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Aldo-keto reductase family 1 member C21 (EC 1.1.1.-) (17-alpha-hydroxysteroid dehydrogenase) (17-alpha-HSD) (3(or 17)-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.209) (3-alpha-hydroxysteroid dehydrogenase) (Dihydrodiol dehydrogenase type 1) (DD1) (Dihydrodiol dehydrogenase type 3) (DD3)

 AK1CL_MOUSE             Reviewed;         323 AA.
Q91WR5; Q6P8V0; Q9CX32;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 2.
12-SEP-2018, entry version 119.
RecName: Full=Aldo-keto reductase family 1 member C21;
EC=1.1.1.-;
AltName: Full=17-alpha-hydroxysteroid dehydrogenase;
Short=17-alpha-HSD;
AltName: Full=3(or 17)-alpha-hydroxysteroid dehydrogenase;
EC=1.1.1.209;
AltName: Full=3-alpha-hydroxysteroid dehydrogenase;
AltName: Full=Dihydrodiol dehydrogenase type 1;
Short=DD1;
AltName: Full=Dihydrodiol dehydrogenase type 3;
Short=DD3;
Name=Akr1c21;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, SUBUNIT,
ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
SPECIFICITY.
STRAIN=ICR; TISSUE=Kidney;
PubMed=15577209; DOI=10.1248/bpb.27.1939;
Ishikura S., Usami N., Nakajima S., Shiraishi H., El-Kabbani O.,
Hara A.;
"Characterization of two isoforms of mouse 3(17)alpha-hydroxysteroid
dehydrogenases of the aldo-keto reductase family.";
Biol. Pharm. Bull. 27:1939-1945(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=16018803; DOI=10.1186/1471-2091-6-12;
Bellemare V., Faucher F., Breton R., Luu-The V.;
"Characterization of 17alpha-hydroxysteroid dehydrogenase activity
(17-alpha-HSD) and its involvement in the biosynthesis of
epitestosterone.";
BMC Biochem. 6:12-12(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION,
AND MUTAGENESIS OF ALA-24.
PubMed=17034817; DOI=10.1016/j.jmb.2006.09.030;
Faucher F., Pereira de Jesus-Tran K., Cantin L., Luu-The V.,
Labrie F., Breton R.;
"Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase
(apoenzyme and enzyme-NADP(H) binary complex): identification of
molecular determinants responsible for the unique 17alpha-reductive
activity of this enzyme.";
J. Mol. Biol. 364:747-763(2006).
[7]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH NADP.
PubMed=17909281; DOI=10.1107/S1744309107040985;
Dhagat U., Carbone V., Chung R.P.-T., Schulze-Briese C., Endo S.,
Hara A., El-Kabbani O.;
"Structure of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21)
holoenzyme from an orthorhombic crystal form: an insight into the
bifunctionality of the enzyme.";
Acta Crystallogr. F 63:825-830(2007).
[8]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 6-323 IN COMPLEX WITH
EPITESTOSTERONE, MUTAGENESIS OF LYS-31, BIOPHYSICOCHEMICAL PROPERTIES,
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=17442338; DOI=10.1016/j.jmb.2007.03.058;
Faucher F., Cantin L., Pereira de Jesus-Tran K., Lemieux M.,
Luu-The V., Labrie F., Breton R.;
"Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids
differently from other aldo-keto reductases: identification and
characterization of amino acid residues critical for substrate
binding.";
J. Mol. Biol. 369:525-540(2007).
[9]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH NADP.
PubMed=19237748; DOI=10.1107/S0907444908044028;
Dhagat U., Endo S., Mamiya H., Hara A., El-Kabbani O.;
"Structure of the G225P/G226P mutant of mouse 3(17)alpha-
hydroxysteroid dehydrogenase (AKR1C21) ternary complex: implications
for the binding of inhibitor and substrate.";
Acta Crystallogr. D 65:257-265(2009).
[10]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT ASP-224, CATALYTIC
ACTIVITY, FUNCTION, AND MUTAGENESIS OF GLN-222 AND TYR-224.
