Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Carbohydrate sulfotransferase 12 (EC 2.8.2.5) (Chondroitin 4-O-sulfotransferase 2) (Chondroitin 4-sulfotransferase 2) (C4ST-2) (C4ST2) (Sulfotransferase Hlo)

 CHSTC_HUMAN             Reviewed;         414 AA.
Q9NRB3; A4D1Z9; Q502W3; Q9NXY7;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 2.
18-JUL-2018, entry version 131.
RecName: Full=Carbohydrate sulfotransferase 12;
EC=2.8.2.5;
AltName: Full=Chondroitin 4-O-sulfotransferase 2;
AltName: Full=Chondroitin 4-sulfotransferase 2;
Short=C4ST-2;
Short=C4ST2;
AltName: Full=Sulfotransferase Hlo;
Name=CHST12; ORFNames=UNQ500/PRO1017;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=10781601; DOI=10.1074/jbc.M002443200;
Hiraoka N., Nakagawa H., Ong E., Akama O.T., Fukuda N.M., Fukuda M.;
"Molecular cloning and expression of two distinct human chondroitin 4-
O-sulfotransferases that belong to the HNK-1 sulfotransferase gene
family.";
J. Biol. Chem. 275:20188-20196(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Xia G., Evers M.R., Schachner M.;
"Cloning and expression of molecules homologous to HNK-1
sulfotransferase.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Skin;
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]
SUBSTRATE SPECIFICITY.
PubMed=12847091; DOI=10.1074/jbc.M306044200;
Mikami T., Mizumoto S., Kago N., Kitagawa H., Sugahara K.;
"Specificities of three distinct human chondroitin/dermatan N-
acetylgalactosamine 4-O-sulfotransferases demonstrated using partially
desulfated dermatan sulfate as an acceptor. Implication of
differential roles in dermatan sulfate biosynthesis.";
J. Biol. Chem. 278:36115-36127(2003).
-!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of the
N-acetylgalactosamine (GalNAc) residue of chondroitin and
desulfated dermatan sulfate. Chondroitin sulfate constitutes the
predominant proteoglycan present in cartilage and is distributed
on the surfaces of many cells and extracellular matrices. Activity
toward partially desulfated dermatan sulfate is however lower.
Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C
is used as an acceptor.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + chondroitin =
adenosine 3',5'-bisphosphate + chondroitin 4'-sulfate.
{ECO:0000269|PubMed:10781601}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed. Expressed a high level in
spinal chord, heart, spleen, thyroid, pituitary gland, adrenal
gland, peripheral blood leukocytes, thymus, lung, small intestine,
fetal kidney, fetal spleen and fetal lung.
{ECO:0000269|PubMed:10781601}.
-!- SIMILARITY: Belongs to the sulfotransferase 2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF239822; AAF81692.1; -; mRNA.
EMBL; AJ289131; CAB92133.1; -; mRNA.
EMBL; AY358574; AAQ88937.1; -; mRNA.
EMBL; AK313484; BAG36268.1; -; mRNA.
EMBL; CH236953; EAL23955.1; -; Genomic_DNA.
EMBL; BC002918; AAH02918.1; -; mRNA.
EMBL; BC095492; AAH95492.1; -; mRNA.
CCDS; CCDS5333.1; -.
RefSeq; NP_001230723.1; NM_001243794.1.
RefSeq; NP_001230724.1; NM_001243795.1.
RefSeq; NP_061111.1; NM_018641.4.
RefSeq; XP_011513745.1; XM_011515443.2.
RefSeq; XP_011513746.1; XM_011515444.2.
UniGene; Hs.288853; -.
UniGene; Hs.744987; -.
ProteinModelPortal; Q9NRB3; -.
BioGrid; 120681; 28.
IntAct; Q9NRB3; 4.
STRING; 9606.ENSP00000258711; -.
iPTMnet; Q9NRB3; -.
PhosphoSitePlus; Q9NRB3; -.
BioMuta; CHST12; -.
EPD; Q9NRB3; -.
MaxQB; Q9NRB3; -.
PaxDb; Q9NRB3; -.
PeptideAtlas; Q9NRB3; -.
PRIDE; Q9NRB3; -.
ProteomicsDB; 82325; -.
DNASU; 55501; -.
Ensembl; ENST00000258711; ENSP00000258711; ENSG00000136213.
Ensembl; ENST00000618655; ENSP00000481912; ENSG00000136213.
GeneID; 55501; -.
KEGG; hsa:55501; -.
UCSC; uc003smc.4; human.
CTD; 55501; -.
DisGeNET; 55501; -.
EuPathDB; HostDB:ENSG00000136213.9; -.
GeneCards; CHST12; -.
HGNC; HGNC:17423; CHST12.
HPA; HPA041680; -.
MIM; 610129; gene.
neXtProt; NX_Q9NRB3; -.
OpenTargets; ENSG00000136213; -.
