease P complex; IDA:FlyBase.
GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
GO; GO:0047015; F:3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0047022; F:7-beta-hydroxysteroid dehydrogenase (NADP+) activity; IDA:FlyBase.
GO; GO:0018454; F:acetoacetyl-CoA reductase activity; IDA:FlyBase.
GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:FlyBase.
GO; GO:0016229; F:steroid dehydrogenase activity; IDA:FlyBase.
GO; GO:0047035; F:testosterone dehydrogenase (NAD+) activity; IDA:FlyBase.
GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; IEA:UniProtKB-EC.
GO; GO:0006637; P:acyl-CoA metabolic process; IDA:FlyBase.
GO; GO:0008209; P:androgen metabolic process; IDA:FlyBase.
GO; GO:0008205; P:ecdysone metabolic process; IDA:FlyBase.
GO; GO:0008210; P:estrogen metabolic process; IDA:FlyBase.
GO; GO:0006631; P:fatty acid metabolic process; IDA:FlyBase.
GO; GO:0090646; P:mitochondrial tRNA processing; IMP:FlyBase.
GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
GO; GO:0008202; P:steroid metabolic process; IDA:FlyBase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
Complete proteome; Mitochondrion; NAD; Oxidoreductase;
Reference proteome; tRNA processing.
CHAIN 1 255 3-hydroxyacyl-CoA dehydrogenase type-2.
/FTId=PRO_0000054813.
NP_BIND 6 31 NAD. {ECO:0000250}.
ACT_SITE 162 162 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 149 149 Substrate. {ECO:0000250}.
MUTAGEN 33 33 L->Q: Lethal allele.
{ECO:0000269|PubMed:9585418}.
MUTAGEN 120 120 F->I: Lethal allele.
{ECO:0000269|PubMed:9585418}.
CONFLICT 134 134 E -> K (in Ref. 4; AAM51999).
{ECO:0000305}.
SEQUENCE 255 AA; 26905 MW; F58690643FA0FD03 CRC64;
MIKNAVSLVT GGASGLGRAT AERLAKQGAS VILADLPSSK GNEVAKELGD KVVFVPVDVT
SEKDVSAALQ TAKDKFGRLD LTVNCAGTAT AVKTFNFNKN VAHRLEDFQR VININTVGTF
NVIRLSAGLM GANEPNQDGQ RGVIVNTASV AAFDGQIGQA AYSASKAAVV GMTLPIARDL
STQGIRICTI APGLFNTPML AALPEKVRTF LAKSIPFPQR LGEPSEYAHL VQAIYENPLL
NGEVIRIDGA LRMMP


Related products :

Catalog number Product name Quantity
20-272-190169 ERAB - Mitochondrial Marker - Mouse monoclonal [10D12] to ERAB - Mitochondrial Marker; EC 1.1.1.35; 3-hydroxyacyl-CoA dehydrogenase type II; Type II HADH; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; 0.1 ml
20-272-190170 ERAB - Mitochondrial Marker - Mouse monoclonal [5F3] to ERAB - Mitochondrial Marker; EC 1.1.1.35; 3-hydroxyacyl-CoA dehydrogenase type II; Type II HADH; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase; EC 0.1 ml
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
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
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
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
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
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
EIAAB11108 17-beta-HSD 3,17-beta-hydroxysteroid dehydrogenase type 3,Edh17b3,Hsd17b3,Rat,Rattus norvegicus,Testicular 17-beta-hydroxysteroid dehydrogenase,Testosterone 17-beta-dehydrogenase 3
EIAAB11107 17-beta-HSD 3,17-beta-hydroxysteroid dehydrogenase type 3,Edh17b3,Hsd17b3,Mouse,Mus musculus,Testicular 17-beta-hydroxysteroid dehydrogenase,Testosterone 17-beta-dehydrogenase 3
15-288-22852 Corticosteroid 11-beta-dehydrogenase isozyme 2 - EC 1.1.1.-; 11-DH2; 11-beta-hydroxysteroid dehydrogenase type 2; 11-beta-HSD2; NAD-dependent 11-beta-hydroxysteroid dehydrogenase Polyclonal 0.05 mg
15-288-22852 Corticosteroid 11-beta-dehydrogenase isozyme 2 - EC 1.1.1.-; 11-DH2; 11-beta-hydroxysteroid dehydrogenase type 2; 11-beta-HSD2; NAD-dependent 11-beta-hydroxysteroid dehydrogenase Polyclonal 0.1 mg
EIAAB11104 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,Edh17b2,Estradiol 17-beta-dehydrogenase 2,Hsd17b2,Mouse,Mus musculus,Testosterone 17-beta-dehydrogenase
EIAAB11103 17-beta-HSD 2,17-beta-hydroxysteroid dehydrogenase type 2,Edh17b2,Estradiol 17-beta-dehydrogenase 2,Hsd17b2,Rat,Rattus norvegicus,Testosterone 17-beta-dehydrogenase
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
EIAAB11146 11-beta-HSD3,11-beta-hydroxysteroid dehydrogenase type 3,11-DH3,Homo sapiens,HSD11B1L,HSD3,Human,Hydroxysteroid 11-beta-dehydrogenase 1-like protein,SCDR10,Short-chain dehydrogenase_reductase 10
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
EIAAB11117 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Estradiol 17-beta-dehydrogenase 8,Hsd17b8,Rat,Rattus norvegicus,Testosterone 17-beta-dehydrogenase 8
CSB-EL010117RA Rat Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial(HADH) ELISA kit 96T
EIAAB11147 11-beta-HSD3,11-beta-hydroxysteroid dehydrogenase type 3,11-DH3,Bos taurus,Bovine,HSD11B1L,HSD3,Hydroxysteroid 11-beta-dehydrogenase 1-like protein
15-288-22261 Short chain 3-hydroxyacyl-CoA dehydrogenase. mitochondrial - EC 1.1.1.35; HCDH; Medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase Polyclonal 0.05 mg
15-288-22261 Short chain 3-hydroxyacyl-CoA dehydrogenase. mitochondrial - EC 1.1.1.35; HCDH; Medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase Polyclonal 0.1 mg
CSB-EL010117PI Pig Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial(HADH) ELISA kit SpeciesPig 96T
CSB-EL010117HU Human Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial(HADH) ELISA kit 96T
CSB-EL010117MO Mouse Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial(HADH) ELISA kit 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





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: 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

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