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Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6 (EC 2.4.99.-) (GalNAc alpha-2,6-sialyltransferase VI) (ST6GalNAc VI) (ST6GalNAcVI) (hST6GalNAc VI) (Sialyltransferase 7F) (SIAT7-F)

 SIA7F_HUMAN             Reviewed;         333 AA.
Q969X2; B3KQ01; Q5T9C4; Q5T9C5; Q9H8A2; Q9ULB8;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
20-JUN-2018, entry version 132.
RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6;
EC=2.4.99.-;
AltName: Full=GalNAc alpha-2,6-sialyltransferase VI;
AltName: Full=ST6GalNAc VI;
Short=ST6GalNAcVI;
Short=hST6GalNAc VI;
AltName: Full=Sialyltransferase 7F;
Short=SIAT7-F;
Name=ST6GALNAC6; Synonyms=SIAT7F; ORFNames=UNQ708/PRO1359;
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 2), FUNCTION, ENZYME ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=12668675; DOI=10.1074/jbc.M211034200;
Tsuchida A., Okajima T., Furukawa K., Ando T., Ishida H., Yoshida A.,
Nakamura Y., Kannagi R., Kiso M., Furukawa K.;
"Synthesis of disialyl Lewis a (Le(a)) structure in colon cancer cell
lines by a sialyltransferase, ST6GalNAc VI, responsible for the
synthesis of alpha-series gangliosides.";
J. Biol. Chem. 278:22787-22794(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=15843597; DOI=10.1093/glycob/cwi063;
Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.;
"The animal sialyltransferases and sialyltransferase-related genes: a
phylogenetic approach.";
Glycobiology 15:805-817(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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] (ISOFORMS 1 AND 2).
TISSUE=Small intestine, and Thyroid;
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] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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] (ISOFORMS 1 AND 3).
TISSUE=Brain, and Muscle;
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]
IDENTIFICATION.
PubMed=16207893; DOI=10.1093/glycob/cwj046;
Patel R.Y., Balaji P.V.;
"Identification of linkage-specific sequence motifs in
sialyltransferases.";
Glycobiology 16:108-116(2006).
[10]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17123352; DOI=10.1042/BJ20061118;
Senda M., Ito A., Tsuchida A., Hagiwara T., Kaneda T., Nakamura Y.,
Kasama K., Kiso M., Yoshikawa K., Katagiri Y., Ono Y., Ogiso M.,
Urano T., Furukawa K., Oshima S., Furukawa K.;
"Identification and expression of a sialyltransferase responsible for
the synthesis of disialylgalactosylgloboside in normal and malignant
kidney cells: downregulation of ST6GalNAc VI in renal cancers.";
Biochem. J. 402:459-470(2007).
[11]
REVIEW ON SIALYL LEWIS ANTIGENS.
PubMed=17760270;
Kannagi R.;
"Carbohydrate antigen sialyl Lewis a - its pathophysiological
significance and induction mechanism in cancer progression.";
Chang Gung Med. J. 30:189-209(2007).
-!- FUNCTION: Alpha-2,6-sialyltransferase involved in the synthesis of
alpha-series gangliosides. Has activity toward GD1a, GT1b and
GM1b. Has no activity toward glycoproteins. Responsible for the
biosynthesis of DSGG (disialylgalactosylgloboside) from MSGG
(monosialylgalactosylgloboside) in normal and malignant kidney.
Participates in the synthesis of disialyl Lewis a (Le(a)).
{ECO:0000269|PubMed:12668675, ECO:0000269|PubMed:17123352}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.33 mM for GM1b {ECO:0000269|PubMed:12668675};
KM=0.46 mM for sialyl-Lc4 {ECO:0000269|PubMed:12668675};
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q969X2-1; Sequence=Displayed;
Name=2;
IsoId=Q969X2-2; Sequence=VSP_030359;
Name=3;
IsoId=Q969X2-3; Sequence=VSP_055722;
-!- TISSUE SPECIFICITY: Expressed in kidney, in proximal tubule
epithelial cells. Expressed in colon cell lines.
{ECO:0000269|PubMed:12668675, ECO:0000269|PubMed:17123352}.
-!- INDUCTION: Down-regulated in renal cancers.
-!- MISCELLANEOUS: The carbohydrate antigen disialyl Lewis a, which is
at least partly synthesized by ST6GALNAC6, is a normal counterpart
of sialyl Lewis a, better known as CA19-9, an antigen widely used
as a serum marker for diagnosis of cancers in the digestive track.
