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

Beta-1,4-galactosyltransferase 2 (Beta-1,4-GalTase 2) (Beta4Gal-T2) (b4Gal-T2) (EC 2.4.1.-) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2) [Includes: Lactose synthase A protein (EC 2.4.1.22); N-acetyllactosamine synthase (EC 2.4.1.90) (Nal synthase); Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase (EC 2.4.1.38); Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase (EC 2.4.1.-)]

 B4GT2_MOUSE             Reviewed;         369 AA.
Q9Z2Y2; Q3TMP2;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
10-MAY-2017, entry version 125.
RecName: Full=Beta-1,4-galactosyltransferase 2;
Short=Beta-1,4-GalTase 2;
Short=Beta4Gal-T2;
Short=b4Gal-T2;
EC=2.4.1.-;
AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2;
AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2;
Includes:
RecName: Full=Lactose synthase A protein;
EC=2.4.1.22;
Includes:
RecName: Full=N-acetyllactosamine synthase;
EC=2.4.1.90;
AltName: Full=Nal synthase;
Includes:
RecName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase;
EC=2.4.1.38;
Includes:
RecName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
EC=2.4.1.-;
Name=B4galt2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9597550; DOI=10.1093/glycob/8.5.517;
Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L.;
"The expanding beta 4-galactosyltransferase gene family: messages from
the databanks.";
Glycobiology 8:517-526(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Sato T.;
"Mouse beta-1,4-galactosyltransferase II (beta-1,4-GalT II).";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
-!- FUNCTION: Responsible for the synthesis of complex-type N-linked
oligosaccharides in many glycoproteins as well as the carbohydrate
moieties of glycolipids. Can produce lactose (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + D-glucose = UDP +
lactose.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + N-acetyl-beta-D-
glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-
acetyl-beta-D-glucosaminylglycopeptide.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + N-acetyl-D-glucosamine
= UDP + N-acetyllactosamine.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
{ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Note=Trans cisternae of Golgi stack. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=b4GalT2;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_461";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF142670; AAF22220.1; -; mRNA.
EMBL; AB019541; BAA34385.1; -; mRNA.
EMBL; AK165829; BAE38399.1; -; mRNA.
CCDS; CCDS18539.1; -.
RefSeq; NP_001240310.1; NM_001253381.1.
RefSeq; NP_059073.1; NM_017377.5.
RefSeq; XP_006503293.1; XM_006503230.3.
RefSeq; XP_017175805.1; XM_017320316.1.
UniGene; Mm.123843; -.
ProteinModelPortal; Q9Z2Y2; -.
SMR; Q9Z2Y2; -.
STRING; 10090.ENSMUSP00000030266; -.
CAZy; GT7; Glycosyltransferase Family 7.
PhosphoSitePlus; Q9Z2Y2; -.
MaxQB; Q9Z2Y2; -.
PaxDb; Q9Z2Y2; -.
PRIDE; Q9Z2Y2; -.
Ensembl; ENSMUST00000030266; ENSMUSP00000030266; ENSMUSG00000028541.
Ensembl; ENSMUST00000084325; ENSMUSP00000081352; ENSMUSG00000028541.
Ensembl; ENSMUST00000106421; ENSMUSP00000102029; ENSMUSG00000028541.
GeneID; 53418; -.
KEGG; mmu:53418; -.
UCSC; uc008ujb.2; mouse.
CTD; 8704; -.
MGI; MGI:1858493; B4galt2.
eggNOG; KOG3916; Eukaryota.
eggNOG; ENOG410ZYYA; LUCA.
GeneTree; ENSGT00760000119140; -.
HOGENOM; HOG000231027; -.
HOVERGEN; HBG058334; -.
InParanoid; Q9Z2Y2; -.
KO; K07967; -.
OMA; EDATYDC; -.
OrthoDB; EOG091G0P66; -.
PhylomeDB; Q9Z2Y2; -.
TreeFam; TF312834; -.
Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
Reactome; R-MMU-975577; N-Glycan antennae elongation.
UniPathway; UPA00378; -.
PRO; PR:Q9Z2Y2; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028541; -.
ExpressionAtlas; Q9Z2Y2; baseline and differential.
Genevisible; Q9Z2Y2; MM.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004461; F:lactose synthase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003945; F:N-acetyllactosamine synthase activity; IEA:UniProtKB-EC.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0007613; P:memory; IMP:MGI.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
GO; GO:0008542; P:visual learning; IMP:MGI.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR003859; Galactosyl_T.
InterPro; IPR027791; Galactosyl_T_C.
InterPro; IPR027995; Galactosyl_T_N.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
PANTHER; PTHR19300; PTHR19300; 1.
Pfam; PF02709; Glyco_transf_7C; 1.
Pfam; PF13733; Glyco_transf_7N; 1.
PRINTS; PR02050; B14GALTRFASE.
SUPFAM; SSF53448; SSF53448; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Manganese; Membrane; Metal-binding;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 369 Beta-1,4-galactosyltransferase 2.
/FTId=PRO_0000080534.
TOPO_DOM 1 15 Cytoplasmic. {ECO:0000255}.
TRANSMEM 16 36 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 37 369 Lumenal. {ECO:0000255}.
REGION 147 151 UDP-alpha-D-galactose binding.
{ECO:0000250}.
REGION 186 188 UDP-alpha-D-galactose binding.
{ECO:0000250}.
REGION 214 215 UDP-alpha-D-galactose binding.
{ECO:0000250}.
REGION 277 280 N-acetyl-D-glucosamine binding.
{ECO:0000250}.
REGION 308 310 UDP-alpha-D-galactose binding.
{ECO:0000250}.
METAL 215 215 Manganese. {ECO:0000250}.
METAL 308 308 Manganese; via tele nitrogen.
{ECO:0000250}.
BINDING 275 275 UDP-alpha-D-galactose. {ECO:0000250}.
BINDING 320 320 N-acetyl-D-glucosamine. {ECO:0000250}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 94 136 {ECO:0000250}.
DISULFID 208 227 {ECO:0000250}.
SEQUENCE 369 AA; 41909 MW; EF4465AFE51C6C30 CRC64;
MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDVYAQHLA FFSRFSTRSP AHALYPAASS
STNCSRPNAT AASSGLPEVP SARPGPTAPV IPPCPDVPPG LVGRVVIEFT SPMPLERVQR
ENPGVLLGGR YSPPDCTPAQ TVAVIIPFRH REHHLRYWLH YLHPMLRRQR LRYGVYVINQ
HGEETFNRAK LLNVGFLEAL KEDAAYDCFI FSDVDLVPMD DRNLYRCGDQ PRHFAIAMDK
FGFRLPYASY FGGVSGLSKA QFLRINGFPN EYWGWGGEDD DIFNRISLTG MKISRPDVRI
GRYRMIKHDR DKHNEPNPQR FNKIQNTKMS MKWDGIGSVR YRVLEVSRQP LFTNITVDIG
QPMSWLTQG


