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Respiratory nitrate reductase 1 beta chain (EC 1.7.99.4) (Nitrate reductase A subunit beta) (Quinol-nitrate oxidoreductase subunit beta)

 NARH_ECOLI              Reviewed;         512 AA.
P11349;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 3.
25-OCT-2017, entry version 172.
RecName: Full=Respiratory nitrate reductase 1 beta chain;
EC=1.7.99.4;
AltName: Full=Nitrate reductase A subunit beta;
AltName: Full=Quinol-nitrate oxidoreductase subunit beta;
Name=narH; OrderedLocusNames=b1225, JW1216;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / TG1;
PubMed=2674654; DOI=10.1007/BF00331275;
Blasco F., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.;
"Nitrate reductase of Escherichia coli: completion of the nucleotide
sequence of the nar operon and reassessment of the role of the alpha
and beta subunits in iron binding and electron transfer.";
Mol. Gen. Genet. 218:249-256(1989).
[2]
SEQUENCE REVISION TO 398-417.
STRAIN=K12 / TG1;
Blasco F.;
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 365-512.
PubMed=2832376; DOI=10.1128/jb.170.4.1721-1729.1988;
Sodergren E.J., Demoss J.A.;
"narI region of the Escherichia coli nitrate reductase (nar) operon
contains two genes.";
J. Bacteriol. 170:1721-1729(1988).
[7]
PROTEIN SEQUENCE OF 1-10.
PubMed=3053688;
Sodergren E.J., Hsu P.Y., Demoss J.A.;
"Roles of the narJ and narI gene products in the expression of nitrate
reductase in Escherichia coli.";
J. Biol. Chem. 263:16156-16162(1988).
[8]
EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
PubMed=1321049; DOI=10.1111/j.1432-1033.1992.tb17020.x;
Guigliarelli B., Asso M., More C., Augier V., Blasco F., Pommier J.,
Giordano G., Bertrand P.;
"EPR and redox characterization of iron-sulfur centers in nitrate
reductases A and Z from Escherichia coli. Evidence for a high-
potential and a low-potential class and their relevance in the
electron-transfer mechanism.";
Eur. J. Biochem. 207:61-68(1992).
[9]
MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR
CLUSTERS.
PubMed=8383531; DOI=10.1021/bi00059a018;
Augier V., Guigliarelli B., Asso M., Bertrand P., Frixon C.,
Giordano G., Chippaux M., Blasco F.;
"Site-directed mutagenesis of conserved cysteine residues within the
beta subunit of Escherichia coli nitrate reductase. Physiological,
biochemical, and EPR characterization of the mutated enzymes.";
Biochemistry 32:2013-2023(1993).
[10]
MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR
CLUSTERS.
PubMed=8388253; DOI=10.1021/bi00070a018;
Augier V., Asso M., Guigliarelli B., More C., Bertrand P.,
Santini C.-L., Blasco F., Chippaux M., Giordano G.;
"Removal of the high-potential [4Fe-4S] center of the beta-subunit
from Escherichia coli nitrate reductase. Physiological, biochemical,
and EPR characterization of site-directed mutated enzymes.";
Biochemistry 32:5099-5108(1993).
[11]
MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR
CLUSTERS.
PubMed=8664273; DOI=10.1021/bi952459p;
Guigliarelli B., Magalon A., Asso M., Bertrand P., Frixon C.,
Giordano G., Blasco F.;
"Complete coordination of the four Fe-S centers of the beta subunit
from Escherichia coli nitrate reductase. Physiological, biochemical,
and EPR characterization of site-directed mutants lacking the highest
or lowest potential [4Fe-4S] clusters.";
Biochemistry 35:4828-4836(1996).
[12]
EPR SPECTROSCOPY, AND REDOX POTENTIOMETRY OF IRON-SULFUR CLUSTERS.
PubMed=9516445; DOI=10.1074/jbc.273.13.7462;
Rothery R.A., Magalon A., Giordano G., Guigliarelli B., Blasco F.,
Weiner J.H.;
"The molybdenum cofactor of Escherichia coli nitrate reductase A
(NarGHI). Effect of a mobAB mutation and interactions with [Fe-S]
clusters.";
J. Biol. Chem. 273:7462-7469(1998).
[13]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
(3FE-4S) AND IRON-SULFUR (4FE-4S), COFACTOR, AND SUBUNIT.
PubMed=12910261; DOI=10.1038/nsb969;
Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F.,
Weiner J.H., Strynadka N.C.J.;
"Insights into the respiratory electron transfer pathway from the
structure of nitrate reductase A.";
Nat. Struct. Biol. 10:681-687(2003).
