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

S-adenosylmethionine synthase (AdoMet synthase) (EC 2.5.1.6) (Methionine adenosyltransferase) (MAT)

 METK_DROME              Reviewed;         408 AA.
P40320; Q0E8V3; Q9VPJ2; Q9VPJ3; Q9VPJ4; Q9VPJ5;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
28-NOV-2002, sequence version 2.
25-OCT-2017, entry version 164.
RecName: Full=S-adenosylmethionine synthase;
Short=AdoMet synthase;
EC=2.5.1.6 {ECO:0000250|UniProtKB:Q00266};
AltName: Full=Methionine adenosyltransferase;
Short=MAT;
Name=Sam-S; Synonyms=M(2)21AB, SamS; ORFNames=CG2674;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE.
STRAIN=Canton-S; TISSUE=Pupae;
PubMed=8150093; DOI=10.1016/0014-5793(94)80526-1;
Larsson J., Rasmuson-Lestander A.;
"Molecular cloning of the S-adenosylmethionine synthetase gene in
Drosophila melanogaster.";
FEBS Lett. 342:329-333(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
-!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from
methionine and ATP. The reaction comprises two steps that are both
catalyzed by the same enzyme: formation of S-adenosylmethionine
(AdoMet) and triphosphate, and subsequent hydrolysis of the
triphosphate. {ECO:0000250|UniProtKB:Q00266}.
-!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate +
diphosphate + S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q00266}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P13444};
Note=Binds 2 magnesium ions per subunit. The magnesium ions
interact primarily with the substrate.
{ECO:0000250|UniProtKB:P13444};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000250|UniProtKB:P13444};
Note=Binds 1 potassium ion per subunit. The potassium ion
interacts primarily with the substrate.
{ECO:0000250|UniProtKB:P13444};
-!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine
biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
{ECO:0000250|UniProtKB:Q00266}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=2; Synonyms=A, D;
IsoId=P40320-1; Sequence=Displayed;
Name=1; Synonyms=B;
IsoId=P40320-2; Sequence=VSP_005963, VSP_005964, VSP_005965;
Name=3; Synonyms=C, J;
IsoId=P40320-3; Sequence=VSP_005963;
Name=4; Synonyms=G;
IsoId=P40320-4; Sequence=VSP_005961, VSP_005962, VSP_005963;
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Expressed throughout development with highest levels at adult
stages. {ECO:0000269|PubMed:8150093}.
-!- SIMILARITY: Belongs to the AdoMet synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X77392; CAA54567.1; -; mRNA.
EMBL; AE014134; AAF51555.1; -; Genomic_DNA.
EMBL; AE014134; AAF51556.1; -; Genomic_DNA.
EMBL; AE014134; AAF51557.1; -; Genomic_DNA.
EMBL; AE014134; AAF51558.1; -; Genomic_DNA.
EMBL; AE014134; AAN10505.1; -; Genomic_DNA.
EMBL; AE014134; AAN10506.1; -; Genomic_DNA.
EMBL; AE014134; AAN10507.1; -; Genomic_DNA.
EMBL; AE014134; AAS64636.1; -; Genomic_DNA.
EMBL; AY051918; AAK93342.1; -; mRNA.
PIR; S43258; S41917.
RefSeq; NP_524923.1; NM_080184.2. [P40320-3]
RefSeq; NP_722593.1; NM_164355.3. [P40320-3]
RefSeq; NP_722594.1; NM_164356.2. [P40320-1]
RefSeq; NP_722595.1; NM_164357.2. [P40320-1]
RefSeq; NP_722596.1; NM_164358.2. [P40320-1]
RefSeq; NP_722597.1; NM_164359.2. [P40320-1]
RefSeq; NP_722598.1; NM_164360.3. [P40320-1]
RefSeq; NP_722599.1; NM_164361.2. [P40320-2]
RefSeq; NP_722600.1; NM_164362.3. [P40320-4]
RefSeq; NP_995602.1; NM_205880.1. [P40320-1]
UniGene; Dm.7020; -.
ProteinModelPortal; P40320; -.
SMR; P40320; -.
BioGrid; 71491; 24.
DIP; DIP-18340N; -.
IntAct; P40320; 9.
STRING; 7227.FBpp0088926; -.
PaxDb; P40320; -.
PRIDE; P40320; -.