Related products :

Catalog number Product name Quantity
EIAAB07054 2-hydroxyacylsphingosine 1-beta-galactosyltransferase,Ceramide UDP-galactosyltransferase,Cerebroside synthase,Cgt,Rat,Rattus norvegicus,UDP-galactose-ceramide galactosyltransferase,Ugt4,Ugt8
EIAAB07053 2-hydroxyacylsphingosine 1-beta-galactosyltransferase,Ceramide UDP-galactosyltransferase,Cerebroside synthase,Cgt,Mouse,Mus musculus,UDP-galactose-ceramide galactosyltransferase,Ugt4,Ugt8,Ugt8a
EIAAB07055 2-hydroxyacylsphingosine 1-beta-galactosyltransferase,Ceramide UDP-galactosyltransferase,Cerebroside synthase,CGT,Homo sapiens,Human,UDP-galactose-ceramide galactosyltransferase,UGT4,UGT8
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
201-20-0575 B4GALT7{xylosylprotein beta 1,4-galactosyltransferase, polypeptide 7 (galactosyltransferase I)}rabbit.pAb 0.1ml
B9D1 B4GALT7 Gene xylosylprotein beta 1,4-galactosyltransferase, polypeptide 7 (galactosyltransferase I)
GS-0170a xylosylprotein beta 1,4-galactosyltransferase, polypeptide 7 (galactosyltransferase I) primary antibody, Host: Rabbit 200ul
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
C1HR C1GALT1 Gene core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1
CSB-EL003489RA Rat core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1 (C1GALT1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL003489CH Chicken core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1 (C1GALT1) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL003489HU Human core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1 (C1GALT1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL003489MO Mouse core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1 (C1GALT1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL003489BO Bovine core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1 (C1GALT1) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
PE007044h Recombinant human Beta-1,4-galactosyltransferase 3 protein 5mg
PE007044h Recombinant human Beta-1,4-galactosyltransferase 3 protein 1mg
PE007044h Recombinant human Beta-1,4-galactosyltransferase 3 protein 200ug
PE007044h Recombinant human Beta-1,4-galactosyltransferase 3 protein 50ug
'H00008704-P01-02 Beta-1,4-Galactosyltransferase 2 antigen 2
EH2226 Beta-1,4-galactosyltransferase 5 Elisa Kit 96T
B3GT4_CANFA Dog ELISA Kit FOR Beta-1,3-galactosyltransferase 4 96T
EM815 Beta-1,4-galactosyltransferase 1 Elisa Kit 96T
EH1330 Beta-1,3-galactosyltransferase 2 Elisa Kit 96T
EH1329 Beta-1,3-galactosyltransferase 1 Elisa Kit 96T
B4GT4_MOUSE Mouse ELISA Kit FOR Beta-1,4-galactosyltransferase 4 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