PubMed=20124700; DOI=10.1107/S0907444909051464;
Dhagat U., Endo S., Mamiya H., Hara A., El-Kabbani O.;
"Studies on a Tyr residue critical for the binding of coenzyme and
substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21):
structure of the Y224D mutant enzyme.";
Acta Crystallogr. D 66:198-204(2010).
-!- FUNCTION: NADP-dependent 17-alpha-hydroxysteroid dehydrogenase
that converts 5-alpha-androstane-3,17-dione into androsterone. Has
lower 3-alpha-hydroxysteroid dehydrogenase activity. Has broad
substrate specificity and acts on various 17-alpha-
hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3-
ketosteroids. Reduction of keto groups is strictly
stereoselective. Reduction of 17-ketosteroids yields only 17-
alpha-hydroxysteroids. Likewise, reduction of 3-ketosteroids
yields only 3-alpha-hydroxysteroids. {ECO:0000269|PubMed:15577209,
ECO:0000269|PubMed:16018803, ECO:0000269|PubMed:17034817,
ECO:0000269|PubMed:17442338, ECO:0000269|PubMed:20124700}.
-!- CATALYTIC ACTIVITY: Androsterone + NAD(P)(+) = 5-alpha-androstane-
3,17-dione + NAD(P)H. {ECO:0000269|PubMed:15577209,
ECO:0000269|PubMed:17442338, ECO:0000269|PubMed:20124700}.
-!- ACTIVITY REGULATION: Inhibited by high concentrations of
substrate. {ECO:0000269|PubMed:15577209}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.8 uM for NADP {ECO:0000269|PubMed:15577209,
ECO:0000269|PubMed:17442338};
KM=19 uM for androstenedione {ECO:0000269|PubMed:15577209,
ECO:0000269|PubMed:17442338};
KM=0.5 uM for 5-beta-pregnane-3-alpha,20-alpha-diol
{ECO:0000269|PubMed:15577209, ECO:0000269|PubMed:17442338};
KM=0.5 uM for 5-beta-pregnane-3,20-dione
{ECO:0000269|PubMed:15577209, ECO:0000269|PubMed:17442338};
KM=0.6 uM for epitestosterone {ECO:0000269|PubMed:15577209,
ECO:0000269|PubMed:17442338};
KM=0.3 uM for androst-4-ene-3,17-dione
{ECO:0000269|PubMed:15577209, ECO:0000269|PubMed:17442338};
pH dependence:
Optimum pH is 10.0. {ECO:0000269|PubMed:15577209,
ECO:0000269|PubMed:17442338};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15577209,
ECO:0000269|PubMed:17034817, ECO:0000269|PubMed:17442338,
ECO:0000269|PubMed:17909281, ECO:0000269|PubMed:19237748}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in kidney and brain.
{ECO:0000269|PubMed:15577209, ECO:0000269|PubMed:16018803}.
-!- SIMILARITY: Belongs to the aldo/keto reductase family.
{ECO:0000305}.
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EMBL; AB178898; BAD18929.1; -; mRNA.
EMBL; AY742217; AAW65159.1; -; mRNA.
EMBL; AK020439; BAB32101.1; -; mRNA.
EMBL; BC013531; AAH13531.1; -; mRNA.
EMBL; BC061057; AAH61057.1; -; mRNA.
EMBL; BC091761; AAH91761.1; -; mRNA.
CCDS; CCDS26225.1; -.
RefSeq; NP_084177.2; NM_029901.2.
UniGene; Mm.27085; -.
PDB; 2HE5; X-ray; 2.90 A; A/B/C/D=1-323.
PDB; 2HE8; X-ray; 1.90 A; A/B=1-323.
PDB; 2HEJ; X-ray; 1.35 A; A/B=1-323.
PDB; 2IPF; X-ray; 1.85 A; A/B=6-323.
PDB; 2IPG; X-ray; 1.90 A; A/B=5-323.
PDB; 2P5N; X-ray; 1.80 A; A/B=1-323.
PDB; 3CV6; X-ray; 2.10 A; A/B=1-323.
PDB; 3FJN; X-ray; 2.30 A; A/B=1-323.
PDBsum; 2HE5; -.
