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Neuraminidase (EC 3.2.1.18)

 NRAM_I75A5              Reviewed;         470 AA.
P03472; Q84070;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 137.
RecName: Full=Neuraminidase {ECO:0000255|HAMAP-Rule:MF_04071};
EC=3.2.1.18 {ECO:0000255|HAMAP-Rule:MF_04071};
Name=NA {ECO:0000255|HAMAP-Rule:MF_04071};
Influenza A virus (strain A/Tern/Australia/G70C/1975 H11N9).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=384509;
NCBI_TaxID=8782; Aves.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=4013081; DOI=10.1016/0042-6822(85)90206-5;
Air G.M., Ritchie L.R., Laver W.G., Colman P.M.;
"Gene and protein sequence of an influenza neuraminidase with
hemagglutinin activity.";
Virology 145:117-122(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3660585; DOI=10.1016/0042-6822(87)90005-5;
Air G.M., Webster R.G., Colman P.M., Laver W.G.;
"Distribution of sequence differences in influenza N9 neuraminidase of
tern and whale viruses and crystallization of the whale neuraminidase
complexed with antibodies.";
Virology 160:346-354(1987).
[3]
REVIEW.
PubMed=15567494; DOI=10.1016/j.virusres.2004.08.012;
Nayak D.P., Hui E.K., Barman S.;
"Assembly and budding of influenza virus.";
Virus Res. 106:147-165(2004).
[4]
REVIEW.
PubMed=16192481; DOI=10.1056/NEJMra050740;
Moscona A.;
"Neuraminidase inhibitors for influenza.";
N. Engl. J. Med. 353:1363-1373(2005).
[5]
REVIEW.
PubMed=15744059; DOI=10.1248/bpb.28.399;
Suzuki Y.;
"Sialobiology of influenza: molecular mechanism of host range
variation of influenza viruses.";
Biol. Pharm. Bull. 28:399-408(2005).
[6]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 83-470.
PubMed=3447170; DOI=10.1002/prot.340020205;
Baker A.T., Varghese J.N., Laver W.G., Air G.M., Colman P.M.;
"Three-dimensional structure of neuraminidase of subtype N9 from an
avian influenza virus.";
Proteins 2:111-117(1987).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 83-470 IN COMPLEX WITH
CALCIUM AND SUBSTRATE ANALOG, DISULFIDE BOND, ACTIVE SITE, COFACTOR,
AND SUBUNIT.
PubMed=8371267; DOI=10.1006/jmbi.1993.1461;
Bossart-Whitaker P., Carson M., Babu Y.S., Smith C.D., Laver W.G.,
Air G.M.;
"Three-dimensional structure of influenza A N9 neuraminidase and its
complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic
acid.";
J. Mol. Biol. 232:1069-1083(1993).
[8]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 83-470 IN COMPLEX WITH
CALCIUM AND SUBSTRATE ANALOG, COFACTOR, DISULFIDE BOND, SUBUNIT, AND
GLYCOSYLATION AT ASN-87; ASN-147 AND ASN-202.
PubMed=7549872; DOI=10.1002/pro.5560040606;
Varghese J.N., Epa V.C., Colman P.M.;
"Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en
and influenza virus neuraminidase.";
Protein Sci. 4:1081-1087(1995).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 83-470 IN COMPLEX WITH
CALCIUM, COFACTOR, ACTIVE SITE, DISULFIDE BOND, AND GLYCOSYLATION AT
ASN-87; ASN-147 AND ASN-202.
PubMed=9342319; DOI=10.1073/pnas.94.22.11808;
Varghese J.N., Colman P.M., van Donkelaar A., Blick T.J.,
Sahasrabudhe A., McKimm-Breschkin J.L.;
"Structural evidence for a second sialic acid binding site in avian
influenza virus neuraminidases.";
Proc. Natl. Acad. Sci. U.S.A. 94:11808-11812(1997).
[10]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 83-470 IN COMPLEX WITH
CALCIUM AND SUBSTRATE ANALOG, CATALYTIC ACTIVITY, ACTIVE SITE,
IDENTIFICATION BY MASS SPECTROMETRY, COFACTOR, ENZYME REGULATION,
DISULFIDE BOND, AND GLYCOSYLATION AT ASN-87; ASN-147 AND ASN-202.
