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Very-long-chain 3-oxoacyl-CoA reductase (EC 1.1.1.330) (17-beta-hydroxysteroid dehydrogenase 12) (17-beta-HSD 12) (3-ketoacyl-CoA reductase) (KAR) (Estradiol 17-beta-dehydrogenase 12) (EC 1.1.1.62) (Short chain dehydrogenase/reductase family 12C member 1)

 DHB12_HUMAN             Reviewed;         312 AA.
Q53GQ0; A8K9B0; D3DR23; Q96EA9; Q96JU2; Q9Y6G8;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 2.
25-OCT-2017, entry version 130.
RecName: Full=Very-long-chain 3-oxoacyl-CoA reductase {ECO:0000305};
EC=1.1.1.330 {ECO:0000269|PubMed:12482854};
AltName: Full=17-beta-hydroxysteroid dehydrogenase 12 {ECO:0000303|PubMed:16166196};
Short=17-beta-HSD 12 {ECO:0000303|PubMed:16166196};
AltName: Full=3-ketoacyl-CoA reductase {ECO:0000303|PubMed:12482854};
Short=KAR {ECO:0000303|PubMed:12482854};
AltName: Full=Estradiol 17-beta-dehydrogenase 12 {ECO:0000303|PubMed:16166196};
EC=1.1.1.62 {ECO:0000269|PubMed:16166196};
AltName: Full=Short chain dehydrogenase/reductase family 12C member 1;
Name=HSD17B12 {ECO:0000312|HGNC:HGNC:18646}; Synonyms=SDR12C1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Liu T., Zhang J., Fu G., Zhang Q., Ye M., Zhou J., Wu J., Shen Y.,
Yu M., Chen S., Mao M., Chen Z.;
"Human steroid dehydrogenase homologue, complete cds.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-280.
TISSUE=Liver, Placenta, Thymus, and Thyroid;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-280.
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-280.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and 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).
[7]
PROTEIN SEQUENCE OF 26-35; 65-72; 104-117; 157-179 AND 207-221, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[8]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=12482854; DOI=10.1074/jbc.M211684200;
Moon Y.-A., Horton J.D.;
"Identification of two mammalian reductases involved in the two-carbon
fatty acyl elongation cascade.";
J. Biol. Chem. 278:7335-7343(2003).
[9]
TISSUE SPECIFICITY.
PubMed=16113833; DOI=10.1267/THRO05020412;
Gnatenko D.V., Cupit L.D., Huang E.C., Dhundale A., Perrotta P.L.,
Bahou W.F.;
"Platelets express steroidogenic 17beta-hydroxysteroid dehydrogenases.
Distinct profiles predict the essential thrombocythemic phenotype.";
Thromb. Haemost. 94:412-421(2005).
[10]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES,
TISSUE SPECIFICITY, AND MUTAGENESIS OF VAL-196 AND PHE-234.
PubMed=16166196; DOI=10.1210/me.2005-0058;
Luu-The V., Tremblay P., Labrie F.;
"Characterization of type 12 17beta-hydroxysteroid dehydrogenase, an
isoform of type 3 17beta-hydroxysteroid dehydrogenase responsible for
estradiol formation in women.";
Mol. Endocrinol. 20:437-443(2006).
[11]
INTERACTION WITH ELOVL1 AND LASS2.
PubMed=20937905; DOI=10.1073/pnas.1005572107;
Ohno Y., Suto S., Yamanaka M., Mizutani Y., Mitsutake S., Igarashi Y.,
Sassa T., Kihara A.;
"ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingolipid
synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 107:18439-18444(2010).
[12]
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).
[13]
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).
[14]
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).
-!- FUNCTION: Catalyzes the second of the four reactions of the long-
chain fatty acids elongation cycle. This endoplasmic reticulum-
bound enzymatic process, allows the addition of two carbons to the
chain of long- and very long-chain fatty acids/VLCFAs per cycle.
This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-
ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid
elongation. Thereby, it may participate in the production of
VLCFAs of different chain lengths that are involved in multiple
biological processes as precursors of membrane lipids and lipid
mediators. May also catalyze the transformation of estrone (E1)
into estradiol (E2) and play a role in estrogen formation.
{ECO:0000269|PubMed:12482854, ECO:0000269|PubMed:16166196}.
