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

N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 (EC 2.4.1.149) (Beta-1,3-N-acetylglucosaminyltransferase 1) (BGnT-1) (Beta-1,3-Gn-T1) (Beta3Gn-T1) (Beta-1,3-galactosyltransferase 7) (Beta-1,3-GalTase 7) (Beta3Gal-T7) (Beta3GalT7) (b3Gal-T7) (Beta-3-Gx-T7) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2) (BGnT-2) (Beta-1,3-Gn-T2) (Beta-1,3-N-acetylglucosaminyltransferase 2) (Beta3Gn-T2) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7)

 B3GN2_HUMAN             Reviewed;         397 AA.
Q9NY97; Q54AC1; Q9NQQ9; Q9NQR0; Q9NUT9;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
11-APR-2003, sequence version 2.
10-OCT-2018, entry version 154.
RecName: Full=N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2;
EC=2.4.1.149 {ECO:0000269|PubMed:11042166, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:9892646};
AltName: Full=Beta-1,3-N-acetylglucosaminyltransferase 1;
Short=BGnT-1;
Short=Beta-1,3-Gn-T1;
Short=Beta3Gn-T1;
AltName: Full=Beta-1,3-galactosyltransferase 7;
Short=Beta-1,3-GalTase 7;
Short=Beta3Gal-T7;
Short=Beta3GalT7;
Short=b3Gal-T7;
AltName: Full=Beta-3-Gx-T7;
AltName: Full=UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7;
AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2;
Short=BGnT-2;
Short=Beta-1,3-Gn-T2;
Short=Beta-1,3-N-acetylglucosaminyltransferase 2;
Short=Beta3Gn-T2;
AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7;
Name=B3GNT2; Synonyms=B3GALT7, B3GNT1;
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), FUNCTION, COFACTOR, AND
CATALYTIC ACTIVITY.
TISSUE=Brain;
PubMed=9892646; DOI=10.1073/pnas.96.2.406;
Zhou D., Dinter A., Gutierrez Gallego R., Kamerling J.P.,
Vliegenthart J.F.G., Berger E.G., Hennet T.;
"A beta-1,3-N-acetylglucosaminyltransferase with poly-N-
acetyllactosamine synthase activity is structurally related to beta-
1,3-galactosyltransferases.";
Proc. Natl. Acad. Sci. U.S.A. 96:406-411(1999).
[2]
SEQUENCE REVISION.
Zhou D., Berger E.G., Hennet T.;
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Amado M., Carneiro F., Clausen H.;
"Cloning and expression of two beta-1,3-galactosyltransferases:
beta3gal-T5 and beta3gal-T6.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Urinary bladder;
Gromova I., Gromov P., Celis J.E.;
"A novel member of beta-1,3-galactosyltransferase family is down
regulated during bladder TCC progression.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, TISSUE
SPECIFICITY, AND FUNCTION.
PubMed=11042166; DOI=10.1074/jbc.M004800200;
Shiraishi N., Natsume A., Togayachi A., Endo T., Akashima T.,
Yamada Y., Imai N., Nakagawa S., Koizumi S., Sekine S., Narimatsu H.,
Sasaki K.;
"Identification and characterization of three novel beta 1,3-N-
acetylglucosaminyltransferases structurally related to the beta 1,3-
galactosyltransferase family.";
J. Biol. Chem. 276:3498-3507(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Testis;
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 [LARGE SCALE MRNA] OF 25-397.
TISSUE=Placenta;
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).
[10]
REVIEW.
PubMed=10580128; DOI=10.1016/S0304-4165(99)00168-3;
Amado M., Almeida R., Schwientek T., Clausen H.;
"Identification and characterization of large galactosyltransferase
gene families: galactosyltransferases for all functions.";
Biochim. Biophys. Acta 1473:35-53(1999).
[11]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-79.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[13]
INTERACTION WITH B3GNT8, AND MUTAGENESIS OF ASP-245.
PubMed=18826941; DOI=10.1074/jbc.M806933200;
Seko A., Yamashita K.;
"Activation of beta1,3-N-acetylglucosaminyltransferase-2 (beta3Gn-T2)
by beta3Gn-T8. Possible involvement of beta3Gn-T8 in increasing poly-
N-acetyllactosamine chains in differentiated HL-60 cells.";
J. Biol. Chem. 283:33094-33100(2008).
[14]
FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=25279697; DOI=10.7554/eLife.03943;
Praissman J.L., Live D.H., Wang S., Ramiah A., Chinoy Z.S.,
Boons G.J., Moremen K.W., Wells L.;
"B4GAT1 is the priming enzyme for the LARGE-dependent functional
glycosylation of alpha-dystroglycan.";
Elife 3:0-0(2014).
-!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase involved in the
synthesis of poly-N-acetyllactosamine. Catalyzes the initiation
and elongation of poly-N-acetyllactosamine chains. Shows a marked
preference for Gal(beta1-4)Glc(NAc)-based acceptors
(PubMed:9892646). Probably constitutes the main polylactosamine
synthase. {ECO:0000269|PubMed:11042166,
ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:9892646}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + beta-D-
galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R = UDP + N-acetyl-
beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-
D-glucosaminyl-R. {ECO:0000269|PubMed:11042166,
ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:9892646}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:9892646};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:25279697}.
-!- SUBUNIT: Interacts with B3GNT8; this interaction greatly increases
B3GNT2 catalytic activity, independently of B3GNT8 enzymatic
activity. {ECO:0000269|PubMed:18826941}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NY97-1; Sequence=Displayed;
Name=2;
IsoId=Q9NY97-2; Sequence=VSP_001791;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay. No
experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11042166}.
-!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
{ECO:0000305}.
-!- CAUTION: Was indicated as B3Gal-T6 in submitted DNA entries.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA92031.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=UDP-
GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_434";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF092051; AAD09764.2; -; mRNA.
EMBL; AJ006077; CAB91546.1; -; mRNA.
EMBL; AF288208; AAF97253.1; -; mRNA.
EMBL; AF288209; AAF97254.1; -; mRNA.
EMBL; AB049584; BAB21530.1; -; mRNA.
EMBL; BC030579; AAH30579.1; -; mRNA.
EMBL; AC093401; AAX93271.1; -; Genomic_DNA.
EMBL; CH471053; EAW99977.1; -; Genomic_DNA.
EMBL; CH471053; EAW99978.1; -; Genomic_DNA.
EMBL; CH471053; EAW99979.1; -; Genomic_DNA.
EMBL; BC047933; AAH47933.1; -; mRNA.
EMBL; AK002009; BAA92031.1; ALT_INIT; mRNA.
CCDS; CCDS1870.1; -. [Q9NY97-1]
RefSeq; NP_001306004.1; NM_001319075.1. [Q9NY97-1]
RefSeq; NP_006568.2; NM_006577.5. [Q9NY97-1]
UniGene; Hs.173203; -.
ProteinModelPortal; Q9NY97; -.
BioGrid; 115919; 37.
IntAct; Q9NY97; 1.
STRING; 9606.ENSP00000305595; -.
CAZy; GT31; Glycosyltransferase Family 31.
GlyConnect; 1533; -.
iPTMnet; Q9NY97; -.
PhosphoSitePlus; Q9NY97; -.
BioMuta; B3GNT2; -.
EPD; Q9NY97; -.
MaxQB; Q9NY97; -.
PaxDb; Q9NY97; -.
PeptideAtlas; Q9NY97; -.
PRIDE; Q9NY97; -.
ProteomicsDB; 83198; -.
ProteomicsDB; 83199; -. [Q9NY97-2]
DNASU; 10678; -.
Ensembl; ENST00000301998; ENSP00000305595; ENSG00000170340. [Q9NY97-1]
Ensembl; ENST00000405767; ENSP00000384692; ENSG00000170340. [Q9NY97-1]
GeneID; 10678; -.
KEGG; hsa:10678; -.
UCSC; uc002sbs.4; human. [Q9NY97-1]
CTD; 10678; -.
DisGeNET; 10678; -.
EuPathDB; HostDB:ENSG00000170340.10; -.
GeneCards; B3GNT2; -.
HGNC; HGNC:15629; B3GNT2.
HPA; HPA005997; -.
MIM; 605581; gene.
neXtProt; NX_Q9NY97; -.
OpenTargets; ENSG00000170340; -.
PharmGKB; PA25218; -.
eggNOG; KOG2287; Eukaryota.
eggNOG; ENOG410ZZ1B; LUCA.
GeneTree; ENSGT00760000118879; -.
HOGENOM; HOG000232195; -.
HOVERGEN; HBG050653; -.
InParanoid; Q9NY97; -.
KO; K00741; -.
OMA; MDQPDIC; -.
OrthoDB; EOG091G0AXM; -.
PhylomeDB; Q9NY97; -.
TreeFam; TF318639; -.
BioCyc; MetaCyc:ENSG00000170340-MONOMER; -.
Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
ChiTaRS; B3GNT2; human.
GeneWiki; B3GNT2; -.
GenomeRNAi; 10678; -.
PRO; PR:Q9NY97; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000170340; Expressed in 209 organ(s), highest expression level in secondary oocyte.
CleanEx; HS_B3GNT1; -.
CleanEx; HS_B3GNT2; -.
Genevisible; Q9NY97; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0008532; F:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; TAS:Reactome.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IDA:UniProtKB.
GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
InterPro; IPR002659; Glyco_trans_31.
PANTHER; PTHR11214; PTHR11214; 1.
Pfam; PF01762; Galactosyl_T; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 397 N-acetyllactosaminide beta-1,3-N-
acetylglucosaminyltransferase 2.
/FTId=PRO_0000219170.
TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}.
TRANSMEM 8 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 397 Lumenal. {ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 219 219 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 11 MSVGRRRIKLL -> MVSRSLV (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_001791.
MUTAGEN 245 245 D->A: Loss of enzymatic activity, no loss
of B3GNT8-binding.
{ECO:0000269|PubMed:18826941}.
CONFLICT 11 11 L -> LL (in Ref. 3; CAB91546).
{ECO:0000305}.
SEQUENCE 397 AA; 46022 MW; B104ECCAE26DC4AC CRC64;
MSVGRRRIKL LGILMMANVF IYFIMEVSKS SSQEKNGKGE VIIPKEKFWK ISTPPEAYWN
REQEKLNRQY NPILSMLTNQ TGEAGRLSNI SHLNYCEPDL RVTSVVTGFN NLPDRFKDFL
LYLRCRNYSL LIDQPDKCAK KPFLLLAIKS LTPHFARRQA IRESWGQESN AGNQTVVRVF
LLGQTPPEDN HPDLSDMLKF ESEKHQDILM WNYRDTFFNL SLKEVLFLRW VSTSCPDTEF
VFKGDDDVFV NTHHILNYLN SLSKTKAKDL FIGDVIHNAG PHRDKKLKYY IPEVVYSGLY
PPYAGGGGFL YSGHLALRLY HITDQVHLYP IDDVYTGMCL QKLGLVPEKH KGFRTFDIEE
KNKNNICSYV DLMLVHSRKP QEMIDIWSQL QSAHLKC