Disialyl Lewis a is predominantly expressed in non-malignant
epithelial cells of the digestive organs, while sialyl Lewis a is
preferentially expressed in cancers. Disialyl Lewis a in normal
epithelial cells serves as a ligand for immunosuppressive
receptors, such as SIGLEC7 and SIGLEC9, expressed on resident
monocytes/macrophages and maintains immunological homeostasis of
mucosal membranes in digestive organs. Sialyl Lewis a, as well as
its positional isomer sialyl Lewis x, serves as a ligand for
vascular cell adhesion molecule E-selectin and facilitates
hematogenous metastasis through mediating adhesion of circulating
cancer cells to vascular endothelium (PubMed:17760270).
{ECO:0000305|PubMed:17760270}.
-!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI12610.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI12611.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAW87712.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=ST6GalNAc VI;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_635";
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EMBL; AJ507293; CAD45373.1; -; mRNA.
EMBL; AB035173; BAA87035.1; -; mRNA.
EMBL; AY358672; AAQ89035.1; -; mRNA.
EMBL; AK023900; BAB14715.1; -; mRNA.
EMBL; AK057100; BAG51863.1; -; mRNA.
EMBL; CR457318; CAG33599.1; -; mRNA.
EMBL; AL157935; CAI12609.1; -; Genomic_DNA.
EMBL; AL157935; CAI12610.1; ALT_SEQ; Genomic_DNA.
EMBL; AL157935; CAI12611.1; ALT_SEQ; Genomic_DNA.
EMBL; AL157935; CAI12612.1; -; Genomic_DNA.
EMBL; CH471090; EAW87711.1; -; Genomic_DNA.
EMBL; CH471090; EAW87712.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471090; EAW87714.1; -; Genomic_DNA.
EMBL; BC006564; AAH06564.1; -; mRNA.
EMBL; BC007802; AAH07802.1; -; mRNA.
EMBL; BC016299; AAH16299.1; -; mRNA.
EMBL; BC036102; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS6882.1; -. [Q969X2-1]
CCDS; CCDS69668.1; -. [Q969X2-2]
CCDS; CCDS69669.1; -. [Q969X2-3]
RefSeq; NP_001273928.1; NM_001286999.1. [Q969X2-3]
RefSeq; NP_001273929.1; NM_001287000.1. [Q969X2-2]
RefSeq; NP_001273930.1; NM_001287001.1. [Q969X2-2]
RefSeq; NP_001273931.1; NM_001287002.1. [Q969X2-2]
RefSeq; NP_001273932.1; NM_001287003.1.
RefSeq; NP_038471.2; NM_013443.4. [Q969X2-1]
RefSeq; XP_011516912.1; XM_011518610.2. [Q969X2-1]
RefSeq; XP_011516913.1; XM_011518611.2. [Q969X2-2]
RefSeq; XP_016870148.1; XM_017014659.1. [Q969X2-3]
RefSeq; XP_016870154.1; XM_017014665.1. [Q969X2-2]
RefSeq; XP_016870155.1; XM_017014666.1. [Q969X2-2]
RefSeq; XP_016870156.1; XM_017014667.1. [Q969X2-2]
UniGene; Hs.109672; -.
ProteinModelPortal; Q969X2; -.
SMR; Q969X2; -.
BioGrid; 119039; 3.
IntAct; Q969X2; 4.
STRING; 9606.ENSP00000291839; -.
SwissLipids; SLP:000001366; -.
CAZy; GT29; Glycosyltransferase Family 29.
iPTMnet; Q969X2; -.
PhosphoSitePlus; Q969X2; -.
DMDM; 74751728; -.
PaxDb; Q969X2; -.
PeptideAtlas; Q969X2; -.
PRIDE; Q969X2; -.
ProteomicsDB; 75868; -.
ProteomicsDB; 75869; -. [Q969X2-2]
DNASU; 30815; -.
Ensembl; ENST00000291839; ENSP00000291839; ENSG00000160408. [Q969X2-1]
Ensembl; ENST00000373141; ENSP00000362234; ENSG00000160408. [Q969X2-2]
Ensembl; ENST00000373142; ENSP00000362235; ENSG00000160408. [Q969X2-3]
Ensembl; ENST00000373144; ENSP00000362237; ENSG00000160408. [Q969X2-2]
Ensembl; ENST00000373146; ENSP00000362239; ENSG00000160408. [Q969X2-1]
Ensembl; ENST00000622357; ENSP00000477575; ENSG00000160408. [Q969X2-2]
GeneID; 30815; -.
KEGG; hsa:30815; -.
UCSC; uc004bsn.3; human. [Q969X2-1]
CTD; 30815; -.
DisGeNET; 30815; -.
EuPathDB; HostDB:ENSG00000160408.14; -.
GeneCards; ST6GALNAC6; -.
H-InvDB; HIX0008413; -.
HGNC; HGNC:23364; ST6GALNAC6.
HPA; HPA018890; -.
MIM; 610135; gene.
neXtProt; NX_Q969X2; -.
OpenTargets; ENSG00000160408; -.
OpenTargets; ENSG00000257524; -.