-!- CATALYTIC ACTIVITY: A very-long-chain (3R)-3-hydroxyacyl-CoA +
NADP(+) = a very-long-chain 3-oxoacyl-CoA + NADPH.
{ECO:0000269|PubMed:12482854}.
-!- CATALYTIC ACTIVITY: 17-beta-estradiol + NAD(P)(+) = estrone +
NAD(P)H. {ECO:0000269|PubMed:16166196}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.5 uM for estrone {ECO:0000269|PubMed:16166196};
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
{ECO:0000269|PubMed:12482854}.
-!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
{ECO:0000269|PubMed:16166196}.
-!- SUBUNIT: Interacts with ELOVL1 and LASS2.
{ECO:0000269|PubMed:20937905}.
-!- INTERACTION:
Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-2963255, EBI-6863754;
Q9UMX0:UBQLN1; NbExp=3; IntAct=EBI-2963255, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-2963255, EBI-10173939;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12482854}; Multi-pass membrane protein
{ECO:0000269|PubMed:12482854}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q53GQ0-1; Sequence=Displayed;
Name=2;
IsoId=Q53GQ0-2; Sequence=VSP_056380, VSP_056381;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in most tissues tested. Highly
expressed in the ovary and mammary. Expressed in platelets.
{ECO:0000269|PubMed:12482854, ECO:0000269|PubMed:16113833,
ECO:0000269|PubMed:16166196}.
-!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
localization for type I membrane proteins. {ECO:0000250}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. 17-beta-HSD 3 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AK027882; Type=Frameshift; Positions=92; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF078850; AAD44482.1; -; mRNA.
EMBL; AK027882; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK074952; BAG52039.1; -; mRNA.
EMBL; AK075216; BAG52086.1; -; mRNA.
EMBL; AK222881; BAD96601.1; -; mRNA.
EMBL; AK292625; BAF85314.1; -; mRNA.
EMBL; AC023085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68082.1; -; Genomic_DNA.
EMBL; CH471064; EAW68087.1; -; Genomic_DNA.
EMBL; CH471064; EAW68088.1; -; Genomic_DNA.
EMBL; BC012043; AAH12043.1; -; mRNA.
EMBL; BC012536; AAH12536.1; -; mRNA.
CCDS; CCDS7905.1; -. [Q53GQ0-1]
RefSeq; NP_057226.1; NM_016142.2. [Q53GQ0-1]
UniGene; Hs.132513; -.
ProteinModelPortal; Q53GQ0; -.
SMR; Q53GQ0; -.
BioGrid; 119328; 44.
IntAct; Q53GQ0; 18.
STRING; 9606.ENSP00000278353; -.
ChEMBL; CHEMBL5998; -.
SwissLipids; SLP:000000433; -.
iPTMnet; Q53GQ0; -.
PhosphoSitePlus; Q53GQ0; -.
SwissPalm; Q53GQ0; -.
BioMuta; HSD17B12; -.
DMDM; 158931120; -.
EPD; Q53GQ0; -.
MaxQB; Q53GQ0; -.
PaxDb; Q53GQ0; -.
PeptideAtlas; Q53GQ0; -.
PRIDE; Q53GQ0; -.
DNASU; 51144; -.
Ensembl; ENST00000278353; ENSP00000278353; ENSG00000149084. [Q53GQ0-1]
Ensembl; ENST00000395700; ENSP00000379052; ENSG00000149084. [Q53GQ0-2]
GeneID; 51144; -.
KEGG; hsa:51144; -.
UCSC; uc001mxq.5; human. [Q53GQ0-1]
CTD; 51144; -.
DisGeNET; 51144; -.
EuPathDB; HostDB:ENSG00000149084.11; -.
GeneCards; HSD17B12; -.
HGNC; HGNC:18646; HSD17B12.
HPA; HPA016427; -.
MIM; 609574; gene.
neXtProt; NX_Q53GQ0; -.
OpenTargets; ENSG00000149084; -.
PharmGKB; PA38618; -.
eggNOG; KOG1014; Eukaryota.
eggNOG; COG0300; LUCA.
GeneTree; ENSGT00390000010069; -.
HOGENOM; HOG000039237; -.
HOVERGEN; HBG005478; -.
InParanoid; Q53GQ0; -.
KO; K10251; -.
OMA; YLVTSAM; -.
OrthoDB; EOG091G06T2; -.
PhylomeDB; Q53GQ0; -.