[14]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
(3FE-4S) AND IRON-SULFUR (4FE-4S), AND COFACTOR.
PubMed=14725769; DOI=10.1016/j.str.2003.11.020;
Jormakka M., Richardson D., Byrne B., Iwata S.;
"Architecture of NarGH reveals a structural classification of Mo-
bisMGD enzymes.";
Structure 12:95-104(2004).
-!- FUNCTION: The nitrate reductase enzyme complex allows E.coli to
use nitrate as an electron acceptor during anaerobic growth. The
beta chain is an electron transfer unit containing four cysteine
clusters involved in the formation of iron-sulfur centers.
Electrons are transferred from the gamma chain to the molybdenum
cofactor of the alpha subunit.
-!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
acceptor.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769};
Note=Binds 3 [4Fe-4S] clusters per subunit.
{ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769};
-!- COFACTOR:
Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
Evidence={ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769};
Note=Binds 1 [3Fe-4S] cluster per subunit.
{ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769};
-!- SUBUNIT: Dimer of heterotrimers each composed of an alpha, a beta
and a gamma chain. Alpha and beta are catalytic chains; gamma
chains are involved in binding the enzyme complex to the
cytoplasmic membrane. {ECO:0000269|PubMed:12910261}.
-!- INTERACTION:
P42593:fadH; NbExp=3; IntAct=EBI-555067, EBI-561933;
P09152:narG; NbExp=13; IntAct=EBI-555067, EBI-547248;
P19317:narW; NbExp=3; IntAct=EBI-555067, EBI-555088;
P19318:narY; NbExp=3; IntAct=EBI-555067, EBI-555059;
P19319:narZ; NbExp=6; IntAct=EBI-555067, EBI-547262;
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
-!- INDUCTION: By nitrate.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/NAR/";
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EMBL; M20147; AAA24195.1; -; Genomic_DNA.
EMBL; U00096; AAC74309.1; -; Genomic_DNA.
EMBL; AP009048; BAA36095.1; -; Genomic_DNA.
EMBL; X16181; CAA34304.1; -; Genomic_DNA.
PIR; F64869; RDECNB.
RefSeq; NP_415743.1; NC_000913.3.
RefSeq; WP_000702650.1; NZ_LN832404.1.
PDB; 1Q16; X-ray; 1.90 A; B=1-512.
PDB; 1R27; X-ray; 2.00 A; B/D=1-512.
PDB; 1SIW; X-ray; 2.20 A; B=1-512.
PDB; 1Y4Z; X-ray; 2.00 A; B=1-512.
PDB; 1Y5I; X-ray; 1.90 A; B=1-512.
PDB; 1Y5L; X-ray; 2.50 A; B=1-512.
PDB; 1Y5N; X-ray; 2.50 A; B=1-512.
PDB; 3EGW; X-ray; 1.90 A; B=1-509.
PDB; 3IR5; X-ray; 2.30 A; B=1-512.
PDB; 3IR6; X-ray; 2.80 A; B=1-512.
PDB; 3IR7; X-ray; 2.50 A; B=1-512.
PDBsum; 1Q16; -.
PDBsum; 1R27; -.
PDBsum; 1SIW; -.
PDBsum; 1Y4Z; -.
PDBsum; 1Y5I; -.
PDBsum; 1Y5L; -.
PDBsum; 1Y5N; -.
PDBsum; 3EGW; -.
PDBsum; 3IR5; -.
PDBsum; 3IR6; -.
PDBsum; 3IR7; -.
ProteinModelPortal; P11349; -.
SMR; P11349; -.
BioGrid; 4262231; 20.
DIP; DIP-10312N; -.
IntAct; P11349; 15.
MINT; MINT-1260007; -.
STRING; 316385.ECDH10B_1284; -.
DrugBank; DB04464; N-Formylmethionine.
TCDB; 5.A.3.1.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
PaxDb; P11349; -.
PRIDE; P11349; -.
EnsemblBacteria; AAC74309; AAC74309; b1225.
EnsemblBacteria; BAA36095; BAA36095; BAA36095.
GeneID; 945780; -.
KEGG; ecj:JW1216; -.
KEGG; eco:b1225; -.
PATRIC; fig|1411691.4.peg.1056; -.
EchoBASE; EB0633; -.
EcoGene; EG10639; narH.
eggNOG; ENOG4108IUE; Bacteria.
eggNOG; COG1140; LUCA.
HOGENOM; HOG000237353; -.
InParanoid; P11349; -.
KO; K00371; -.
PhylomeDB; P11349; -.
BioCyc; EcoCyc:NARH-MONOMER; -.