PharmGKB; PA134891331; -.
eggNOG; KOG2692; Eukaryota.
eggNOG; ENOG410XT8P; LUCA.
GeneTree; ENSGT00550000074444; -.
HOGENOM; HOG000293316; -.
HOVERGEN; HBG058710; -.
InParanoid; Q969X2; -.
KO; K03376; -.
OMA; RKGNHHR; -.
OrthoDB; EOG091G0H9S; -.
PhylomeDB; Q969X2; -.
TreeFam; TF323961; -.
BRENDA; 2.4.99.7; 2681.
Reactome; R-HSA-4085001; Sialic acid metabolism.
ChiTaRS; ST6GALNAC6; human.
GeneWiki; ST6GALNAC6; -.
GenomeRNAi; 30815; -.
PRO; PR:Q969X2; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000160408; -.
CleanEx; HS_ST6GALNAC6; -.
ExpressionAtlas; Q969X2; baseline and differential.
Genevisible; Q969X2; HS.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
GO; GO:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; ISS:BHF-UCL.
GO; GO:0008373; F:sialyltransferase activity; IDA:BHF-UCL.
GO; GO:0009988; P:cell-cell recognition; IC:BHF-UCL.
GO; GO:0001574; P:ganglioside biosynthetic process; ISS:BHF-UCL.
GO; GO:0009100; P:glycoprotein metabolic process; IDA:BHF-UCL.
GO; GO:0006687; P:glycosphingolipid metabolic process; IDA:BHF-UCL.
GO; GO:0006677; P:glycosylceramide metabolic process; IDA:BHF-UCL.
GO; GO:0009312; P:oligosaccharide biosynthetic process; ISS:BHF-UCL.
GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IBA:GO_Central.
Gene3D; 3.90.1480.20; -; 1.
InterPro; IPR001675; Glyco_trans_29.
InterPro; IPR038578; GT29-like_sf.
InterPro; IPR012163; Sialyl_trans.
Pfam; PF00777; Glyco_transf_29; 1.
PIRSF; PIRSF005557; Sialyl_trans; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 333 Alpha-N-acetylgalactosaminide alpha-2,6-
sialyltransferase 6.
/FTId=PRO_0000314795.
TOPO_DOM 1 43 Cytoplasmic. {ECO:0000255}.
TRANSMEM 44 64 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 65 333 Lumenal. {ECO:0000255}.
COMPBIAS 30 33 Poly-Arg.
COMPBIAS 112 115 Poly-Ser.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 108 256 {ECO:0000250}.
VAR_SEQ 1 34 Missing (in isoform 2).
{ECO:0000303|PubMed:12668675,
ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15843597,
ECO:0000303|Ref.5}.
/FTId=VSP_030359.
VAR_SEQ 272 333 QRPRLQRMPYHYYEPKGPDECVTYIQNEHSRKGNHHRFITE
KRVFSSWAQLYGITFSHPSWT -> GPASSACPTTTTSPRG
RTNVSPTSRMSTVARATTTASSPRKGSSHRGPSCMASPSPT
PPGPRPPSLWDLRRVRGEAASAQPLGQGPSSGQSRLAGVSP
SQSGP (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055722.
CONFLICT 73 73 L -> M (in Ref. 8; BC036102).
{ECO:0000305}.
CONFLICT 174 174 R -> Q (in Ref. 8; BC036102).
{ECO:0000305}.
CONFLICT 228 228 R -> Q (in Ref. 8; BC036102).
{ECO:0000305}.
CONFLICT 249 249 M -> T (in Ref. 3; BAB14715).
{ECO:0000305}.
SEQUENCE 333 AA; 38068 MW; 5DB6FFA7D7A707C0 CRC64;
MACSRPPSQC EPTSLPPGPP AGRRHLPLSR RRREMSSNKE QRSAVFVILF ALITILILYS
SNSANEVFHY GSLRGRSRRP VNLKKWSITD GYVPILGNKT LPSRCHQCVI VSSSSHLLGT
KLGPEIERAE CTIRMNDAPT TGYSADVGNK TTYRVVAHSS VFRVLRRPQE FVNRTPETVF
IFWGPPSKMQ KPQGSLVRVI QRAGLVFPNM EAYAVSPGRM RQFDDLFRGE TGKDREKSHS
WLSTGWFTMV IAVELCDHVH VYGMVPPNYC SQRPRLQRMP YHYYEPKGPD ECVTYIQNEH
SRKGNHHRFI TEKRVFSSWA QLYGITFSHP SWT


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EIAAB38398 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5,GalNAc alpha-2,6-sialyltransferase V,GD1 alpha synthase,Homo sapiens,Human,Sialyltransferase 7E,SIAT7E,SIAT7-E,ST6GalNAc V,ST6GALNAC5,ST6Gal
EIAAB38397 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5,GalNAc alpha-2,6-sialyltransferase V,GD1 alpha synthase,Mouse,Mus musculus,Sialyltransferase 7E,Siat7e,SIAT7-E,ST6GalNAc V,St6galnac5,ST6Gal
EIAAB38387 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1,GalNAc alpha-2,6-sialyltransferase I,Homo sapiens,Human,Sialyltransferase 7A,SIAT7A,SIAT7-A,ST6GalNAc I,ST6GALNAC1,ST6GalNAcI,UNQ543_PRO848
EIAAB38394 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3,GalNAc alpha-2,6-sialyltransferase III,Homo sapiens,Human,Sialyltransferase 7C,SIAT7C,SIAT7-C,ST6GalNAc III,ST6GALNAC3,ST6GalNAcIII,STY,UNQ2
EIAAB38391 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2,GalNAc alpha-2,6-sialyltransferase II,Homo sapiens,Human,Sialyltransferase 7B,SIAT7B,SIAT7-B,SIATL1,ST6GalNAc II,ST6GALNAC2,ST6GalNAcII,SThM
EIAAB38392 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3,GalNAc alpha-2,6-sialyltransferase III,Rat,Rattus norvegicus,Sialyltransferase 7C,Siat7c,SIAT7-C,ST6GalNAc III,St6galnac3,ST6GalNAcIII,STY
EIAAB38393 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3,GalNAc alpha-2,6-sialyltransferase III,Mouse,Mus musculus,Sialyltransferase 7C,Siat7c,SIAT7-C,ST6GalNAc III,St6galnac3,ST6GalNAcIII,STY
EIAAB38388 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1,GalNAc alpha-2,6-sialyltransferase I,Mouse,Mus musculus,Sialyltransferase 7A,Siat7a,SIAT7-A,ST6GalNAc I,St6galnac1,ST6GalNAcI
EIAAB38386 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1,Chicken,Gallus gallus,GalNAc alpha-2,6-sialyltransferase I,Sialyltransferase 7A,SIAT7A,SIAT7-A,ST6GalNAc I,ST6GALNAC1,ST6GalNAcI
EIAAB38390 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2,Gal-beta-1,3-GalNAc alpha-2,6-sialyltransferase,GalNAc alpha-2,6-sialyltransferase II,Mouse,Mus musculus,Sialyltransferase 7B,Siat7,Siat7b,S
EIAAB38389 Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 2,Chicken,Gal-beta-1,3-GalNAc alpha-2,6-sialyltransferase,Gallus gallus,GalNAc alpha-2,6-sialyltransferase II,Sialyltransferase 7B,SIAT7B,SIAT
EIAAB38408 Alpha-2,8-sialyltransferase 8C,Alpha-2,8-sialyltransferase III,Homo sapiens,Human,Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R alpha 2,8-sialyltransferase,Sialyltransferase 8C,Sialytransferase St8Sia III,SIAT8
EIAAB38409 Alpha-2,8-sialyltransferase 8C,Alpha-2,8-sialyltransferase III,Mouse,Mus musculus,Sia-alpha-2,3-Gal-beta-1,4-GlcNAc-R alpha 2,8-sialyltransferase,Sialyltransferase 8C,Sialytransferase St8Sia III,Siat8
EIAAB38382 Alpha 2,3-ST 2,Beta-galactoside alpha-2,3-sialyltransferase 2,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Homo sa
EIAAB38377 Alpha 2,3-ST 1,Beta-galactoside alpha-2,3-sialyltransferase 1,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Homo sa
EIAAB38379 Alpha 2,3-ST 1,Beta-galactoside alpha-2,3-sialyltransferase 1,Chicken,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gallus ga
EIAAB38376 Alpha 2,3-ST 1,Beta-galactoside alpha-2,3-sialyltransferase 1,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Mouse,M
EIAAB38381 Alpha 2,3-ST 2,Beta-galactoside alpha-2,3-sialyltransferase 2,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Mouse,M
EIAAB38383 Alpha 2,3-sialyltransferase IV,Alpha 2,3-ST 4,Beta-galactoside alpha-2,3-sialyltransferase 4,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4,Gal-beta-1,4-GalNAc-alpha-2,3-sial
EIAAB38384 Alpha 2,3-sialyltransferase IV,Alpha 2,3-ST 4,Beta-galactoside alpha-2,3-sialyltransferase 4,CGS23,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4,Gal-beta-1,4-GalNAc-alpha-2,
EIAAB38385 Alpha 2,3-sialyltransferase IV,Alpha 2,3-ST 4,Beta-galactoside alpha-2,3-sialyltransferase 4,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4,Gal-beta-1,4-GalNAc-alpha-2,3-sial
EIAAB38378 Alpha 2,3-ST 1,Beta-galactoside alpha-2,3-sialyltransferase 1,CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1,Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase,Gal-NAc6S,Pig,Sia


 

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