TreeFam; TF314591; -.
BRENDA; 1.1.1.62; 2681.
Reactome; R-HSA-193048; Androgen biosynthesis.
Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
SABIO-RK; Q53GQ0; -.
UniPathway; UPA00094; -.
UniPathway; UPA00769; -.
ChiTaRS; HSD17B12; human.
GeneWiki; HSD17B12; -.
GenomeRNAi; 51144; -.
PRO; PR:Q53GQ0; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149084; -.
CleanEx; HS_HSD17B12; -.
ExpressionAtlas; Q53GQ0; baseline and differential.
Genevisible; Q53GQ0; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:Ensembl.
GO; GO:0102339; F:3-oxo-arachidoyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0102340; F:3-oxo-behenoyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0102342; F:3-oxo-cerotoyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0102341; F:3-oxo-lignoceroyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0005518; F:collagen binding; IEA:Ensembl.
GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:Ensembl.
GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; EXP:Reactome.
GO; GO:0006703; P:estrogen biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
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;
Alternative splicing; Complete proteome; Direct protein sequencing;
Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
NADP; Oxidoreductase; Polymorphism; Reference proteome;
Steroid biosynthesis; Transmembrane; Transmembrane helix.
CHAIN 1 312 Very-long-chain 3-oxoacyl-CoA reductase.
/FTId=PRO_0000248368.
TRANSMEM 4 24 Helical. {ECO:0000255}.
TRANSMEM 182 202 Helical. {ECO:0000255}.
TRANSMEM 271 291 Helical. {ECO:0000255}.
NP_BIND 50 79 NADP. {ECO:0000250}.
MOTIF 308 312 Di-lysine motif.
ACT_SITE 202 202 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 189 189 Substrate. {ECO:0000250}.
VAR_SEQ 95 98 KEKF -> SNYT (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056380.
VAR_SEQ 99 312 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056381.
VARIANT 280 280 S -> L (in dbSNP:rs11555762).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
/FTId=VAR_027277.
MUTAGEN 196 196 V->W: No effect.
{ECO:0000269|PubMed:16166196}.
MUTAGEN 234 234 F->A: Allows the conversion of
androstenedione to testosterone.
{ECO:0000269|PubMed:16166196}.
SEQUENCE 312 AA; 34324 MW; 8518336D7F514E50 CRC64;
MESALPAAGF LYWVGAGTVA YLALRISYSL FTALRVWGVG NEAGVGPGLG EWAVVTGSTD
GIGKSYAEEL AKHGMKVVLI SRSKDKLDQV SSEIKEKFKV ETRTIAVDFA SEDIYDKIKT
GLAGLEIGIL VNNVGMSYEY PEYFLDVPDL DNVIKKMINI NILSVCKMTQ LVLPGMVERS
KGAILNISSG SGMLPVPLLT IYSATKTFVD FFSQCLHEEY RSKGVFVQSV LPYFVATKLA
KIRKPTLDKP SPETFVKSAI KTVGLQSRTN GYLIHALMGS IISNLPSWIY LKIVMNMNKS
TRAHYLKKTK KN


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EIAAB11101 17-beta-HSD 14,17-beta-hydroxysteroid dehydrogenase 14,17-beta-hydroxysteroid dehydrogenase DHRS10,Bos taurus,Bovine,Dehydrogenase_reductase SDR family member 10,DHRS10,HSD17B14,Retinal short-chain de
EIAAB34167 EPHD-2,Epidermal retinol dehydrogenase 2,Homo sapiens,Human,RDHE2,RDH-E2,Retinal short-chain dehydrogenase reductase 2,retSDR2,SDR16C5,Short-chain dehydrogenase_reductase family 16C member 5
AKR1E2 AKR1C4 Gene aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I; dihydrodiol dehydrogenase 4)
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
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
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
U1774m CLIA 17-beta-HSD 13,17-beta-hydroxysteroid dehydrogenase 13,Alcohol dehydrogenase PAN1B-like,Hsd17b13,Mouse,Mus musculus,Scdr9,Short-chain dehydrogenase_reductase 9 96T
E1774m ELISA kit 17-beta-HSD 13,17-beta-hydroxysteroid dehydrogenase 13,Alcohol dehydrogenase PAN1B-like,Hsd17b13,Mouse,Mus musculus,Scdr9,Short-chain dehydrogenase_reductase 9 96T


 

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