PubMed=23429702; DOI=10.1126/science.1232552;
Kim J.H., Resende R., Wennekes T., Chen H.M., Bance N., Buchini S.,
Watts A.G., Pilling P., Streltsov V.A., Petric M., Liggins R.,
Barrett S., McKimm-Breschkin J.L., Niikura M., Withers S.G.;
"Mechanism-based covalent neuraminidase inhibitors with broad-spectrum
influenza antiviral activity.";
Science 340:71-75(2013).
-!- FUNCTION: Catalyzes the removal of terminal sialic acid residues
from viral and cellular glycoconjugates. Cleaves off the terminal
sialic acids on the glycosylated HA during virus budding to
facilitate virus release. Additionally helps virus spread through
the circulation by further removing sialic acids from the cell
surface. These cleavages prevent self-aggregation and ensure the
efficient spread of the progeny virus from cell to cell.
Otherwise, infection would be limited to one round of replication.
Described as a receptor-destroying enzyme because it cleaves a
terminal sialic acid from the cellular receptors. May facilitate
viral invasion of the upper airways by cleaving the sialic acid
moities on the mucin of the airway epithelial cells. Likely to
plays a role in the budding process through its association with
lipid rafts during intracellular transport. May additionally
display a raft-association independent effect on budding. Plays a
role in the determination of host range restriction on replication
and virulence. Sialidase activity in late endosome/lysosome
traffic seems to enhance virus replication. {ECO:0000255|HAMAP-
Rule:MF_04071}.
-!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,
alpha-(2->8)- glycosidic linkages of terminal sialic acid residues
in oligosaccharides, glycoproteins, glycolipids, colominic acid
and synthetic substrates. {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:23429702}.
-!- COFACTOR:
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:23429702,
ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267,
ECO:0000269|PubMed:9342319};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319};
-!- ENZYME REGULATION: Inhibited by the neuraminidase inhibitors
zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs
interfere with the release of progeny virus from infected cells
and are effective against all influenza strains. Resistance to
neuraminidase inhibitors is quite rare. {ECO:0000255|HAMAP-
Rule:MF_04071, ECO:0000269|PubMed:23429702}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-
Rule:MF_04071}; Single-pass type II membrane protein
{ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates
at the apical plasma membrane in infected polarized epithelial
cells, which is the virus assembly site. Uses lipid rafts for cell
surface transport and apical sorting. In the virion, forms a
mushroom-shaped spike on the surface of the membrane.
{ECO:0000255|HAMAP-Rule:MF_04071}.
-!- DOMAIN: Intact N-terminus is essential for virion morphogenesis.
Possess two apical sorting signals, one in the ectodomain, which
is likely to be a glycan, and the other in the transmembrane
domain. The transmembrane domain also plays a role in lipid raft
association. {ECO:0000255|HAMAP-Rule:MF_04071}.
-!- PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872,
ECO:0000269|PubMed:9342319}.
-!- MISCELLANEOUS: The influenza A genome consist of 8 RNA segments.
Genetic variation of hemagglutinin and/or neuraminidase genes
results in the emergence of new influenza strains. The mechanism
of variation can be the result of point mutations or the result of
genetic reassortment between segments of two different strains.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 34 family.
{ECO:0000255|HAMAP-Rule:MF_04071}.
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EMBL; M11445; AAA43353.1; -; Genomic_RNA.
EMBL; M17813; AAA43574.1; -; Genomic_RNA.
PIR; A00884; NMIV9.
PDB; 1A14; X-ray; 2.50 A; N=83-470.
PDB; 1BJI; X-ray; 2.00 A; A=83-470.
PDB; 1F8B; X-ray; 1.80 A; A=83-470.
PDB; 1F8C; X-ray; 1.70 A; A=83-470.
PDB; 1F8D; X-ray; 1.40 A; A=83-470.
PDB; 1F8E; X-ray; 1.40 A; A=83-470.
PDB; 1INY; X-ray; 2.40 A; A=83-470.
PDB; 1L7F; X-ray; 1.80 A; A=83-470.
PDB; 1L7G; X-ray; 1.85 A; A=83-470.
PDB; 1L7H; X-ray; 1.85 A; A=83-470.
PDB; 1MWE; X-ray; 1.70 A; A=83-470.
