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Cytosolic sulfotransferase 18 (AtSOT18) (EC 2.8.2.38) (Desulfo-glucosinolate sulfotransferase B) (Sulfotransferase 5B) (AtST5b)

 SOT18_ARATH             Reviewed;         350 AA.
Q9C9C9; Q8LA18;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 98.
RecName: Full=Cytosolic sulfotransferase 18;
Short=AtSOT18;
EC=2.8.2.38 {ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
AltName: Full=Desulfo-glucosinolate sulfotransferase B;
AltName: Full=Sulfotransferase 5B;
Short=AtST5b;
Name=SOT18; Synonyms=ST5B; OrderedLocusNames=At1g74090;
ORFNames=F2P9.4;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, AND INDUCTION.
PubMed=15358770; DOI=10.1074/jbc.M407681200;
Piotrowski M., Schemenewitz A., Lopukhina A., Mueller A., Janowitz T.,
Weiler E.W., Oecking C.;
"Desulfoglucosinolate sulfotransferases from Arabidopsis thaliana
catalyze the final step in the biosynthesis of the glucosinolate core
structure.";
J. Biol. Chem. 279:50717-50725(2004).
[7]
GENE FAMILY, SUBCELLULAR LOCATION, AND NOMENCLATURE.
PubMed=15234990; DOI=10.1093/jxb/erh183;
Klein M., Papenbrock J.;
"The multi-protein family of Arabidopsis sulphotransferases and their
relatives in other plant species.";
J. Exp. Bot. 55:1809-1820(2004).
[8]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=cv. Columbia;
PubMed=15866872; DOI=10.1074/jbc.M502332200;
Hirai M.Y., Klein M., Fujikawa Y., Yano M., Goodenowe D.B.,
Yamazaki Y., Kanaya S., Nakamura Y., Kitayama M., Suzuki H.,
Sakurai N., Shibata D., Tokuhisa J., Reichelt M., Gershenzon J.,
Papenbrock J., Saito K.;
"Elucidation of gene-to-gene and metabolite-to-gene networks in
Arabidopsis by integration of metabolomics and transcriptomics.";
J. Biol. Chem. 280:25590-25595(2005).
[9]
MUTAGENESIS OF ASP-301, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION,
BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANTS GLY-301 AND ASN-339.
STRAIN=cv. C24, and cv. Columbia;
PubMed=16367753; DOI=10.1111/j.1742-4658.2005.05048.x;
Klein M., Reichelt M., Gershenzon J., Papenbrock J.;
"The three desulfoglucosinolate sulfotransferase proteins in
Arabidopsis have different substrate specificities and are
differentially expressed.";
FEBS J. 273:122-136(2006).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=cv. C24, and cv. Columbia;
PubMed=19077143; DOI=10.1111/j.1399-3054.2008.01182.x;
Klein M., Papenbrock J.;
"Kinetics and substrate specificities of desulfo-glucosinolate
sulfotransferases in Arabidopsis thaliana.";
Physiol. Plantarum 135:140-149(2009).
[11]
FUNCTION.
PubMed=21281472; DOI=10.1186/1472-6750-11-12;
Moeldrup M.E., Geu-Flores F., Olsen C.E., Halkier B.A.;
"Modulation of sulfur metabolism enables efficient glucosinolate
engineering.";
BMC Biotechnol. 11:12-12(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl
sulfate (PAPS) as sulfonate donor to catalyze the sulfate
conjugation of desulfo-glucosinolates (dsGSs), the final step in
the biosynthesis of the glucosinolate core structure. Preferred
substrate are the long-chain desulfo-glucosinolates, 7-
methylthioheptyl and 8-methylthiooctyl, derived from methionine.
Substrate preference is desulfo-benzyl glucosinolate > desulfo-4-
methylthiobutyl glucosinolate > desulfo-6-methylthiohexyl
glucosinolate > desulfo-3-methylthiopropyl glucosinolate >
desulfo-indol-3-yl methyl glucosinolate > desulfo-singrin >
desulfo-3-butenyl glucosinolate. {ECO:0000269|PubMed:15358770,
ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143, ECO:0000269|PubMed:21281472}.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + an aliphatic
desulfoglucosinolate = adenosine 3',5'-bisphosphate + an aliphatic
glucosinolate. {ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143}.
-!- ACTIVITY REGULATION: Inhibited by phosphoadenosine 5'-phosphate
(PAP).
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=50 uM for desulfobenzyl glucosinolate (in cv. Columbia)
{ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
KM=35 uM for 3'-phospho-5'-adenylyl sulfate (in cv. C24)
{ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
KM=60 uM for 3'-phospho-5'-adenylyl sulfate (in cv. Columbia)
{ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
KM=100 uM for desulfo-3-methylthiopropyl glucosinolate (in cv.