EnsemblMetazoa; FBtr0089428; FBpp0088444; FBgn0005278. [P40320-2]
EnsemblMetazoa; FBtr0089429; FBpp0088445; FBgn0005278. [P40320-1]
EnsemblMetazoa; FBtr0089430; FBpp0088446; FBgn0005278. [P40320-1]
EnsemblMetazoa; FBtr0089431; FBpp0088447; FBgn0005278. [P40320-3]
EnsemblMetazoa; FBtr0089432; FBpp0088448; FBgn0005278. [P40320-1]
EnsemblMetazoa; FBtr0089433; FBpp0088449; FBgn0005278. [P40320-1]
EnsemblMetazoa; FBtr0089434; FBpp0088450; FBgn0005278. [P40320-1]
EnsemblMetazoa; FBtr0089435; FBpp0088451; FBgn0005278. [P40320-3]
EnsemblMetazoa; FBtr0089436; FBpp0088452; FBgn0005278. [P40320-4]
EnsemblMetazoa; FBtr0089437; FBpp0088926; FBgn0005278. [P40320-1]
GeneID; 48552; -.
KEGG; dme:Dmel_CG2674; -.
CTD; 48552; -.
FlyBase; FBgn0005278; Sam-S.
eggNOG; KOG1506; Eukaryota.
eggNOG; COG0192; LUCA.
GeneTree; ENSGT00900000141246; -.
HOGENOM; HOG000120097; -.
InParanoid; P40320; -.
KO; K00789; -.
OMA; PGHFLFT; -.
OrthoDB; EOG091G08Z2; -.
PhylomeDB; P40320; -.
Reactome; R-DME-156581; Methylation.
Reactome; R-DME-1614635; Sulfur amino acid metabolism.
Reactome; R-DME-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
UniPathway; UPA00315; UER00080.
ChiTaRS; Sam-S; fly.
GenomeRNAi; 48552; -.
PRO; PR:P40320; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0005278; -.
ExpressionAtlas; P40320; differential.
Genevisible; P40320; DM.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004478; F:methionine adenosyltransferase activity; ISS:FlyBase.
GO; GO:0022416; P:chaeta development; IGI:FlyBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IMP:FlyBase.
GO; GO:0035220; P:wing disc development; IGI:FlyBase.
HAMAP; MF_00086; S_AdoMet_synth1; 1.
InterPro; IPR022631; ADOMET_SYNTHASE_CS.
InterPro; IPR022630; S-AdoMet_synt_C.
InterPro; IPR022629; S-AdoMet_synt_central.
InterPro; IPR022628; S-AdoMet_synt_N.
InterPro; IPR002133; S-AdoMet_synthetase.
InterPro; IPR022636; S-AdoMet_synthetase_sfam.
PANTHER; PTHR11964; PTHR11964; 1.
Pfam; PF02773; S-AdoMet_synt_C; 1.
Pfam; PF02772; S-AdoMet_synt_M; 1.
Pfam; PF00438; S-AdoMet_synt_N; 1.
PIRSF; PIRSF000497; MAT; 1.
SUPFAM; SSF55973; SSF55973; 3.
TIGRFAMs; TIGR01034; metK; 1.
PROSITE; PS00376; ADOMET_SYNTHASE_1; 1.
PROSITE; PS00377; ADOMET_SYNTHASE_2; 1.
2: Evidence at transcript level;
Alternative splicing; ATP-binding; Complete proteome; Magnesium;
Metal-binding; Nucleotide-binding; One-carbon metabolism; Potassium;
Reference proteome; Transferase.
CHAIN 1 408 S-adenosylmethionine synthase.
/FTId=PRO_0000174446.
NP_BIND 190 192 ATP. {ECO:0000250|UniProtKB:Q00266}.
NP_BIND 258 261 ATP. {ECO:0000250|UniProtKB:Q00266}.
NP_BIND 275 276 ATP. {ECO:0000250|UniProtKB:P0A817}.
METAL 34 34 Magnesium.
{ECO:0000250|UniProtKB:P13444}.
METAL 68 68 Potassium.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 40 40 ATP. {ECO:0000250|UniProtKB:Q00266}.
BINDING 81 81 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 124 124 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 269 269 ATP. {ECO:0000250|UniProtKB:Q00266}.
BINDING 269 269 Methionine; shared with neighboring
subunit. {ECO:0000250|UniProtKB:P0A817}.
BINDING 292 292 ATP; via amide nitrogen; shared with
neighboring subunit.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 296 296 ATP; shared with neighboring subunit.
{ECO:0000250|UniProtKB:P0A817}.
BINDING 300 300 ATP; shared with neighboring subunit.
{ECO:0000250|UniProtKB:P13444}.
BINDING 300 300 Methionine.
{ECO:0000250|UniProtKB:P0A817}.
VAR_SEQ 1 27 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_005961.
VAR_SEQ 28 41 TFLFTSESVGEGHP -> MISAECHSEEYTPN (in
isoform 4). {ECO:0000305}.
/FTId=VSP_005962.
VAR_SEQ 112 141 FKTCNVLLALDQQSPEIAAGVHVNRAEEEI -> WKTLNLL
VAIEQQSPNIANGVHINREEEDV (in isoform 1,
isoform 3 and isoform 4). {ECO:0000305}.