PharmGKB; PA134969008; -.
eggNOG; KOG4651; Eukaryota.
eggNOG; ENOG4111GJR; LUCA.
GeneTree; ENSGT00760000119214; -.
HOGENOM; HOG000231801; -.
HOVERGEN; HBG097841; -.
InParanoid; Q9NRB3; -.
KO; K04742; -.
OMA; DIPNYEL; -.
OrthoDB; EOG091G0FZO; -.
PhylomeDB; Q9NRB3; -.
TreeFam; TF325581; -.
BioCyc; MetaCyc:HS06130-MONOMER; -.
BRENDA; 2.8.2.5; 2681.
Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
ChiTaRS; CHST12; human.
GeneWiki; CHST12; -.
GenomeRNAi; 55501; -.
PRO; PR:Q9NRB3; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000136213; -.
CleanEx; HS_CHST12; -.
ExpressionAtlas; Q9NRB3; baseline and differential.
Genevisible; Q9NRB3; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0030173; C:integral component of Golgi membrane; NAS:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; NAS:UniProtKB.
GO; GO:0047756; F:chondroitin 4-sulfotransferase activity; IDA:UniProtKB.
GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IDA:UniProtKB.
GO; GO:0030208; P:dermatan sulfate biosynthetic process; IDA:UniProtKB.
InterPro; IPR018011; Carb_sulfotrans_8-10.
InterPro; IPR005331; Sulfotransferase.
PANTHER; PTHR12137; PTHR12137; 1.
Pfam; PF03567; Sulfotransfer_2; 1.
2: Evidence at transcript level;
Carbohydrate metabolism; Complete proteome; Glycoprotein;
Golgi apparatus; Membrane; Polymorphism; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 414 Carbohydrate sulfotransferase 12.
/FTId=PRO_0000189668.
TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}.
TRANSMEM 6 26 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 27 414 Lumenal. {ECO:0000255}.
NP_BIND 171 177 PAPS. {ECO:0000250}.
NP_BIND 245 253 PAPS. {ECO:0000250}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 52 52 P -> H (in dbSNP:rs3735099).
/FTId=VAR_021471.
VARIANT 61 61 T -> S (in dbSNP:rs3735100).
/FTId=VAR_021472.
VARIANT 94 94 P -> L (in dbSNP:rs12536223).
/FTId=VAR_033738.
VARIANT 109 109 R -> S (in dbSNP:rs17132395).
/FTId=VAR_021473.
VARIANT 145 145 A -> P (in dbSNP:rs17132399).
/FTId=VAR_021474.
CONFLICT 30 30 G -> S (in Ref. 1; AAF81692).
{ECO:0000305}.
CONFLICT 42 42 R -> K (in Ref. 1; AAF81692).
{ECO:0000305}.
CONFLICT 92 92 P -> L (in Ref. 1; AAF81692).
{ECO:0000305}.
CONFLICT 380 380 W -> C (in Ref. 1; AAF81692).
{ECO:0000305}.
SEQUENCE 414 AA; 48414 MW; 8730D8731F623078 CRC64;
MTKARLFRLW LVLGSVFMIL LIIVYWDSAG AAHFYLHTSF SRPHTGPPLP TPGPDRDREL
TADSDVDEFL DKFLSAGVKQ SDLPRKETEQ PPAPGSMEES VRGYDWSPRD ARRSPDQGRQ
QAERRSVLRG FCANSSLAFP TKERAFDDIP NSELSHLIVD DRHGAIYCYV PKVACTNWKR
VMIVLSGSLL HRGAPYRDPL RIPREHVHNA SAHLTFNKFW RRYGKLSRHL MKVKLKKYTK
FLFVRDPFVR LISAFRSKFE LENEEFYRKF AVPMLRLYAN HTSLPASARE AFRAGLKVSF
ANFIQYLLDP HTEKLAPFNE HWRQVYRLCH PCQIDYDFVG KLETLDEDAA QLLQLLQVDR
QLRFPPSYRN RTASSWEEDW FAKIPLAWRQ QLYKLYEADF VLFGYPKPEN LLRD


Related products :

Catalog number Product name Quantity
EIAAB07297 C4ST2,C4ST-2,Carbohydrate sulfotransferase 12,Chondroitin 4-O-sulfotransferase 2,Chondroitin 4-sulfotransferase 2,CHST12,Homo sapiens,Human,Sulfotransferase Hlo,UNQ500_PRO1017
EIAAB07296 C4ST2,C4ST-2,Carbohydrate sulfotransferase 12,Chondroitin 4-O-sulfotransferase 2,Chondroitin 4-sulfotransferase 2,Chst12,Mouse,Mus musculus
EIAAB07293 C4S-1,C4ST1,C4ST-1,Carbohydrate sulfotransferase 11,Chondroitin 4-O-sulfotransferase 1,Chondroitin 4-sulfotransferase 1,CHST11,Homo sapiens,Human
EIAAB07298 C4ST3,C4ST-3,Carbohydrate sulfotransferase 13,Chondroitin 4-O-sulfotransferase 3,Chondroitin 4-sulfotransferase 3,CHST13,Homo sapiens,Human