C24) {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
KM=55 uM for desulfo-3-methylthiopropyl glucosinolate (in cv.
Columbia) {ECO:0000269|PubMed:15866872,
ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
KM=130 uM for desulfo-4-methylthiobutyl glucosinolate (in cv.
C24) {ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
KM=43 uM for desulfo-4-methylthiobutyl glucosinolate (in cv.
Columbia) {ECO:0000269|PubMed:15866872,
ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
Vmax=171 pmol/sec/mg enzyme with desulfo-benzyl glucosinolate as
substrate (in cv. C24) {ECO:0000269|PubMed:15866872,
ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
Vmax=851 pmol/sec/mg enzyme with desulfo-benzyl glucosinolate as
substrate (in cv. Columbia) {ECO:0000269|PubMed:15866872,
ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
Vmax=467 pmol/sec/mg enzyme with desulfo-allyl glucosinolate as
substrate (in cv. Columbia) {ECO:0000269|PubMed:15866872,
ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
Vmax=27 pmol/sec/mg enzyme with 3'-phosphoadenosine 5'-
phosphosulfate as substrate (in cv. C24)
{ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
Vmax=860 pmol/sec/mg enzyme with 3'-phosphoadenosine 5'-
phosphosulfate as substrate (in cv. Columbia)
{ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
Vmax=99 pmol/sec/mg enzyme with desulfo-3-methylthiopropyl
glucosinolate as substrate (in cv. C24)
{ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
Vmax=2763 pmol/sec/mg enzyme with desulfo-3-methylthiopropyl
glucosinolate as substrate (in cv. Columbia)
{ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
Vmax=131 pmol/sec/mg enzyme with desulfo-4-
methylthiobutylglucosinolate as substrate (in cv. C24)
{ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
Vmax=1883 pmol/sec/mg enzyme with desulfo-4-methylthiobutyl
glucosinolate as substrate (in cv. Columbia)
{ECO:0000269|PubMed:15866872, ECO:0000269|PubMed:16367753,
ECO:0000269|PubMed:19077143};
pH dependence:
Optimum pH is 9.0. {ECO:0000269|PubMed:15866872,
ECO:0000269|PubMed:16367753, ECO:0000269|PubMed:19077143};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15234990,
ECO:0000269|PubMed:16367753}.
-!- TISSUE SPECIFICITY: Expressed in roots, leaves and stems. Barely
detected in siliques and flowers. {ECO:0000269|PubMed:16367753}.
-!- DEVELOPMENTAL STAGE: Low expression in young plants (up to 4
weeks), then slight increase in older plants.
{ECO:0000269|PubMed:16367753}.
-!- INDUCTION: Not induced by coronatine, methyl jasmonate or high
sulfate concentration. {ECO:0000269|PubMed:15358770,
ECO:0000269|PubMed:16367753}.
-!- POLYMORPHISM: In cv. C24, the substrate preference is restricted
to a small number of desulfo-gulcosinolates: desulfo-6-
methylthiohexyl glucosinolate > desulfo-benzyl glucosinolate >
desulfo-2-phenylethyl glucosinolate (PubMed:16367753).
{ECO:0000269|PubMed:16367753}.
-!- MISCELLANEOUS: Strong differences in the kinetic behavior between
the same protein from different cultivars.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
{ECO:0000305}.
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EMBL; AC016662; AAG52515.1; -; Genomic_DNA.
EMBL; CP002684; AEE35549.1; -; Genomic_DNA.
EMBL; BT004984; AAO50517.1; -; mRNA.
EMBL; AK117463; BAC42128.1; -; mRNA.
EMBL; AY088081; AAM65627.1; -; mRNA.
PIR; H96768; H96768.
RefSeq; NP_177549.1; NM_106069.3.
UniGene; At.34922; -.
PDB; 5MEK; X-ray; 1.74 A; A=26-347.
PDB; 5MEX; X-ray; 1.92 A; A=26-347.
PDBsum; 5MEK; -.
PDBsum; 5MEX; -.
ProteinModelPortal; Q9C9C9; -.
SMR; Q9C9C9; -.
STRING; 3702.AT1G74090.1; -.
iPTMnet; Q9C9C9; -.
PaxDb; Q9C9C9; -.
PRIDE; Q9C9C9; -.
EnsemblPlants; AT1G74090.1; AT1G74090.1; AT1G74090.
GeneID; 843749; -.
Gramene; AT1G74090.1; AT1G74090.1; AT1G74090.
KEGG; ath:AT1G74090; -.
Araport; AT1G74090; -.
TAIR; locus:2031516; AT1G74090.
eggNOG; KOG1584; Eukaryota.
eggNOG; ENOG4111H56; LUCA.
HOGENOM; HOG000037210; -.
