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

Polypeptide N-acetylgalactosaminyltransferase 15 (EC 2.4.1.41) (Polypeptide GalNAc transferase-like protein 2) (GalNAc-T-like protein 2) (pp-GaNTase-like protein 2) (Polypeptide N-acetylgalactosaminyltransferase-like protein 2) (Protein-UDP acetylgalactosaminyltransferase-like protein 2) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2)

 GLT15_HUMAN             Reviewed;         639 AA.
Q8N3T1; A6NMN1; B2R638; F1LIP6; Q86T60; Q96C46; Q96DJ5;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
25-OCT-2017, entry version 132.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 15;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase-like protein 2;
Short=GalNAc-T-like protein 2;
Short=pp-GaNTase-like protein 2;
AltName: Full=Polypeptide N-acetylgalactosaminyltransferase-like protein 2;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase-like protein 2;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2;
Name=GALNT15; Synonyms=GALNTL2; ORFNames=UNQ770/PRO1564;
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=15147861; DOI=10.1016/j.febslet.2004.03.108;
Cheng L., Tachibana K., Iwasaki H., Kameyama A., Zhang Y., Kubota T.,
Hiruma T., Tachibana K., Kudo T., Guo J.-M., Narimatsu H.;
"Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-
T15.";
FEBS Lett. 566:17-24(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
TISSUE=Osteoarthritic cartilage;
PubMed=11597177; DOI=10.1053/joca.2001.0421;
Kumar S., Connor J.R., Dodds R.A., Halsey W., Van Horn M., Mao J.,
Sathe G.M., Mui P., Agarwal P., Badger A.M., Lee J.C., Gowen M.,
Lark M.W.;
"Identification and initial characterization of 5000 expressed
sequenced tags (ESTs) each from adult human normal and osteoarthritic
cartilage cDNA libraries.";
Osteoarthritis Cartilage 9:641-653(2001).
[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=Brain;
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 MRNA], AND VARIANT THR-432.
TISSUE=Adipose tissue, and Spinal cord;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-432.
Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
-!- FUNCTION: Catalyzes the initial reaction in O-linked
oligosaccharide biosynthesis, the transfer of an N-acetyl-D-
galactosamine residue to a serine or threonine residue on the
protein receptor. Although it displays a much weaker activity
toward all substrates tested compared to GALNT2, it is able to
transfer up to seven GalNAc residues to the Muc5AC peptide,
suggesting that it can fill vicinal Thr/Ser residues in
cooperation with other GALNT proteins. Prefers Muc1a as substrate.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
{ECO:0000269|PubMed:15147861}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in small
intestine, placenta, spleen, cerebral cortex and ovary. Expressed
at intermediate level in uterus, mammary gland, stomach,
cerebellum and whole brain. Weakly expressed in fetal brain, bone
marrow, thyroid gland, thymus, heart, skeletal muscle, lung,
liver, colon, pancreas, kidney and testis. Not expressed in
leukocyte. Expressed in both normal and osteoarthritic cartilage.
Expressed at low level in chondrocytes in all zones of both normal
and osteoarthritic cartilage. {ECO:0000269|PubMed:11597177,
ECO:0000269|PubMed:15147861}.
-!- DOMAIN: There are two conserved domains in the glycosyltransferase
region: the N-terminal domain (domain A, also called GT1 motif),
which is probably involved in manganese coordination and substrate
binding and the C-terminal domain (domain B, also called
Gal/GalNAc-T motif), which is probably involved in catalytic
reaction and UDP-Gal binding. {ECO:0000250}.
-!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
contributes to the glycopeptide specificity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-!- CAUTION: Was originally termed Galnt15/pp-GaNTase 15.
{ECO:0000305|PubMed:15147861}.
-!- SEQUENCE CAUTION:
Sequence=CAD89983.1; Type=Frameshift; Positions=169, 192, 206, 222, 270; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Polypeptide N-acetylgalactosaminyltransferase-like protein 2;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_501";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB078149; BAD29961.1; -; mRNA.