PDB; 1NCA; X-ray; 2.50 A; N=82-470.
PDB; 1NCB; X-ray; 2.50 A; N=82-470.
PDB; 1NCC; X-ray; 2.50 A; N=82-470.
PDB; 1NMC; X-ray; 2.50 A; A/N=83-470.
PDB; 1NNA; X-ray; 2.50 A; A=84-470.
PDB; 1NNB; X-ray; 2.80 A; A=84-470.
PDB; 1NNC; X-ray; 1.80 A; A=83-470.
PDB; 1XOE; X-ray; 2.20 A; A=84-470.
PDB; 1XOG; X-ray; 2.80 A; A=84-470.
PDB; 2C4A; X-ray; 2.15 A; A=83-470.
PDB; 2C4L; X-ray; 2.15 A; A=83-470.
PDB; 2QWA; X-ray; 1.70 A; A=83-470.
PDB; 2QWB; X-ray; 2.00 A; A=83-470.
PDB; 2QWC; X-ray; 1.60 A; A=83-470.
PDB; 2QWD; X-ray; 2.00 A; A=83-470.
PDB; 2QWE; X-ray; 2.00 A; A=83-470.
PDB; 2QWF; X-ray; 1.90 A; A=83-470.
PDB; 2QWG; X-ray; 1.80 A; A=83-470.
PDB; 2QWH; X-ray; 1.80 A; A=83-470.
PDB; 2QWI; X-ray; 2.00 A; A=83-470.
PDB; 2QWJ; X-ray; 2.00 A; A=83-470.
PDB; 2QWK; X-ray; 1.80 A; A=83-470.
PDB; 3NN9; X-ray; 2.30 A; A=83-470.
PDB; 3W09; X-ray; 2.00 A; A=83-470.
PDB; 4DGR; X-ray; 1.55 A; A=82-470.
PDB; 4NN9; X-ray; 2.30 A; A=83-470.
PDB; 4WEG; X-ray; 2.10 A; A=83-470.
PDB; 5NN9; X-ray; 2.30 A; A=83-470.
PDB; 6NN9; X-ray; 2.30 A; A=83-470.
PDB; 7NN9; X-ray; 2.00 A; A=83-470.
PDBsum; 1A14; -.
PDBsum; 1BJI; -.
PDBsum; 1F8B; -.
PDBsum; 1F8C; -.
PDBsum; 1F8D; -.
PDBsum; 1F8E; -.
PDBsum; 1INY; -.
PDBsum; 1L7F; -.
PDBsum; 1L7G; -.
PDBsum; 1L7H; -.
PDBsum; 1MWE; -.
PDBsum; 1NCA; -.
PDBsum; 1NCB; -.
PDBsum; 1NCC; -.
PDBsum; 1NMC; -.
PDBsum; 1NNA; -.
PDBsum; 1NNB; -.
PDBsum; 1NNC; -.
PDBsum; 1XOE; -.
PDBsum; 1XOG; -.
PDBsum; 2C4A; -.
PDBsum; 2C4L; -.
PDBsum; 2QWA; -.
PDBsum; 2QWB; -.
PDBsum; 2QWC; -.
PDBsum; 2QWD; -.
PDBsum; 2QWE; -.
PDBsum; 2QWF; -.
PDBsum; 2QWG; -.
PDBsum; 2QWH; -.
PDBsum; 2QWI; -.
PDBsum; 2QWJ; -.
PDBsum; 2QWK; -.
PDBsum; 3NN9; -.
PDBsum; 3W09; -.
PDBsum; 4DGR; -.
PDBsum; 4NN9; -.
PDBsum; 4WEG; -.
PDBsum; 5NN9; -.
PDBsum; 6NN9; -.
PDBsum; 7NN9; -.
ProteinModelPortal; P03472; -.
SMR; P03472; -.
BindingDB; P03472; -.
DrugBank; DB02600; 5-N-Acetyl-3-(1-Ethylpropyl)-1-Cyclohexene-1-Carboxylic Acid.
DrugBank; DB03655; Bcx-1812.
DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
CAZy; GH34; Glycoside Hydrolase Family 34.
iPTMnet; P03472; -.
EvolutionaryTrace; P03472; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0046761; P:viral budding from plasma membrane; IEA:InterPro.
CDD; cd15483; Influenza_NA; 1.
HAMAP; MF_04071; INFV_NRAM; 1.
InterPro; IPR001860; Glyco_hydro_34.
InterPro; IPR033654; Sialidase_Influenza_A/B.
InterPro; IPR036278; Sialidase_sf.
Pfam; PF00064; Neur; 1.
SUPFAM; SSF50939; SSF50939; 1.
1: Evidence at protein level;
3D-structure; Calcium; Disulfide bond; Glycoprotein; Glycosidase;
Host cell membrane; Host membrane; Hydrolase; Membrane; Metal-binding;
Signal-anchor; Transmembrane; Transmembrane helix; Virion.
CHAIN 1 470 Neuraminidase.
/FTId=PRO_0000078721.
TOPO_DOM 1 14 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TRANSMEM 15 35 Helical. {ECO:0000255|HAMAP-
Rule:MF_04071}.
TOPO_DOM 36 470 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04071}.
REGION 11 33 Involved in apical transport and lipid
raft association. {ECO:0000255|HAMAP-
Rule:MF_04071}.
REGION 36 89 Hypervariable stalk region.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 92 470 Head of neuraminidase.
{ECO:0000255|HAMAP-Rule:MF_04071}.
REGION 278 279 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_04071}.
COMPBIAS 345 348 Poly-Asn.
ACT_SITE 152 152 Proton donor/acceptor.
{ECO:0000255|HAMAP-Rule:MF_04071}.
ACT_SITE 406 406 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_04071}.
METAL 295 295 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:23429702,
ECO:0000269|PubMed:7549872,
ECO:0000269|PubMed:8371267,
ECO:0000269|PubMed:9342319}.
METAL 299 299 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:23429702,
ECO:0000269|PubMed:7549872,
ECO:0000269|PubMed:8371267,
ECO:0000269|PubMed:9342319}.
METAL 326 326 Calcium. {ECO:0000255|HAMAP-
Rule:MF_04071,
ECO:0000269|PubMed:23429702,
ECO:0000269|PubMed:7549872,
ECO:0000269|PubMed:8371267,
ECO:0000269|PubMed:9342319}.
METAL 348 348 Calcium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:23429702,
ECO:0000269|PubMed:7549872,
ECO:0000269|PubMed:8371267,
ECO:0000269|PubMed:9342319}.
BINDING 119 119 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 153 153 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 294 294 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
BINDING 372 372 Substrate. {ECO:0000255|HAMAP-
Rule:MF_04071}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:23429702,
ECO:0000269|PubMed:7549872,
ECO:0000269|PubMed:9342319}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:23429702,
ECO:0000269|PubMed:7549872,
ECO:0000269|PubMed:9342319}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04071,
ECO:0000269|PubMed:23429702,
ECO:0000269|PubMed:7549872,
ECO:0000269|PubMed:9342319}.
DISULFID 93 419 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 125 130 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 177 195
DISULFID 185 232 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 234 239 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 280 293 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 282 291 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 320 338 {ECO:0000255|HAMAP-Rule:MF_04071}.
DISULFID 423 449 {ECO:0000255|HAMAP-Rule:MF_04071}.
CONFLICT 377 377 M -> I (in Ref. 2; AAA43574).
CONFLICT 387 388 DK -> ER (in Ref. 2; AAA43574).
STRAND 96 103 {ECO:0000244|PDB:1F8D}.
HELIX 106 110 {ECO:0000244|PDB:1F8D}.
STRAND 115 126 {ECO:0000244|PDB:1F8D}.
STRAND 129 143 {ECO:0000244|PDB:1F8D}.
HELIX 144 146 {ECO:0000244|PDB:1F8D}.
TURN 147 150 {ECO:0000244|PDB:1F8D}.
STRAND 158 163 {ECO:0000244|PDB:1F8D}.
TURN 170 172 {ECO:0000244|PDB:1F8D}.
STRAND 174 186 {ECO:0000244|PDB:1F8D}.
STRAND 188 198 {ECO:0000244|PDB:1F8D}.
STRAND 200 202 {ECO:0000244|PDB:1INY}.
STRAND 204 209 {ECO:0000244|PDB:1F8D}.
STRAND 212 218 {ECO:0000244|PDB:1F8D}.
STRAND 220 223 {ECO:0000244|PDB:1F8D}.
