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

Ganglioside GM2 activator (Cerebroside sulfate activator protein) (GM2-AP) (Sphingolipid activator protein 3) (SAP-3) [Cleaved into: Ganglioside GM2 activator isoform short]

 SAP3_HUMAN              Reviewed;         193 AA.
P17900; B2R699; D3DQH6; Q14426; Q14428; Q6LBL5;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 4.
07-NOV-2018, entry version 185.
RecName: Full=Ganglioside GM2 activator;
AltName: Full=Cerebroside sulfate activator protein;
AltName: Full=GM2-AP;
AltName: Full=Sphingolipid activator protein 3;
Short=SAP-3;
Contains:
RecName: Full=Ganglioside GM2 activator isoform short;
Flags: Precursor;
Name=GM2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-59 AND VAL-69.
PubMed=2059210; DOI=10.1016/0006-291X(91)90671-S;
Xie B., McInnes B., Neote K., Lamhonwah A.-M., Mahuran D.;
"Isolation and expression of a full-length cDNA encoding the human G-
M2 activator protein.";
Biochem. Biophys. Res. Commun. 177:1217-1223(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-19; VAL-59 AND VAL-69.
PubMed=1915857; DOI=10.1016/0014-5793(91)81084-L;
Klima H., Tanaka A., Schnabel D., Nakano T., Schroeder M., Suzuki K.,
Sandhoff K.;
"Characterization of full-length cDNAs and the gene coding for the
human GM2 activator protein.";
FEBS Lett. 289:260-264(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=1554364; DOI=10.1042/bj2820807;
Nagarajan S., Chen H.C., Li S.C., Li Y.T., Lockyer J.;
"Evidence for two cDNAs encoding human GM2-activator protein.";
Biochem. J. 282:807-813(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-19; VAL-59 AND VAL-69.
PubMed=1427911; DOI=10.1016/S0888-7543(05)80190-9;
Xie B., Kennedy J.L., McInnes B., Auger D., Mahuran D.J.;
"Identification of a processed pseudogene related to the functional
gene encoding the GM2 activator protein: localization of the
pseudogene to human chromosome 3 and the functional gene to human
chromosome 5.";
Genomics 14:796-798(1992).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-19 AND
VAL-69.
TISSUE=Substantia nigra;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-19; VAL-59 AND
VAL-69.
PubMed=10364519; DOI=10.1086/302463;
Chen B., Rigat B., Curry C., Mahuran D.J.;
"Structure of the GM2A gene: identification of an exon 2 nonsense
mutation and a naturally occurring transcript with an in-frame
deletion of exon 2.";
Am. J. Hum. Genet. 65:77-87(1999).
[8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-59 AND
VAL-69.
TISSUE=Uterus;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 15-193, AND VARIANTS THR-19; VAL-59 AND
VAL-69.
PubMed=2753159; DOI=10.1016/0014-5793(89)81454-1;
Schroeder M., Klima H., Nakano T., Kwon H., Quintern L.E.,
Gaertner S., Suzuki K., Sandhoff K.;
"Isolation of a cDNA encoding the human GM2 activator protein.";
FEBS Lett. 251:197-200(1989).
[11]
PROTEIN SEQUENCE OF 32-193.
TISSUE=Kidney;
PubMed=2209618; DOI=10.1111/j.1432-1033.1990.tb19280.x;
Furst W., Schubert J., Machleidt W., Meyer H.E., Sandhoff K.;
"The complete amino-acid sequences of human ganglioside GM2 activator
protein and cerebroside sulfate activator protein.";
Eur. J. Biochem. 192:709-714(1990).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=11090283; DOI=10.1006/jmbi.2000.4225;
Wright C.S., Li S.-C., Rastinejad F.;
"Crystal structure of human GM2-activator protein with a novel beta-
cup topology.";
J. Mol. Biol. 304:411-422(2000).
[14]
VARIANT GM2GAB ARG-138.
PubMed=1915858; DOI=10.1016/0014-5793(91)81211-P;
Schroeder M., Schnabel D., Suzuki K., Sandhoff K.;
"A mutation in the gene of a glycolipid-binding protein (GM2
activator) that causes GM2-gangliosidosis variant AB.";
FEBS Lett. 290:1-3(1991).
[15]
VARIANT GM2GAB PRO-169.
PubMed=8244332; DOI=10.1007/BF00216446;
Schroder M., Schnabel D., Hurwitz R., Young E., Suzuki K.,
Sandhoff K.;
"Molecular genetics of GM2-gangliosidosis AB variant: a novel mutation
and expression in BHK cells.";
Hum. Genet. 92:437-440(1993).
[16]
VARIANT GM2GAB LYS-88 DEL.
PubMed=8900233;
Schepers U., Glombitza G., Lemm T., Hoffmann A., Chabas A., Ozand P.,
Sandhoff K.;
"Molecular analysis of a GM2-activator deficiency in two patients with
GM2-gangliosidosis AB variant.";
Am. J. Hum. Genet. 59:1048-1056(1996).