EIAAB07294 C4S-1,C4ST1,C4ST-1,Carbohydrate sulfotransferase 11,Chondroitin 4-O-sulfotransferase 1,Chondroitin 4-sulfotransferase 1,Chst11,Mouse,Mus musculus
EIAAB07295 C4S-1,C4ST1,C4ST-1,Carbohydrate sulfotransferase 11,Chondroitin 4-O-sulfotransferase 1,Chondroitin 4-sulfotransferase 1,Chst11,Rat,Rattus norvegicus
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
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
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
EIAAB07283 C6ST-2,Carbohydrate sulfotransferase 7,Chondroitin 6-sulfotransferase 2,Chst7,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 5,GlcNAc6ST-4,Gn6st-4,Gst5,GST-5,mC6ST-2,Mouse,Mus
EIAAB07284 C6ST-2,Carbohydrate sulfotransferase 7,Chondroitin 6-sulfotransferase 2,CHST7,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 5,GlcNAc6ST-4,Gn6st-4,GST-5,Homo sapiens,Human,N-ac
EIAAB07275 C6st,C6ST-1,Carbohydrate sulfotransferase 3,Chondroitin 6-O-sulfotransferase 1,Chst3,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 0,Gst0,GST-0,Mouse,Mus musculus
EIAAB07282 C6ST-2,Carbohydrate sulfotransferase 7,Chondroitin 6-sulfotransferase 2,Chst7,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 5,GlcNAc6ST-4,Gn6st-4,GST-5,N-acetylglucosamine 6-O
EIAAB07273 C6ST-1,Carbohydrate sulfotransferase 3,Chicken,Chondroitin 6-O-sulfotransferase 1,CHST3,Gallus gallus
EIAAB40145 Alcohol sulfotransferase,Hydroxysteroid sulfotransferase 2,Rat,Rattus norvegicus,ST2B1,Sulfotransferase 2B1,Sulfotransferase family cytosolic 2B member 1,Sult2b1
EIAAB40146 Alcohol sulfotransferase,Hydroxysteroid sulfotransferase 2,Mouse,Mus musculus,ST2B1,Sulfotransferase 2B1,Sulfotransferase family cytosolic 2B member 1,Sult2b,Sult2b1
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
EIAAB40144 Alcohol sulfotransferase,Homo sapiens,HSST2,Human,Hydroxysteroid sulfotransferase 2,ST2B1,Sulfotransferase 2B1,Sulfotransferase family cytosolic 2B member 1,SULT2B1
EIAAB40140 Bile salt sulfotransferase,Dehydroepiandrosterone sulfotransferase,DHEA-ST,Homo sapiens,HST,HST,Human,Hydroxysteroid Sulfotransferase,ST2,ST2A1,ST2A3,STD,Sulfotransferase 2A1,SULT2A1
EIAAB07270 Carbohydrate sulfotransferase 1,CHST1,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 1,GST-1,Homo sapiens,Human,Keratan sulfate Gal-6 sulfotransferase,KS6ST,KSGal6ST,KSST
EIAAB07268 Carbohydrate sulfotransferase 1,Chst1,Galactose_N-acetylglucosamine_N-acetylglucosamine 6-O-sulfotransferase 1,Gst1,GST-1,Keratan sulfate Gal-6 sulfotransferase,KS6ST,KSGal6ST,KSST,Mouse,Mus musculus
EIAAB40115 Aryl sulfotransferase,Aryl sulfotransferase IV,ASTIV,Minoxidil sulfotransferase,Mx-ST,Phenol sulfotransferase,PST-1,Rat,Rattus norvegicus,ST1A1,St1a1,Sulfokinase,Sulfotransferase 1A1,Sult1a1,Tyrosine-
EIAAB07287 Carbohydrate sulfotransferase 9,CHST9,GalNAc-4-O-sulfotransferase 2,GalNAc-4-ST2,GalNAc4ST-2,Homo sapiens,Human,N-acetylgalactosamine-4-O-sulfotransferase 2,UNQ2549_PRO6175
EIAAB40112 Aryl sulfotransferase,Mouse,mSTp1,Mus musculus,Phenol sulfotransferase,Phenol_aryl sulfotransferase,ST1A1,St1a1,ST1A4,Stp,Stp1,Sulfokinase,Sulfotransferase 1A1,Sult1a1
EIAAB40120 Homo sapiens,Human,ST1B1,ST1B2,ST1B2,Sulfotransferase 1B1,Sulfotransferase 1B2,Sulfotransferase family cytosolic 1B member 1,SULT1B1,SULT1B2,Thyroid hormone sulfotransferase


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur