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Aldo-keto reductase family 1 member C4 (EC 1.1.1.-) (3-alpha-HSD1) (3-alpha-hydroxysteroid dehydrogenase type I) (EC 1.1.1.357) (Chlordecone reductase) (CDR) (EC 1.1.1.225) (Dihydrodiol dehydrogenase 4) (DD-4) (DD4) (HAKRA)

 AK1C4_HUMAN             Reviewed;         323 AA.
P17516; Q5T6A3; Q8WW84; Q9NS54;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
20-DEC-2017, entry version 190.
RecName: Full=Aldo-keto reductase family 1 member C4;
EC=1.1.1.-;
AltName: Full=3-alpha-HSD1;
AltName: Full=3-alpha-hydroxysteroid dehydrogenase type I;
EC=1.1.1.357;
AltName: Full=Chlordecone reductase;
Short=CDR;
EC=1.1.1.225;
AltName: Full=Dihydrodiol dehydrogenase 4;
Short=DD-4;
Short=DD4;
AltName: Full=HAKRA;
Name=AKR1C4; Synonyms=CHDR;
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 VARIANT ARG-250.
TISSUE=Liver;
PubMed=8274401; DOI=10.1016/0960-0760(93)90308-J;
Qin K.-N., New M.I., Cheng K.-C.;
"Molecular cloning of multiple cDNAs encoding human enzymes
structurally related to 3 alpha-hydroxysteroid dehydrogenase.";
J. Steroid Biochem. Mol. Biol. 46:673-679(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND VARIANT
ARG-250.
PubMed=7650035; DOI=10.1074/jbc.270.34.20162;
Khanna M., Qin K.-N., Wang R.W., Cheng K.-C.;
"Substrate specificity, gene structure, and tissue-specific
distribution of multiple human 3 alpha-hydroxysteroid
dehydrogenases.";
J. Biol. Chem. 270:20162-20168(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-250.
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS CYS-145; ARG-250 AND VAL-311.
TISSUE=Liver;
PubMed=10634139;
Kume T., Iwasa H., Shiraishi H., Yokoi T., Nagashima K., Otsuka M.,
Terada T., Takagi T., Hara A., Kamataki T.;
"Characterization of a novel variant (S145C/L311V) of 3alpha-
hydroxysteroid/dihydrodiol dehydrogenase in human liver.";
Pharmacogenetics 9:763-771(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ARG-250.
TISSUE=Liver;
PubMed=10672042; DOI=10.1046/j.1365-2443.2000.00310.x;
Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y.,
Watanabe K., Ito S.;
"Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with
three aldo-keto reductase genes.";
Genes Cells 5:111-125(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION OF 3-ALPHA-HSD ACTIVITY,
TISSUE SPECIFICITY, AND VARIANT ARG-250.
TISSUE=Liver;
PubMed=11158055; DOI=10.1210/jcem.86.2.7216;
Dufort I., Labrie F., Luu-The V.;
"Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases:
differential lability and tissue distribution.";
J. Clin. Endocrinol. Metab. 86:841-846(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-170 AND
ARG-250.
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-323, AND VARIANT ARG-250.
TISSUE=Liver;
PubMed=2187532; DOI=10.1021/bi00456a034;
Winters C.J., Molowa D.T., Guzelian P.S.;
"Isolation and characterization of cloned cDNAs encoding human liver
chlordecone reductase.";
Biochemistry 29:1080-1087(1990).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-323, PROTEIN SEQUENCE OF 5-29; 76-131;
184-201 AND 271-294, AND VARIANT ARG-250.
TISSUE=Liver;
PubMed=8172617; DOI=10.1042/bj2990545;
Deyashiki Y., Ogasawara A., Nakayama T., Nakanishi M., Miyabe Y.,
Sato K., Hara A.;
"Molecular cloning of two human liver 3 alpha-
hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical
with chlordecone reductase and bile-acid binder.";
Biochem. J. 299:545-552(1994).
[11]
PROTEIN SEQUENCE OF 40-54; 105-121; 162-175; 184-196; 277-291 AND
307-321, AND CHARACTERIZATION AS 3-ALPHA-HSD.