PDBsum; 2HE8; -.
PDBsum; 2HEJ; -.
PDBsum; 2IPF; -.
PDBsum; 2IPG; -.
PDBsum; 2P5N; -.
PDBsum; 3CV6; -.
PDBsum; 3FJN; -.
DisProt; DP00690; -.
ProteinModelPortal; Q91WR5; -.
SMR; Q91WR5; -.
STRING; 10090.ENSMUSP00000021628; -.
BindingDB; Q91WR5; -.
ChEMBL; CHEMBL1075270; -.
iPTMnet; Q91WR5; -.
PhosphoSitePlus; Q91WR5; -.
MaxQB; Q91WR5; -.
PaxDb; Q91WR5; -.
PeptideAtlas; Q91WR5; -.
PRIDE; Q91WR5; -.
Ensembl; ENSMUST00000021628; ENSMUSP00000021628; ENSMUSG00000021207.
GeneID; 77337; -.
KEGG; mmu:77337; -.
UCSC; uc007pjr.1; mouse.
CTD; 77337; -.
MGI; MGI:1924587; Akr1c21.
eggNOG; KOG1577; Eukaryota.
eggNOG; COG0656; LUCA.
GeneTree; ENSGT00760000119041; -.
HOGENOM; HOG000250272; -.
HOVERGEN; HBG000020; -.
InParanoid; Q91WR5; -.
OMA; QIAMERG; -.
OrthoDB; EOG091G0D69; -.
PhylomeDB; Q91WR5; -.
TreeFam; TF106492; -.
BRENDA; 1.1.1.148; 3474.
BRENDA; 1.1.1.209; 3474.
BRENDA; 1.1.1.50; 3474.
Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-MMU-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
Reactome; R-MMU-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-MMU-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
Reactome; R-MMU-5365859; RA biosynthesis pathway.
Reactome; R-MMU-975634; Retinoid metabolism and transport.
SABIO-RK; Q91WR5; -.
EvolutionaryTrace; Q91WR5; -.
PRO; PR:Q91WR5; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021207; Expressed in 40 organ(s), highest expression level in kidney.
CleanEx; MM_AKR1C21; -.
ExpressionAtlas; Q91WR5; baseline and differential.
Genevisible; Q91WR5; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; IMP:CAFA.
GO; GO:0072555; F:17-beta-ketosteroid reductase activity; IMP:CAFA.
GO; GO:0047024; F:5alpha-androstane-3beta,17beta-diol dehydrogenase activity; IMP:CAFA.
GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; ISO:MGI.
GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISA:MGI.
GO; GO:0047042; F:androsterone dehydrogenase (B-specific) activity; ISO:MGI.
GO; GO:0047023; F:androsterone dehydrogenase activity; IDA:UniProtKB.
GO; GO:0032052; F:bile acid binding; ISO:MGI.
GO; GO:0031406; F:carboxylic acid binding; ISO:MGI.
GO; GO:0047086; F:ketosteroid monooxygenase activity; ISO:MGI.
GO; GO:1902121; F:lithocholic acid binding; IMP:CAFA.
GO; GO:0070401; F:NADP+ binding; IMP:CAFA.
GO; GO:0070402; F:NADPH binding; IMP:CAFA.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; ISO:MGI.
GO; GO:0018636; F:phenanthrene 9,10-monooxygenase activity; ISO:MGI.
GO; GO:0005496; F:steroid binding; IMP:CAFA.
GO; GO:0033764; F:steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:MGI.
GO; GO:0047115; F:trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity; ISO:MGI.
GO; GO:0055114; P:oxidation-reduction process; IMP:CAFA.
GO; GO:0006694; P:steroid biosynthetic process; ISA:MGI.
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; PS00062; ALDOKETO_REDUCTASE_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Lipid metabolism; NADP;
Oxidoreductase; Reference proteome; Steroid metabolism.
CHAIN 1 323 Aldo-keto reductase family 1 member C21.
/FTId=PRO_0000326222.
NP_BIND 20 24 NADP. {ECO:0000269|PubMed:17034817,
ECO:0000269|PubMed:17909281,
ECO:0000269|PubMed:19237748}.