InParanoid; Q9C9C9; -.
KO; K22321; -.
OMA; HILAYWK; -.
OrthoDB; EOG09360D4I; -.
PhylomeDB; Q9C9C9; -.
BioCyc; MetaCyc:AT1G74090-MONOMER; -.
BRENDA; 2.8.2.24; 399.
Reactome; R-ATH-156584; Cytosolic sulfonation of small molecules.
PRO; PR:Q9C9C9; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9C9C9; baseline and differential.
Genevisible; Q9C9C9; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0080066; F:3-methylthiopropyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
GO; GO:0080067; F:4-methylthiobutyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
GO; GO:0080068; F:5-methylthiopentyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
GO; GO:0080069; F:7-methylthioheptyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
GO; GO:0080070; F:8-methylthiooctyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
GO; GO:0047364; F:desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
GO; GO:0080071; F:indol-3-yl-methyl-desulfoglucosinolate sulfotransferase activity; IDA:TAIR.
GO; GO:0019761; P:glucosinolate biosynthetic process; IDA:TAIR.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000863; Sulfotransferase_dom.
Pfam; PF00685; Sulfotransfer_1; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Reference proteome; Transferase.
CHAIN 1 350 Cytosolic sulfotransferase 18.
/FTId=PRO_0000315847.
NP_BIND 93 98 PAPS. {ECO:0000250}.
NP_BIND 313 315 PAPS. {ECO:0000250}.
COMPBIAS 11 16 Poly-Thr.
COMPBIAS 268 271 Poly-Glu.
ACT_SITE 155 155 Proton acceptor. {ECO:0000250}.
BINDING 177 177 PAPS. {ECO:0000250}.
BINDING 185 185 PAPS. {ECO:0000250}.
BINDING 243 243 PAPS. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
VARIANT 301 301 D -> G (in strain: cv. C24).
{ECO:0000269|PubMed:16367753}.
VARIANT 339 339 K -> N (in strain: cv. C24).
{ECO:0000269|PubMed:16367753}.
MUTAGEN 301 301 D->G: 25 time reduction of activity with
desulfo-benzyl glucosinolate as
substrate. {ECO:0000269|PubMed:16367753}.
CONFLICT 31 31 E -> K (in Ref. 5; AAM65627).
{ECO:0000305}.
HELIX 29 42 {ECO:0000244|PDB:5MEK}.
STRAND 46 51 {ECO:0000244|PDB:5MEK}.
STRAND 54 59 {ECO:0000244|PDB:5MEK}.
STRAND 62 64 {ECO:0000244|PDB:5MEK}.
HELIX 66 78 {ECO:0000244|PDB:5MEK}.
STRAND 86 90 {ECO:0000244|PDB:5MEK}.
HELIX 96 108 {ECO:0000244|PDB:5MEK}.
TURN 109 111 {ECO:0000244|PDB:5MEK}.
HELIX 114 116 {ECO:0000244|PDB:5MEK}.
HELIX 118 120 {ECO:0000244|PDB:5MEK}.
HELIX 124 127 {ECO:0000244|PDB:5MEK}.
TURN 131 133 {ECO:0000244|PDB:5MEK}.
HELIX 134 137 {ECO:0000244|PDB:5MEK}.
HELIX 142 145 {ECO:0000244|PDB:5MEK}.
STRAND 151 154 {ECO:0000244|PDB:5MEK}.
HELIX 158 160 {ECO:0000244|PDB:5MEK}.
HELIX 163 168 {ECO:0000244|PDB:5MEK}.
STRAND 171 176 {ECO:0000244|PDB:5MEK}.
HELIX 179 190 {ECO:0000244|PDB:5MEK}.
HELIX 203 211 {ECO:0000244|PDB:5MEK}.
HELIX 220 233 {ECO:0000244|PDB:5MEK}.
TURN 235 237 {ECO:0000244|PDB:5MEK}.
STRAND 238 242 {ECO:0000244|PDB:5MEK}.
HELIX 243 248 {ECO:0000244|PDB:5MEK}.
HELIX 250 260 {ECO:0000244|PDB:5MEK}.
HELIX 267 271 {ECO:0000244|PDB:5MEK}.
HELIX 274 281 {ECO:0000244|PDB:5MEK}.
HELIX 284 288 {ECO:0000244|PDB:5MEK}.
HELIX 291 293 {ECO:0000244|PDB:5MEK}.
STRAND 300 302 {ECO:0000244|PDB:5MEK}.
HELIX 308 311 {ECO:0000244|PDB:5MEK}.
HELIX 319 322 {ECO:0000244|PDB:5MEK}.
HELIX 326 340 {ECO:0000244|PDB:5MEK}.
TURN 341 343 {ECO:0000244|PDB:5MEK}.