PubMed=1530633; DOI=10.1016/0006-291X(92)91260-W;
Binstock J.M., Iyer R.B., Hamby C.V., Fried V.A., Schwartz I.S.,
Weinstein B.I., Southren A.L.;
"Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity
with human hepatic chlordecone reductase.";
Biochem. Biophys. Res. Commun. 187:760-766(1992).
[12]
INVOLVEMENT IN SRXY8.
PubMed=21802064; DOI=10.1016/j.ajhg.2011.06.009;
Fluck C.E., Meyer-Boni M., Pandey A.V., Kempna P., Miller W.L.,
Schoenle E.J., Biason-Lauber A.;
"Why boys will be boys: two pathways of fetal testicular androgen
biosynthesis are needed for male sexual differentiation.";
Am. J. Hum. Genet. 89:201-218(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]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADP.
Structural genomics consortium (SGC);
"Crystal structure of human 3-alpha hydroxysteroid/dihydrodiol
dehydrogenase (AKR1C4) complexed with NADP+.";
Submitted (FEB-2006) to the PDB data bank.
-!- FUNCTION: Catalyzes the transformation of the potent androgen
dihydrotestosterone (DHT) into the less active form, 5-alpha-
androstan-3-alpha,17-beta-diol (3-alpha-diol). Also has some 20-
alpha-hydroxysteroid dehydrogenase activity. The biotransformation
of the pesticide chlordecone (kepone) to its corresponding alcohol
leads to increased biliary excretion of the pesticide and
concomitant reduction of its neurotoxicity since bile is the major
excretory route.
-!- CATALYTIC ACTIVITY: Chlordecone alcohol + NADP(+) = chlordecone +
NADPH.
-!- CATALYTIC ACTIVITY: A 3-alpha-hydroxysteroid + NAD(P)(+) = a 3-
oxosteroid + NAD(P)H.
-!- SUBUNIT: Monomer. {ECO:0000269|Ref.14}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:11158055,
ECO:0000269|PubMed:7650035}.
-!- PTM: The N-terminus is blocked.
-!- POLYMORPHISM: The allele with Cys-145/Val-311 shows a three- to
five-fold decrease in catalytic efficiency for xenobiotic and
steroidal substrates compared to the Ser-145/Leu-311 allele.
-!- DISEASE: 46,XY sex reversal 8 (SRXY8) [MIM:614279]: A disorder of
sex development. Affected individuals have a 46,XY karyotype but
present as phenotypically normal females.
{ECO:0000269|PubMed:21802064}. Note=The gene represented in this
entry may act as a disease modifier. A splicing mutation resulting
in loss of AKR1C4 exon 2 has been found in affected individuals
carrying a causative mutation in AKR1C2 (PubMed:21802064). These
patients manifest a more severe disease phenotype than individuals
only carrying mutations in AKR1C2. {ECO:0000269|PubMed:21802064}.
-!- SIMILARITY: Belongs to the aldo/keto reductase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA35658.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; S68287; AAD14010.1; -; mRNA.
EMBL; AB045829; BAA99542.1; -; mRNA.
EMBL; AB031085; BAA92885.1; -; mRNA.
EMBL; AB032163; BAA92893.1; -; Genomic_DNA.
EMBL; AL355303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC020744; AAH20744.1; -; mRNA.
EMBL; M33375; AAA35658.1; ALT_INIT; mRNA.
EMBL; D26125; BAA05122.1; -; mRNA.
CCDS; CCDS7064.1; -.
PIR; A57407; A57407.
PIR; S59620; S59620.
RefSeq; NP_001809.3; NM_001818.3.
UniGene; Hs.567245; -.
PDB; 2FVL; X-ray; 2.40 A; A/B/C=1-323.
PDBsum; 2FVL; -.
ProteinModelPortal; P17516; -.
SMR; P17516; -.
BioGrid; 107534; 4.
STRING; 9606.ENSP00000263126; -.
BindingDB; P17516; -.
ChEMBL; CHEMBL4999; -.
DrugBank; DB00157; NADH.
SwissLipids; SLP:000000805; -.
iPTMnet; P17516; -.
PhosphoSitePlus; P17516; -.
BioMuta; AKR1C4; -.
DMDM; 308153631; -.
EPD; P17516; -.
MaxQB; P17516; -.
PaxDb; P17516; -.
PeptideAtlas; P17516; -.
PRIDE; P17516; -.
DNASU; 1109; -.
Ensembl; ENST00000263126; ENSP00000263126; ENSG00000198610.