STRAND 225 227 {ECO:0000244|PDB:1NCB}.
STRAND 229 231 {ECO:0000244|PDB:1NCC}.
STRAND 238 246 {ECO:0000244|PDB:1F8D}.
STRAND 248 250 {ECO:0000244|PDB:1F8D}.
STRAND 252 260 {ECO:0000244|PDB:1F8D}.
STRAND 263 269 {ECO:0000244|PDB:1F8D}.
STRAND 278 285 {ECO:0000244|PDB:1F8D}.
STRAND 288 294 {ECO:0000244|PDB:1F8D}.
STRAND 296 298 {ECO:0000244|PDB:2QWC}.
STRAND 303 308 {ECO:0000244|PDB:1F8D}.
TURN 309 312 {ECO:0000244|PDB:1F8D}.
STRAND 313 318 {ECO:0000244|PDB:1F8D}.
STRAND 321 323 {ECO:0000244|PDB:4DGR}.
STRAND 326 328 {ECO:0000244|PDB:1F8D}.
STRAND 338 340 {ECO:0000244|PDB:1F8D}.
HELIX 358 360 {ECO:0000244|PDB:1NCA}.
STRAND 362 365 {ECO:0000244|PDB:1F8D}.
STRAND 369 379 {ECO:0000244|PDB:1F8D}.
TURN 381 385 {ECO:0000244|PDB:1F8D}.
STRAND 392 403 {ECO:0000244|PDB:1F8D}.
STRAND 407 410 {ECO:0000244|PDB:1F8D}.
STRAND 416 420 {ECO:0000244|PDB:1F8D}.
STRAND 423 431 {ECO:0000244|PDB:1F8D}.
TURN 432 434 {ECO:0000244|PDB:1F8D}.
STRAND 441 453 {ECO:0000244|PDB:1F8D}.
HELIX 466 469 {ECO:0000244|PDB:1F8D}.
SEQUENCE 470 AA; 52469 MW; F114226CF93E1370 CRC64;
MNPNQKILCT SATALVIGTI AVLIGITNLG LNIGLHLKPS CNCSHSQPEA TNASQTIINN
YYNDTNITQI SNTNIQVEER AIRDFNNLTK GLCTINSWHI YGKDNAVRIG EDSDVLVTRE
PYVSCDPDEC RFYALSQGTT IRGKHSNGTI HDRSQYRALI SWPLSSPPTV YNSRVECIGW
SSTSCHDGKT RMSICISGPN NNASAVIWYN RRPVTEINTW ARNILRTQES ECVCHNGVCP
VVFTDGSATG PAETRIYYFK EGKILKWEPL AGTAKHIEEC SCYGERAEIT CTCRDNWQGS
NRPVIRIDPV AMTHTSQYIC SPVLTDNPRP NDPTVGKCND PYPGNNNNGV KGFSYLDGVN
TWLGRTISIA SRSGYEMLKV PNALTDDKSK PTQGQTIVLN TDWSGYSGSF MDYWAEGECY
RACFYVELIR GRPKEDKVWW TSNSIVSMCS STEFLGQWDW PDGAKIEYFL


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orb82550 Influenza A H5N1 Neuraminidase protein Influenza A H5N1 (Avian) Neuraminidase, C-terminal is an infectious disease antigen_toxin. For research use only. 50
E02N0063 Rat Neuraminidase 96 Tests/kit
BP941 Neuraminidase 1 ml
BP941 Neuraminidase 1 ml
BP941 Neuraminidase 1 ml
NB100-94433 Neuraminidase 0.1 mg
E02N0003 Rat Neuraminidase elisa kit 96 Tests/kit
E13N0063 Anserine Neuraminidase 96 Tests/kit
E02N0003 Rat Neuraminidase ELISA , NA
E07N0063 Porcine Neuraminidase 96 Tests/kit
EC-32118-S Neuraminidase (Isoenzyme S), 1U
E02N0003 Rat Neuraminidase ELISA 96T/kit
E04N0063 Rabbit Neuraminidase 96 Tests/kit
NLS004761 Neuraminidase, Purified 10U
NLS004759 Neuraminidase, Purified 5U
GWB-73EE7F Influenza A Neuraminidase N1
NB100-94432 Neuraminidase 0.1 mg


 

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