Related products :

Catalog number Product name Quantity
E1725h ELISA GnT I.2,Homo sapiens,Human,MGAT1.2,POMGnT1,POMGNT1,Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1,UDP-GlcNAc alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.2,U 96T
E1725h ELISA kit GnT I.2,Homo sapiens,Human,MGAT1.2,POMGnT1,POMGNT1,Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1,UDP-GlcNAc alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase 96T
U1725h CLIA GnT I.2,Homo sapiens,Human,MGAT1.2,POMGnT1,POMGNT1,Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1,UDP-GlcNAc alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.2,UN 96T
EIAAB34382 Beta-1,3-N-acetylglucosaminyltransferase radical fringe,Homo sapiens,Human,O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase,RFNG
EIAAB34385 Beta-1,3-N-acetylglucosaminyltransferase radical fringe,O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase,Rat,Rattus norvegicus,Rfng
EIAAB34384 Beta-1,3-N-acetylglucosaminyltransferase radical fringe,Mouse,Mus musculus,O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase,Rfng
26-502 B3GALT6 (Beta-1,3-galactosyltransferase) transfers galactose from UDP-galactose to substrates with a terminal beta-linked galactose residue. It has a preference for galactose-beta-1,4-xylose that is f 0.05 mg
EIAAB34383 Beta-1,3-N-acetylglucosaminyltransferase radical fringe,Chicken,Gallus gallus,O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase,RFNG
20-783-72339 RAT ANTI HUMAN CD77 - EC 2.4.1.228; Alpha-1.4-galactosyltransferase; UDP-galactose beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase; Alpha-1.4-N-acetylglucosaminyltransferase; Alpha4Gal-T1; G 100 TESTS
E1073r Pig ELISA Kit FOR UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5 96T
B3GN7_RAT Rat ELISA Kit FOR UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7 96T
B3GNT4 B3GNT2 Gene UDP-GlcNAc betaGal beta-1,3-N-acetylglucosaminyltransferase 2
I0530 UDP-GlcNAc:betaGal beta-1, 3-N-acetylglucosaminyltransferase 5 (B3GNT5), Rat, ELISA Kit 96T
B3GNT6 B3GNT4 Gene UDP-GlcNAc betaGal beta-1,3-N-acetylglucosaminyltransferase 4
201-20-0569 B3GNT5{UDP-GlcNAc betaGal beta-1,3-N-acetylglucosaminyltransferase 5}rabbit.pAb 0.1ml
I0529 UDP-GlcNAc:betaGal beta-1, 3-N-acetylglucosaminyltransferase 5 (B3GNT5), Pig, ELISA Kit 96T
B4GALNT2 B3GNTL1 Gene UDP-GlcNAc betaGal beta-1,3-N-acetylglucosaminyltransferase-like 1
B4GALNT1 B3GNT9 Gene UDP-GlcNAc betaGal beta-1,3-N-acetylglucosaminyltransferase 9
201-20-0568 B3GNT4{UDP-GlcNAc betaGal beta-1,3-N-acetylglucosaminyltransferase 4}rabbit.pAb 0.1ml
E1491p Human ELISA Kit FOR UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 96T
B3GNT5 B3GNT3 Gene UDP-GlcNAc betaGal beta-1,3-N-acetylglucosaminyltransferase 3
B3GNT3 B3GNT1 Gene UDP-GlcNAc betaGal beta-1,3-N-acetylglucosaminyltransferase 1
B3GNT7 B3GNT5 Gene UDP-GlcNAc betaGal beta-1,3-N-acetylglucosaminyltransferase 5
B3GNT9 B3GNT7 Gene UDP-GlcNAc betaGal beta-1,3-N-acetylglucosaminyltransferase 7
B3GN3_MOUSE Mouse ELISA Kit FOR UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3 96T


 

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