Ensembl; ENST00000380448; ENSP00000369814; ENSG00000198610.
GeneID; 1109; -.
KEGG; hsa:1109; -.
UCSC; uc001ihw.2; human.
CTD; 1109; -.
DisGeNET; 1109; -.
EuPathDB; HostDB:ENSG00000198610.10; -.
GeneCards; AKR1C4; -.
HGNC; HGNC:387; AKR1C4.
HPA; HPA044720; -.
HPA; HPA068265; -.
MalaCards; AKR1C4; -.
MIM; 600451; gene.
MIM; 614279; phenotype.
neXtProt; NX_P17516; -.
OpenTargets; ENSG00000198610; -.
Orphanet; 90796; 46,XY disorder of sex development due to isolated 17,20 lyase deficiency.
PharmGKB; PA24680; -.
eggNOG; KOG1577; Eukaryota.
eggNOG; COG0656; LUCA.
GeneTree; ENSGT00760000119041; -.
HOGENOM; HOG000250272; -.
HOVERGEN; HBG000020; -.
InParanoid; P17516; -.
KO; K00037; -.
OMA; NPKEDHY; -.
OrthoDB; EOG091G0D69; -.
PhylomeDB; P17516; -.
TreeFam; TF106492; -.
BioCyc; MetaCyc:HS10739-MONOMER; -.
BRENDA; 1.1.1.357; 2681.
Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-HSA-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SABIO-RK; P17516; -.
SIGNOR; P17516; -.
EvolutionaryTrace; P17516; -.
GeneWiki; 3-alpha-HSD; -.
GenomeRNAi; 1109; -.
PRO; PR:P17516; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000198610; -.
CleanEx; HS_AKR1C4; -.
Genevisible; P17516; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0004033; F:aldo-keto reductase (NADP) activity; TAS:Reactome.
GO; GO:0047023; F:androsterone dehydrogenase activity; IDA:UniProtKB.
GO; GO:0015125; F:bile acid transmembrane transporter activity; TAS:ProtInc.
GO; GO:0047743; F:chlordecone reductase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
GO; GO:0001758; F:retinal dehydrogenase activity; IDA:UniProtKB.
GO; GO:0008209; P:androgen metabolic process; TAS:ProtInc.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:ProtInc.
GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
GO; GO:0071395; P:cellular response to jasmonic acid stimulus; IDA:UniProtKB.
GO; GO:0044597; P:daunorubicin metabolic process; IMP:UniProtKB.
GO; GO:0044598; P:doxorubicin metabolic process; IMP:UniProtKB.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0008202; P:steroid metabolic process; TAS:ProtInc.
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;
NADP; Oxidoreductase; Polymorphism; Reference proteome.
CHAIN 1 323 Aldo-keto reductase family 1 member C4.
/FTId=PRO_0000124640.
NP_BIND 20 24 NADP. {ECO:0000269|Ref.14}.
NP_BIND 166 167 NADP. {ECO:0000269|Ref.14}.
NP_BIND 216 221 NADP. {ECO:0000269|Ref.14}.
NP_BIND 270 280 NADP. {ECO:0000269|Ref.14}.
ACT_SITE 55 55 Proton donor. {ECO:0000250}.
BINDING 50 50 NADP. {ECO:0000269|Ref.14}.
BINDING 117 117 Substrate. {ECO:0000250}.
BINDING 190 190 NADP. {ECO:0000269|Ref.14}.
SITE 54 54 Important for substrate specificity.
{ECO:0000250}.
SITE 84 84 Lowers pKa of active site Tyr.
{ECO:0000250}.
VARIANT 135 135 G -> E (in dbSNP:rs11253043).
/FTId=VAR_028240.
VARIANT 145 145 S -> C (in dbSNP:rs3829125).
{ECO:0000269|PubMed:10634139}.
/FTId=VAR_013290.
VARIANT 170 170 C -> Y (in dbSNP:rs17851824).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_028241.
VARIANT 250 250 Q -> R (in dbSNP:rs4880718).
{ECO:0000269|PubMed:10634139,
ECO:0000269|PubMed:10672042,
ECO:0000269|PubMed:11158055,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2187532,
ECO:0000269|PubMed:7626489,
ECO:0000269|PubMed:7650035,
ECO:0000269|PubMed:8172617,
ECO:0000269|PubMed:8274401}.
/FTId=VAR_028242.
VARIANT 311 311 L -> V (in dbSNP:rs17134592).
{ECO:0000269|PubMed:10634139}.
/FTId=VAR_013291.
HELIX 3 5 {ECO:0000244|PDB:2FVL}.
STRAND 7 9 {ECO:0000244|PDB:2FVL}.
STRAND 15 22 {ECO:0000244|PDB:2FVL}.
HELIX 33 44 {ECO:0000244|PDB:2FVL}.
STRAND 48 50 {ECO:0000244|PDB:2FVL}.
HELIX 53 55 {ECO:0000244|PDB:2FVL}.
HELIX 58 71 {ECO:0000244|PDB:2FVL}.
HELIX 76 78 {ECO:0000244|PDB:2FVL}.
STRAND 80 85 {ECO:0000244|PDB:2FVL}.
HELIX 87 89 {ECO:0000244|PDB:2FVL}.
HELIX 92 106 {ECO:0000244|PDB:2FVL}.
STRAND 111 117 {ECO:0000244|PDB:2FVL}.
STRAND 124 126 {ECO:0000244|PDB:2FVL}.
HELIX 144 156 {ECO:0000244|PDB:2FVL}.
STRAND 159 167 {ECO:0000244|PDB:2FVL}.
HELIX 170 177 {ECO:0000244|PDB:2FVL}.
STRAND 187 192 {ECO:0000244|PDB:2FVL}.
HELIX 200 208 {ECO:0000244|PDB:2FVL}.
STRAND 212 217 {ECO:0000244|PDB:2FVL}.
TURN 225 227 {ECO:0000244|PDB:2FVL}.
HELIX 235 237 {ECO:0000244|PDB:2FVL}.
HELIX 239 247 {ECO:0000244|PDB:2FVL}.
HELIX 252 262 {ECO:0000244|PDB:2FVL}.
STRAND 266 270 {ECO:0000244|PDB:2FVL}.
HELIX 274 280 {ECO:0000244|PDB:2FVL}.
HELIX 281 285 {ECO:0000244|PDB:2FVL}.
HELIX 290 297 {ECO:0000244|PDB:2FVL}.
HELIX 309 311 {ECO:0000244|PDB:2FVL}.
STRAND 318 321 {ECO:0000244|PDB:2FVL}.
SEQUENCE 323 AA; 37067 MW; E728CE4B420E8C58 CRC64;
MDPKYQRVEL NDGHFMPVLG FGTYAPPEVP RNRAVEVTKL AIEAGFRHID SAYLYNNEEQ
VGLAIRSKIA DGSVKREDIF YTSKLWCTFF QPQMVQPALE SSLKKLQLDY VDLYLLHFPM
ALKPGETPLP KDENGKVIFD TVDLSATWEV MEKCKDAGLA KSIGVSNFNC RQLEMILNKP
GLKYKPVCNQ VECHPYLNQS KLLDFCKSKD IVLVAHSALG TQRHKLWVDP NSPVLLEDPV
LCALAKKHKQ TPALIALRYQ LQRGVVVLAK SYNEQRIREN IQVFEFQLTS EDMKVLDGLN
RNYRYVVMDF LMDHPDYPFS DEY


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E2220b ELISA 20-alpha-HSD,20-alpha-hydroxysteroid dehydrogenase,AKR1B1,Aldehyde reductase,Aldose reductase,AR,Bos taurus,Bovine 96T
U2220b CLIA kit 20-alpha-HSD,20-alpha-hydroxysteroid dehydrogenase,AKR1B1,Aldehyde reductase,Aldose reductase,AR,Bos taurus,Bovine 96T
U2220b CLIA 20-alpha-HSD,20-alpha-hydroxysteroid dehydrogenase,AKR1B1,Aldehyde reductase,Aldose reductase,AR,Bos taurus,Bovine 96T
E2220b 20-alpha-HSD,20-alpha-hydroxysteroid dehydrogenase,AKR1B1,Aldehyde reductase,Aldose reductase,AR,Bos taurus,Bovine
CSB-EL001539RA Rat aldo-keto reductase family 1, member B1 (aldose reductase) (AKR1B1) ELISA kit, Species Rat, Sample Type serum, plasma 96T


 

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