BioCyc; MetaCyc:NARH-MONOMER; -.
BRENDA; 1.7.5.1; 2026.
EvolutionaryTrace; P11349; -.
PRO; PR:P11349; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0031224; C:intrinsic component of membrane; IDA:EcoCyc.
GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IDA:EcoCyc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0044799; C:NarGHI complex; IDA:EcoCyc.
GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:EcoCyc.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
GO; GO:0009055; F:electron carrier activity; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008940; F:nitrate reductase activity; IMP:EcoCyc.
GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
GO; GO:0042126; P:nitrate metabolic process; IMP:EcoCyc.
CDD; cd10557; NarH_beta-like; 1.
InterPro; IPR017896; 4Fe4S_Fe-S-bd.
InterPro; IPR029263; Nitr_red_bet_C.
InterPro; IPR006547; NO3_Rdtase_bsu.
Pfam; PF13247; Fer4_11; 1.
Pfam; PF14711; Nitr_red_bet_C; 1.
TIGRFAMs; TIGR01660; narH; 1.
PROSITE; PS51379; 4FE4S_FER_2; 3.
1: Evidence at protein level;
3D-structure; 3Fe-4S; 4Fe-4S; Cell membrane; Complete proteome;
Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
Membrane; Metal-binding; Nitrate assimilation; Oxidoreductase;
Reference proteome; Repeat; Transport.
CHAIN 1 512 Respiratory nitrate reductase 1 beta
chain.
/FTId=PRO_0000096720.
DOMAIN 7 35 4Fe-4S ferredoxin-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
DOMAIN 175 206 4Fe-4S ferredoxin-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
DOMAIN 208 237 4Fe-4S ferredoxin-type 3.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
METAL 16 16 Iron-sulfur 1 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 19 19 Iron-sulfur 1 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 22 22 Iron-sulfur 1 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 26 26 Iron-sulfur 2 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 184 184 Iron-sulfur 3 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 187 187 Iron-sulfur 3 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 192 192 Iron-sulfur 3 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 196 196 Iron-sulfur 4 (3Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 217 217 Iron-sulfur 4 (3Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 223 223 Iron-sulfur 4 (3Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 227 227 Iron-sulfur 3 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 244 244 Iron-sulfur 2 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 247 247 Iron-sulfur 2 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 259 259 Iron-sulfur 2 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
METAL 263 263 Iron-sulfur 1 (4Fe-4S).
{ECO:0000269|PubMed:12910261,
ECO:0000269|PubMed:14725769}.
CONFLICT 398 417 DTKPVLRALKRMLAMRHYKR -> EYQTGTARTETYAGDAS
LQT (in Ref. 6; AAA24195). {ECO:0000305}.
STRAND 3 12 {ECO:0000244|PDB:1Q16}.
TURN 13 15 {ECO:0000244|PDB:1Q16}.
HELIX 21 30 {ECO:0000244|PDB:1Q16}.
STRAND 41 49 {ECO:0000244|PDB:1Q16}.
TURN 51 57 {ECO:0000244|PDB:1Q16}.
HELIX 59 62 {ECO:0000244|PDB:1Q16}.
STRAND 65 68 {ECO:0000244|PDB:1Q16}.
STRAND 74 76 {ECO:0000244|PDB:1Q16}.
HELIX 81 85 {ECO:0000244|PDB:1Q16}.
TURN 86 89 {ECO:0000244|PDB:1Q16}.
HELIX 97 100 {ECO:0000244|PDB:1Q16}.
STRAND 104 106 {ECO:0000244|PDB:1Q16}.
HELIX 109 113 {ECO:0000244|PDB:1Q16}.
STRAND 126 128 {ECO:0000244|PDB:1Q16}.
TURN 129 131 {ECO:0000244|PDB:1Q16}.
TURN 142 148 {ECO:0000244|PDB:1Q16}.
HELIX 152 155 {ECO:0000244|PDB:1Q16}.
HELIX 159 161 {ECO:0000244|PDB:1Q16}.
HELIX 167 170 {ECO:0000244|PDB:1Q16}.
HELIX 172 174 {ECO:0000244|PDB:1Q16}.
STRAND 178 182 {ECO:0000244|PDB:1Q16}.
HELIX 191 194 {ECO:0000244|PDB:1Q16}.
STRAND 201 204 {ECO:0000244|PDB:1Q16}.
TURN 205 207 {ECO:0000244|PDB:1Q16}.
STRAND 210 212 {ECO:0000244|PDB:1Q16}.
TURN 214 216 {ECO:0000244|PDB:1Q16}.
HELIX 223 226 {ECO:0000244|PDB:1Q16}.
STRAND 232 235 {ECO:0000244|PDB:1Q16}.
TURN 236 239 {ECO:0000244|PDB:1Q16}.
STRAND 240 243 {ECO:0000244|PDB:1Q16}.
HELIX 248 251 {ECO:0000244|PDB:1Q16}.
TURN 252 254 {ECO:0000244|PDB:1Q16}.
HELIX 258 261 {ECO:0000244|PDB:1Q16}.
STRAND 268 276 {ECO:0000244|PDB:1Q16}.
HELIX 277 279 {ECO:0000244|PDB:1Q16}.
HELIX 280 284 {ECO:0000244|PDB:1Q16}.
HELIX 289 291 {ECO:0000244|PDB:1Q16}.
HELIX 292 297 {ECO:0000244|PDB:1Q16}.
HELIX 306 314 {ECO:0000244|PDB:1Q16}.
HELIX 319 325 {ECO:0000244|PDB:1Q16}.
HELIX 329 334 {ECO:0000244|PDB:1Q16}.
STRAND 341 343 {ECO:0000244|PDB:1Q16}.
HELIX 345 347 {ECO:0000244|PDB:1Q16}.
STRAND 352 356 {ECO:0000244|PDB:1Q16}.
STRAND 366 368 {ECO:0000244|PDB:1Q16}.
HELIX 380 382 {ECO:0000244|PDB:1Q16}.
STRAND 383 385 {ECO:0000244|PDB:1Q16}.
HELIX 387 394 {ECO:0000244|PDB:1Q16}.
HELIX 399 420 {ECO:0000244|PDB:1Q16}.
HELIX 428 432 {ECO:0000244|PDB:1Q16}.
HELIX 437 447 {ECO:0000244|PDB:1Q16}.
HELIX 452 455 {ECO:0000244|PDB:1Q16}.
TURN 463 466 {ECO:0000244|PDB:1Q16}.
HELIX 469 475 {ECO:0000244|PDB:1Q16}.
SEQUENCE 512 AA; 58066 MW; 2E7719C8D078BAEA CRC64;
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ GFPTDWENQE
KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY YEPFDFDYQN LHTAPEGSKS
QPIARPRSLI TGERMAKIEK GPNWEDDLGG EFDKLAKDKN FDNIQKAMYS QFENTFMMYL
PRLCEHCLNP ACVATCPSGA IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK
SEKCIFCYPR IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL PMVWYVPPLS
PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK PVLRALKRML AMRHYKRAET
VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA NYEDRFVVPS SHRELAREAF PEKNGCGFTF
GDGCHGSDTK FNLFNSRRID AIDVTSKTEP HP


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E0463h ELISA kit Homo sapiens,Human,Thyroid-stimulating hormone subunit beta,Thyrotropin beta chain,Thyrotropin subunit beta,TSHB,TSH-B,TSH-beta 96T
E0830Rb ELISA kit Follicle-stimulating hormone beta subunit,Follitropin beta chain,Follitropin subunit beta,FSHB,FSH-B,FSH-beta,Oryctolagus cuniculus,Rabbit 96T
E0830h ELISA kit Follicle-stimulating hormone beta subunit,Follitropin beta chain,Follitropin subunit beta,FSHB,FSH-B,FSH-beta,Homo sapiens,Human 96T
E0463h ELISA Homo sapiens,Human,Thyroid-stimulating hormone subunit beta,Thyrotropin beta chain,Thyrotropin subunit beta,TSHB,TSH-B,TSH-beta 96T
E0830m ELISA kit Follicle-stimulating hormone beta subunit,Follitropin beta chain,Follitropin subunit beta,Fshb,FSH-B,FSH-beta,Mouse,Mus musculus 96T
E0463b ELISA Bos taurus,Bovine,Thyroid-stimulating hormone subunit beta,Thyrotropin beta chain,Thyrotropin subunit beta,TSHB,TSH-B,TSH-beta 96T
E0830m ELISA Follicle-stimulating hormone beta subunit,Follitropin beta chain,Follitropin subunit beta,Fshb,FSH-B,FSH-beta,Mouse,Mus musculus 96T
E0463m ELISA Mouse,Mus musculus,Thyroid-stimulating hormone subunit beta,Thyrotropin beta chain,Thyrotropin subunit beta,Tshb,TSH-B,TSH-beta 96T
E0830r ELISA Follicle-stimulating hormone beta subunit,Follitropin beta chain,Follitropin subunit beta,Fshb,FSH-B,FSH-beta,Rat,Rattus norvegicus 96T


 

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