SEQUENCE 350 AA; 40465 MW; AB68B7477262EB57 CRC64;
MESETLTAKA TITTTTLPSH DETKTESTEF EKNQKRYQDL ISTFPHEKGW RPKEPLIEYG
GYWWLPSLLE GCIHAQEFFQ ARPSDFLVCS YPKTGTTWLK ALTFAIANRS RFDDSSNPLL
KRNPHEFVPY IEIDFPFFPE VDVLKDKGNT LFSTHIPYEL LPDSVVKSGC KMVYIWREPK
DTFISMWTFL HKERTELGPV SNLEESFDMF CRGLSGYGPY LNHILAYWKA YQENPDRILF
LKYETMRADP LPYVKSLAEF MGHGFTAEEE EKGVVEKVVN LCSFETLKNL EANKGEKDRE
DRPGVYANSA YFRKGKVGDW SNYLTPEMAA RIDGLMEEKF KGTGLLEHGK


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EIAAB07274 C6ST-1,Carbohydrate sulfotransferase 3,Chondroitin 6-O-sulfotransferase 1,Chondroitin 6-sulfotransferase,CHST3,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 0,GST-0,Homo sapie
EIAAB07297 C4ST2,C4ST-2,Carbohydrate sulfotransferase 12,Chondroitin 4-O-sulfotransferase 2,Chondroitin 4-sulfotransferase 2,CHST12,Homo sapiens,Human,Sulfotransferase Hlo,UNQ500_PRO1017
EIAAB40114 Aryl sulfotransferase 1,HAST1_HAST2,Homo sapiens,Human,OK_SW-cl.88,Phenol sulfotransferase 1,Phenol-sulfating phenol sulfotransferase 1,P-PST 1,ST1A1,ST1A3,STP,STP1,Sulfotransferase 1A1,SULT1A1,Thermo
EIAAB40116 Aryl sulfotransferase 2,Homo sapiens,Human,Phenol sulfotransferase 2,Phenol-sulfating phenol sulfotransferase 2,P-PST 2,ST1A2,STP2,Sulfotransferase 1A2,SULT1A2
EIAAB40117 Aryl sulfotransferase 1A3_1A4,Catecholamine-sulfating phenol sulfotransferase,HAST3,Homo sapiens,Human,Monoamine-sulfating phenol sulfotransferase,M-PST,Placental estrogen sulfotransferase,ST1A3_ST1A4
EIAAB40121 Bos taurus,Bovine,ST1B1,Sulfotransferase 1B1,Sulfotransferase family cytosolic 1B member 1,SULT1B1
18-003-44263 Carbohydrate sulfotransferase 7 - EC 2.8.2.17; EC 2.8.2.-; Chondroitin 6-sulfotransferase 2; C6ST-2; N-acetylglucosamine 6-O-sulfotransferase 1; GlcNAc6ST-4; Galactose_N-acetylglucosamine_N-acetylgluc 0.1 mg Protein A
EIAAB40141 Bile salt sulfotransferase 1,Hydroxysteroid sulfotransferase,Mouse,Mus musculus,ST,ST2A1,Sta1,Sulfotransferase 2A1,Sult2a1
EIAAB40111 Aryl sulfotransferase,Bos taurus,Bovine,Phenol sulfotransferase,Phenol-sulfating phenol sulfotransferase,P-PST,ST1A1,STP,Sulfotransferase 1A1,SULT1A1
EIAAB40160 Brain sulfotransferase-like protein,mBR-STL,Mouse,Mus musculus,Nervous system sulfotransferase,NST,ST4A1,Sulfotransferase 4A1,Sult4a1,Sultx3
EIAAB40143 Bile salt sulfotransferase 2,Hydroxysteroid sulfotransferase,Mouse,Mus musculus,ST,ST2A2,Sta2,Sth2,Sulfotransferase 2A2,Sult2a2
EIAAB07276 C6ST-1,Carbohydrate sulfotransferase 3,Chondroitin 6-O-sulfotransferase 1,Chst3,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 0,GST-0,Rat,Rattus norvegicus
EIAAB40161 Brain sulfotransferase-like protein,Nervous system sulfotransferase,NST,Rat,Rattus norvegicus,rBR-STL,ST4A1,Sulfotransferase 4A1,Sult4a1,Sultx3
EIAAB40162 Brain sulfotransferase-like protein,hBR-STL,hBR-STL-1,Homo sapiens,Human,Nervous system sulfotransferase,NST,ST4A1,Sulfotransferase 4A1,SULT4A1,SULTX3
EIAAB07269 Carbohydrate sulfotransferase 1,Chst1,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 1,GST-1,Keratan sulfate Gal-6 sulfotransferase,KS6ST,KSGal6ST,KSST,Rat,Rattus norvegicus


 

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