-!- FUNCTION: The large binding pocket can accommodate several single
chain phospholipids and fatty acids, GM2A also exhibits some
calcium-independent phospholipase activity (By similarity). Binds
gangliosides and stimulates ganglioside GM2 degradation. It
stimulates only the breakdown of ganglioside GM2 and glycolipid
GA2 by beta-hexosaminidase A. It extracts single GM2 molecules
from membranes and presents them in soluble form to beta-
hexosaminidase A for cleavage of N-acetyl-D-galactosamine and
conversion to GM3. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- PTM: The serines in positions 32 and 33 are absent in 80% of the
sequenced protein.
-!- DISEASE: GM2-gangliosidosis AB (GM2GAB) [MIM:272750]: An autosomal
recessive lysosomal storage disease marked by the accumulation of
GM2 gangliosides in the neuronal cells. It is characterized by GM2
gangliosides accumulation in the presence of both normal
hexosaminidase A and B. {ECO:0000269|PubMed:1915858,
ECO:0000269|PubMed:8244332, ECO:0000269|PubMed:8900233}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SEQUENCE CAUTION:
Sequence=CAA43408.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA43994.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M76477; AAA35907.1; -; mRNA.
EMBL; X62078; CAA43993.1; -; mRNA.
EMBL; X62078; CAA43994.1; ALT_INIT; mRNA.
EMBL; X61095; CAA43408.1; ALT_INIT; mRNA.
EMBL; L01439; AAA52767.1; -; mRNA.
EMBL; AF124719; AAD25741.1; -; Genomic_DNA.
EMBL; AF124717; AAD25741.1; JOINED; Genomic_DNA.
EMBL; AF124718; AAD25741.1; JOINED; Genomic_DNA.
EMBL; AK312494; BAG35396.1; -; mRNA.
EMBL; AC008385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW61680.1; -; Genomic_DNA.
EMBL; CH471062; EAW61681.1; -; Genomic_DNA.
EMBL; BC009273; AAH09273.1; -; mRNA.
EMBL; X16087; CAA34215.1; -; mRNA.
CCDS; CCDS4313.1; -.
PIR; I54178; I54178.
PIR; S13195; S13195.
PIR; S22411; S22411.
RefSeq; NP_000396.2; NM_000405.4.
UniGene; Hs.483873; -.
PDB; 1G13; X-ray; 2.00 A; A/B/C=32-193.
PDB; 1PU5; X-ray; 1.90 A; A/B/C=32-193.
PDB; 1PUB; X-ray; 2.51 A; A=32-193.
PDB; 1TJJ; X-ray; 2.00 A; A/B/C=32-193.
PDB; 2AF9; X-ray; 2.00 A; A=32-193.
PDB; 2AG2; X-ray; 2.00 A; A/B/C=32-193.
PDB; 2AG4; X-ray; 1.80 A; A/B=32-193.
PDB; 2AG9; X-ray; 2.20 A; A/B=32-193.
PDBsum; 1G13; -.
PDBsum; 1PU5; -.
PDBsum; 1PUB; -.
PDBsum; 1TJJ; -.
PDBsum; 2AF9; -.
PDBsum; 2AG2; -.
PDBsum; 2AG4; -.
PDBsum; 2AG9; -.
ProteinModelPortal; P17900; -.
SMR; P17900; -.
BioGrid; 109022; 27.
IntAct; P17900; 3.
STRING; 9606.ENSP00000349687; -.
DrugBank; DB04660; Choline alfoscerate.
DrugBank; DB02325; Isopropyl Alcohol.
DrugBank; DB03017; Lauric Acid.
DrugBank; DB03633; Lpc-Ether.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB02261; Platelet Activating Factor.
SwissLipids; SLP:000000476; -.
BioMuta; GM2A; -.
DMDM; 160331912; -.
EPD; P17900; -.
MaxQB; P17900; -.
PaxDb; P17900; -.
PeptideAtlas; P17900; -.
PRIDE; P17900; -.
ProteomicsDB; 53524; -.
DNASU; 2760; -.
Ensembl; ENST00000357164; ENSP00000349687; ENSG00000196743.
GeneID; 2760; -.
KEGG; hsa:2760; -.
UCSC; uc003ltr.5; human.
CTD; 2760; -.
DisGeNET; 2760; -.
EuPathDB; HostDB:ENSG00000196743.8; -.
GeneCards; GM2A; -.
H-InvDB; HIX0005327; -.
HGNC; HGNC:4367; GM2A.
HPA; HPA008063; -.
MalaCards; GM2A; -.
MIM; 272750; phenotype.
MIM; 613109; gene.
neXtProt; NX_P17900; -.
OpenTargets; ENSG00000196743; -.
Orphanet; 309246; GM2 gangliosidosis, AB variant.
PharmGKB; PA28752; -.
eggNOG; ENOG410IX9N; Eukaryota.
eggNOG; ENOG4111JSM; LUCA.