/FTId=VSP_005963.
VAR_SEQ 147 200 GIMFGYATDETEECMPLTVVLAHKLNEKIAELRRSDVFWWA
RPDSKTQVTCEYL -> VSISKRAMCCWHWTNNRLRSLREC
MSTVPRKRSVPEIRVSCLDMPPTKPRNVCP (in
isoform 1). {ECO:0000305}.
/FTId=VSP_005964.
VAR_SEQ 201 408 Missing (in isoform 1). {ECO:0000305}.
/FTId=VSP_005965.
CONFLICT 34 34 E -> V (in Ref. 1; CAA54567).
{ECO:0000305}.
CONFLICT 94 94 V -> I (in Ref. 1; CAA54567).
{ECO:0000305}.
CONFLICT 290 290 G -> A (in Ref. 1; CAA54567).
{ECO:0000305}.
CONFLICT 400 408 EAKPLEIDN -> SQASGD (in Ref. 1;
CAA54567). {ECO:0000305}.
SEQUENCE 408 AA; 44697 MW; CA0F97C1EA6623DF CRC64;
MPQKTNGHSA NGCNGSNGNS YDMEDGATFL FTSESVGEGH PDKMCDQISD AILDAHLKQD
PNAKVACETV AKTGMILLCG EITSKAVVDY QKVVRETVQH IGYDDSSKGF DFKTCNVLLA
LDQQSPEIAA GVHVNRAEEE IGAGDQGIMF GYATDETEEC MPLTVVLAHK LNEKIAELRR
SDVFWWARPD SKTQVTCEYL FNQGSAVPKR VHTIVVSMQH SEKISLETLR SEVMEKVVKV
VIPAKYIDAN TIVHINPCGL FVIGGPMGDA GLTGRKIIVD TYGGWGAHGG GAFSGKDFTK
VDRSAAYAAR WVAKSLVKAG LCKRCLVQVS YAIGLAEPLS ITVFDYGTSH KSQKELLDII
RRNFDLRPGK IVKDLNLRQP IYQRTSTYGH FGRAGFSWEE AKPLEIDN


Related products :

Catalog number Product name Quantity
15-288-22390A S-adenosylmethionine synthetase isoform type-2 - EC 2.5.1.6; Methionine adenosyltransferase 2; AdoMet synthetase 2; Methionine adenosyltransferase II; MAT-II Polyclonal 0.1 mg
15-288-22390A S-adenosylmethionine synthetase isoform type-2 - EC 2.5.1.6; Methionine adenosyltransferase 2; AdoMet synthetase 2; Methionine adenosyltransferase II; MAT-II Polyclonal 0.05 mg
10-288-22390F S-adenosylmethionine synthetase isoform type-2 - EC 2.5.1.6; Methionine adenosyltransferase 2; AdoMet synthetase 2; Methionine adenosyltransferase II; MAT-II 0.05 mg
10-288-22390F S-adenosylmethionine synthetase isoform type-2 - EC 2.5.1.6; Methionine adenosyltransferase 2; AdoMet synthetase 2; Methionine adenosyltransferase II; MAT-II 0.1 mg
27-079 MAT2B belongs to the methionine adenosyltransferase (MAT) family. MAT catalyzes the biosynthesis of S-adenosylmethionine from methionine and ATP. This protein is the regulatory beta subunit of MAT.The 0.05 mg
29-561 MAT1A catalyzes the formation of S-adenosylmethionine from methionine and ATP. Methionine adenosyltransferase deficiency is caused by recessive and dominant mutations, the latter identified in autosom 0.1 mg
EIAAB06601 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,Homo sapiens,Human
EIAAB06600 Bos taurus,Bovine,CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,
EIAAB06599 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,Cds,CDS 1,Cds1,CTP phosphatidate cytidylyltransferase 1,Mouse,Mus musc
EIAAB06603 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,Cds2,CTP phosphatidate cytidylyltransferase 2,Mouse,Mus musculus
EIAAB06597 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,CDS,CDS 1,CDS1,CTP phosphatidate cytidylyltransferase 1,Homo sapiens,H
E0167h ELISA kit Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostag 96T
E0167h ELISA Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandi 96T
EIAAB28570 (2-5')oligo(A) synthase 1B,2-5A synthase 1B,2'-5'-oligoadenylate synthase 1B,2'-5'-oligoadenylate synthase-like protein 1,Mouse,Mus musculus,Oas1b,Oias2
U0167m CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167b ELISA kit Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167r ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
E0167m ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167r ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
U0167r CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
E0167m ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167b ELISA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
U0167b CLIA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167p ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 96T
U0167p CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 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