NP_BIND 166 167 NADP. {ECO:0000269|PubMed:17034817,
ECO:0000269|PubMed:17909281,
ECO:0000269|PubMed:19237748}.
NP_BIND 216 224 NADP. {ECO:0000269|PubMed:17034817,
ECO:0000269|PubMed:17909281,
ECO:0000269|PubMed:19237748}.
NP_BIND 270 280 NADP. {ECO:0000269|PubMed:17034817,
ECO:0000269|PubMed:17909281,
ECO:0000269|PubMed:19237748}.
ACT_SITE 55 55 Proton donor.
BINDING 31 31 Substrate.
BINDING 50 50 NADP. {ECO:0000269|PubMed:17034817,
ECO:0000269|PubMed:17909281,
ECO:0000269|PubMed:19237748}.
BINDING 117 117 Substrate.
BINDING 190 190 NADP. {ECO:0000269|PubMed:17034817,
ECO:0000269|PubMed:17909281,
ECO:0000269|PubMed:19237748}.
SITE 84 84 Lowers pKa of active site Tyr.
{ECO:0000250}.
MUTAGEN 24 24 A->Y: Reduces enzyme activity and
affinity for substrate. Alters the
stereospecificity, so that
androstenedione is converted to
testosterone.
{ECO:0000269|PubMed:17034817}.
MUTAGEN 31 31 K->A: No effect on affinity for
androstenedione. Slight increase of
catalytic activity.
{ECO:0000269|PubMed:17442338}.
MUTAGEN 222 222 Q->N: Decreases affinity for NADP.
Changes enzyme activity, leading to the
production of testosterone and
concomitantly reducing the production of
epi-testosterone.
{ECO:0000269|PubMed:20124700}.
MUTAGEN 224 224 Y->D: Decreases affinity for NADP.
Changes enzyme activity, leading to the
production of testosterone and
concomitantly reducing the production of
epi-testosterone.
{ECO:0000269|PubMed:20124700}.
MUTAGEN 224 224 Y->F: No effect on enzyme activity.
Decreases affinity for NADP.
{ECO:0000269|PubMed:20124700}.
CONFLICT 27 27 L -> V (in Ref. 1; BAD18929 and 4;
AAH13531/AAH91761). {ECO:0000305}.
CONFLICT 60 60 H -> R (in Ref. 1; BAD18929 and 4;
AAH13531/AAH91761). {ECO:0000305}.
CONFLICT 91 91 H -> R (in Ref. 1; BAD18929 and 4;
AAH13531/AAH91761). {ECO:0000305}.
CONFLICT 100 100 E -> V (in Ref. 1; BAD18929 and 4;
AAH13531/AAH91761). {ECO:0000305}.
CONFLICT 170 170 Y -> S (in Ref. 1; BAD18929 and 4;
AAH13531/AAH91761). {ECO:0000305}.
CONFLICT 294 294 K -> E (in Ref. 4; AAH61057).
{ECO:0000305}.
STRAND 7 9 {ECO:0000244|PDB:2HEJ}.
STRAND 15 22 {ECO:0000244|PDB:2HEJ}.
STRAND 27 29 {ECO:0000244|PDB:2HE5}.
HELIX 33 44 {ECO:0000244|PDB:2HEJ}.
STRAND 48 50 {ECO:0000244|PDB:2HEJ}.
HELIX 53 55 {ECO:0000244|PDB:2HEJ}.
HELIX 58 70 {ECO:0000244|PDB:2HEJ}.
HELIX 76 78 {ECO:0000244|PDB:2HEJ}.
STRAND 80 85 {ECO:0000244|PDB:2HEJ}.
HELIX 87 89 {ECO:0000244|PDB:2HEJ}.
TURN 92 94 {ECO:0000244|PDB:2HEJ}.
HELIX 95 106 {ECO:0000244|PDB:2HEJ}.
STRAND 111 117 {ECO:0000244|PDB:2HEJ}.
STRAND 121 123 {ECO:0000244|PDB:3FJN}.
STRAND 125 129 {ECO:0000244|PDB:3FJN}.