EMBL; AY035399; AAK63127.1; -; mRNA.
EMBL; AY358443; AAQ88808.1; -; mRNA.
EMBL; AK312425; BAG35335.1; -; mRNA.
EMBL; AL831925; CAD38585.1; -; mRNA.
EMBL; AL832575; CAD89983.1; ALT_FRAME; mRNA.
EMBL; AC087858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64266.1; -; Genomic_DNA.
EMBL; BC014789; AAH14789.1; -; mRNA.
CCDS; CCDS33711.1; -.
RefSeq; NP_473451.3; NM_054110.4.
UniGene; Hs.411308; -.
ProteinModelPortal; Q8N3T1; -.
SMR; Q8N3T1; -.
BioGrid; 125583; 1.
IntAct; Q8N3T1; 2.
MINT; MINT-4724072; -.
STRING; 9606.ENSP00000344260; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
PhosphoSitePlus; Q8N3T1; -.
BioMuta; GALNT15; -.
DMDM; 51316023; -.
PaxDb; Q8N3T1; -.
PeptideAtlas; Q8N3T1; -.
PRIDE; Q8N3T1; -.
DNASU; 117248; -.
Ensembl; ENST00000339732; ENSP00000344260; ENSG00000131386.
GeneID; 117248; -.
KEGG; hsa:117248; -.
UCSC; uc003car.5; human.
CTD; 117248; -.
DisGeNET; 117248; -.
EuPathDB; HostDB:ENSG00000131386.17; -.
GeneCards; GALNT15; -.
HGNC; HGNC:21531; GALNT15.
HPA; HPA017076; -.
HPA; HPA051551; -.
MIM; 615131; gene.
neXtProt; NX_Q8N3T1; -.
OpenTargets; ENSG00000131386; -.
PharmGKB; PA134936170; -.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00900000140827; -.
HOGENOM; HOG000038227; -.
HOVERGEN; HBG051699; -.
InParanoid; Q8N3T1; -.
KO; K00710; -.
OMA; ETWLGSF; -.
OrthoDB; EOG091G04OC; -.
PhylomeDB; Q8N3T1; -.
TreeFam; TF313267; -.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
GeneWiki; GALNTL2; -.
GenomeRNAi; 117248; -.
PRO; PR:Q8N3T1; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000131386; -.
CleanEx; HS_GALNTL2; -.
ExpressionAtlas; Q8N3T1; baseline and differential.
Genevisible; Q8N3T1; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030133; C:transport vesicle; IDA:LIFEdb.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; TAS:Reactome.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
CDD; cd00161; RICIN; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00535; Glycos_transf_2; 1.
Pfam; PF00652; Ricin_B_lectin; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
Polymorphism; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 639 Polypeptide N-
acetylgalactosaminyltransferase 15.
/FTId=PRO_0000059137.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.
TRANSMEM 12 34 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 35 639 Lumenal. {ECO:0000255}.
DOMAIN 504 631 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 190 299 Catalytic subdomain A.
REGION 358 420 Catalytic subdomain B.
METAL 283 283 Manganese. {ECO:0000250}.
METAL 285 285 Manganese. {ECO:0000250}.
METAL 417 417 Manganese. {ECO:0000250}.
BINDING 231 231 Substrate. {ECO:0000250}.
BINDING 260 260 Substrate. {ECO:0000250}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 574 574 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 181 412 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 403 482 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 517 536 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 562 575 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 603 620 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VARIANT 68 68 V -> G (in dbSNP:rs36026882).
/FTId=VAR_049243.
VARIANT 151 151 P -> L (in dbSNP:rs11715981).
/FTId=VAR_049244.
VARIANT 324 324 P -> A (in dbSNP:rs12634179).
/FTId=VAR_049245.
VARIANT 432 432 A -> T (in dbSNP:rs17851238).
{ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.7}.
/FTId=VAR_049246.
VARIANT 510 510 H -> Y (in dbSNP:rs2271077).
/FTId=VAR_019593.
CONFLICT 44 44 V -> D (in Ref. 5; CAD38585).
{ECO:0000305}.
CONFLICT 326 326 K -> R (in Ref. 5; CAD89983).
{ECO:0000305}.
SEQUENCE 639 AA; 73063 MW; F5DCA523AF4965DA CRC64;
MLLRKRYRHR PCRLQFLLLL LMLGCVLMMV AMLHPPHHTL HQTVTAQASK HSPEARYRLD
FGESQDWVLE AEDEGEEYSP LEGLPPFISL REDQLLVAVA LPQARRNQSQ GRRGGSYRLI
KQPRRQDKEA PKRDWGADED GEVSEEEELT PFSLDPRGLQ EALSARIPLQ RALPEVRHPL
CLQQHPQDSL PTASVILCFH DEAWSTLLRT VHSILDTVPR AFLKEIILVD DLSQQGQLKS
ALSEYVARLE GVKLLRSNKR LGAIRARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI
AGDRSRVVSP VIDVIDWKTF QYYPSKDLQR GVLDWKLDFH WEPLPEHVRK ALQSPISPIR
SPVVPGEVVA MDRHYFQNTG AYDSLMSLRG GENLELSFKA WLCGGSVEIL PCSRVGHIYQ
NQDSHSPLDQ EATLRNRVRI AETWLGSFKE TFYKHSPEAF SLSKAEKPDC MERLQLQRRL
GCRTFHWFLA NVYPELYPSE PRPSFSGKLH NTGLGLCADC QAEGDILGCP MVLAPCSDSR
QQQYLQHTSR KEIHFGSPQH LCFAVRQEQV ILQNCTEEGL AIHQQHWDFQ ENGMIVHILS
GKCMEAVVQE NNKDLYLRPC DGKARQQWRF DQINAVDER


Related products :

Catalog number Product name Quantity
26-349 GALNT10 belongs to the polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family. Polypeptide GalNAc transferases initiate the synthesis of mucin-type oligosaccharides by transferring GalNAc 0.05 mg
30-452 GALNT10 belongs to the polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family. Polypeptide GalNAc transferases initiate the synthesis of mucin-type oligosaccharides by transferring GalNAc 0.05 mg
30-240 GALNT6 is a member of the UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Gol 0.1 mg
26-171 GALNT6 is a member of the UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. GalNAc-Ts initiate mucin-type O-linked glycosylation in the Gol 0.05 mg
GALNT14 GALNT12 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 12 (GalNAc-T12)
GALNT8 GALNT6 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 6 (GalNAc-T6)
GALNT3 GALNT14 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 14 (GalNAc-T14)
GALNT4 GALNT2 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)
GALNT6 GALNT4 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 4 (GalNAc-T4)
GALNT7 GALNT5 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5)
GALNT9 GALNT7 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 7 (GalNAc-T7)
GALNTL1 GALNT8 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 8 (GalNAc-T8)
201-20-2178 GALNT7{UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 7 (GalNAc-T7)}rabbit.pAb 0.2ml
GALNT11 GALNT1 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)
201-20-2176 GALNT14{UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 14 (GalNAc-T14)}rabbit.pAb 0.2ml
GALNT13 GALNT11 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 11 (GalNAc-T11)
GALNT5 GALNT3 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 3 (GalNAc-T3)
GALNTL2 GALNT9 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 9 (GalNAc-T9)
GALNT12 GALNT10 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 10 (GalNAc-T10)
201-20-2177 GALNT4{UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 4 (GalNAc-T4)}rabbit.pAb 0.2ml
GALNT2 GALNT13 Gene UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 13 (GalNAc-T13)
CSB-EL009205RA Rat UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 11 (GalNAc-T11) (GALNT11) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL009204RA Rat UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 10 (GalNAc-T10) (GALNT10) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL009212RA Rat UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5) (GALNT5) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL009203PI Pig UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1) (GALNT1) ELISA kit, Species Pig, Sample Type serum, plasma 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