HELIX 144 156 {ECO:0000244|PDB:2HEJ}.
STRAND 159 167 {ECO:0000244|PDB:2HEJ}.
HELIX 170 177 {ECO:0000244|PDB:2HEJ}.
STRAND 187 192 {ECO:0000244|PDB:2HEJ}.
STRAND 194 197 {ECO:0000244|PDB:3CV6}.
HELIX 200 208 {ECO:0000244|PDB:2HEJ}.
STRAND 212 216 {ECO:0000244|PDB:2HEJ}.
TURN 225 227 {ECO:0000244|PDB:2HEJ}.
HELIX 228 231 {ECO:0000244|PDB:3FJN}.
HELIX 235 237 {ECO:0000244|PDB:2HEJ}.
HELIX 239 248 {ECO:0000244|PDB:2HEJ}.
HELIX 252 261 {ECO:0000244|PDB:2HEJ}.
TURN 262 264 {ECO:0000244|PDB:2HEJ}.
STRAND 266 269 {ECO:0000244|PDB:2HEJ}.
HELIX 274 280 {ECO:0000244|PDB:2HEJ}.
HELIX 281 285 {ECO:0000244|PDB:2HEJ}.
HELIX 290 297 {ECO:0000244|PDB:2HEJ}.
HELIX 309 311 {ECO:0000244|PDB:2HEJ}.
STRAND 318 321 {ECO:0000244|PDB:2P5N}.
SEQUENCE 323 AA; 36877 MW; 0D598A0559EFBF11 CRC64;
MNSKCHCVIL NDGNFIPVLG FGTALPLECP KSKAKELTKI AIDAGFHHFD SASVYNTEDH
VGEAIRSKIA DGTVRREDIF YTSKVWCTSL HPELVRASLE RSLQKLQFDY VDLYLIHYPM
ALKPGEENFP VDEHGKLIFD RVDLCATWEA MEKCKDAGLT KSIGVSNFNY RQLEMILNKP
GLKYKPVCNQ VECHPYLNQM KLLDFCKSKD IVLVAYGVLG TQRYGGWVDQ NSPVLLDEPV
LGSMAKKYNR TPALIALRYQ LQRGIVVLNT SLKEERIKEN MQVFEFQLSS EDMKVLDGLN
RNMRYIPAAI FKGHPNWPFL DEY


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Catalog number Product name Quantity
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AKR1E2 AKR1C4 Gene aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol dehydrogenase 4)
AKR1C4 AKR1C2 Gene aldo-keto reductase family 1, member C2 (dihydrodiol dehydrogenase 2; bile acid binding protein; 3-alpha hydroxysteroid dehydrogenase, type III)
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
CSB-PA001545GA01HU Rabbit anti-human aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol dehydrogenase 4) polyclonal Antibody Primary antibody Host: 50ul
CSB-PA001545GA01HU Rabbit anti-human aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol dehydrogenase 4) polyclonal Antibody Primary antibody Host: 150ul
CSB-EL001545HU Human aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol dehydrogenase 4) (AKR1C4) ELISA kit, Species Human, Sample Type serum, p 96T
CSB-EL001543HU Human aldo-keto reductase family 1, member C2 (dihydrodiol dehydrogenase 2; bile acid binding protein; 3-alpha hydroxysteroid dehydrogenase, type III) (AKR1C2) ELISA kit, Species Human, Sample Type se 96T
201-20-0259 AKR1C3{aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)}rabbit.pAb 0.1ml
AKR1D1 AKR1C3 Gene aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II)
GS-0063a aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II) primary antibody, Host: Rabbit 200ul
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
CSB-EL001544HU Human aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II) (AKR1C3) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-PA001544GA01HU Rabbit anti-human aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA001544GA01HU Rabbit anti-human aldo-keto reductase family 1, member C3 (3-alpha hydroxysteroid dehydrogenase, type II) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
EIAAB11263 3-alpha-HSD,3-alpha-hydroxysteroid dehydrogenase,Akr1c9,Hydroxyprostaglandin dehydrogenase,Rat,Rattus norvegicus
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
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
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
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
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


 

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