GeneTree; ENSGT00390000003288; -.
HOGENOM; HOG000031350; -.
HOVERGEN; HBG000260; -.
InParanoid; P17900; -.
KO; K12383; -.
OMA; WLSTGNY; -.
OrthoDB; EOG091G0VEB; -.
PhylomeDB; P17900; -.
TreeFam; TF353575; -.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; GM2A; human.
EvolutionaryTrace; P17900; -.
GeneWiki; GM2A; -.
GenomeRNAi; 2760; -.
PRO; PR:P17900; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000196743; Expressed in 239 organ(s), highest expression level in visceral pleura.
CleanEx; HS_GM2A; -.
ExpressionAtlas; P17900; baseline and differential.
Genevisible; P17900; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0032428; F:beta-N-acetylgalactosaminidase activity; IEA:Ensembl.
GO; GO:0005319; F:lipid transporter activity; IEA:Ensembl.
GO; GO:0016004; F:phospholipase activator activity; IEA:Ensembl.
GO; GO:0030290; F:sphingolipid activator protein activity; TAS:Reactome.
GO; GO:0006689; P:ganglioside catabolic process; IEA:Ensembl.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0019915; P:lipid storage; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0009313; P:oligosaccharide catabolic process; IEA:Ensembl.
GO; GO:0051345; P:positive regulation of hydrolase activity; IEA:Ensembl.
Gene3D; 2.70.220.10; -; 1.
InterPro; IPR028996; GM2-AP.
InterPro; IPR036846; GM2-AP_sf.
InterPro; IPR003172; ML_dom.
PANTHER; PTHR17357; PTHR17357; 1.
Pfam; PF02221; E1_DerP2_DerF2; 1.
SMART; SM00737; ML; 1.
SUPFAM; SSF63707; SSF63707; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Gangliosidosis; Glycoprotein;
Hydrolase; Lipid metabolism; Lysosome; Polymorphism;
Reference proteome; Signal; Sphingolipid metabolism.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 31 {ECO:0000269|PubMed:2209618}.
/FTId=PRO_0000031639.
CHAIN 32 193 Ganglioside GM2 activator.
/FTId=PRO_0000031640.
CHAIN 34 193 Ganglioside GM2 activator isoform short.
/FTId=PRO_0000031641.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
DISULFID 39 183
DISULFID 99 106
DISULFID 112 138
DISULFID 125 136
VARIANT 19 19 A -> T (in dbSNP:rs1048719).
{ECO:0000269|PubMed:10364519,
ECO:0000269|PubMed:1427911,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:1915857,
ECO:0000269|PubMed:2753159}.
/FTId=VAR_013830.
VARIANT 59 59 I -> V (in dbSNP:rs153477).
{ECO:0000269|PubMed:10364519,
ECO:0000269|PubMed:1427911,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1915857,
ECO:0000269|PubMed:2059210,
ECO:0000269|PubMed:2753159}.
/FTId=VAR_036892.
VARIANT 69 69 M -> V (in dbSNP:rs153478).
{ECO:0000269|PubMed:10364519,
ECO:0000269|PubMed:1427911,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1915857,
ECO:0000269|PubMed:2059210,
ECO:0000269|PubMed:2753159}.
/FTId=VAR_036893.
VARIANT 88 88 Missing (in GM2GAB).
{ECO:0000269|PubMed:8900233}.
/FTId=VAR_011697.
VARIANT 138 138 C -> R (in GM2GAB; dbSNP:rs137852797).
{ECO:0000269|PubMed:1915858}.
/FTId=VAR_006947.
VARIANT 169 169 R -> P (in GM2GAB; dbSNP:rs104893892).
{ECO:0000269|PubMed:8244332}.
/FTId=VAR_011698.
CONFLICT 39 39 C -> R (in Ref. 5; BAG35396).
{ECO:0000305}.
STRAND 35 40 {ECO:0000244|PDB:2AG4}.
TURN 41 43 {ECO:0000244|PDB:2AG4}.
STRAND 45 74 {ECO:0000244|PDB:2AG4}.
STRAND 81 90 {ECO:0000244|PDB:2AG4}.
STRAND 93 96 {ECO:0000244|PDB:2AG4}.
STRAND 103 105 {ECO:0000244|PDB:2AG4}.
STRAND 107 109 {ECO:0000244|PDB:1PUB}.
HELIX 111 118 {ECO:0000244|PDB:2AG4}.
STRAND 121 123 {ECO:0000244|PDB:1PUB}.
HELIX 129 132 {ECO:0000244|PDB:2AG4}.
STRAND 137 140 {ECO:0000244|PDB:2AG9}.
STRAND 142 154 {ECO:0000244|PDB:2AG4}.
TURN 161 163 {ECO:0000244|PDB:2AG9}.
STRAND 164 176 {ECO:0000244|PDB:2AG4}.
STRAND 179 192 {ECO:0000244|PDB:2AG4}.
SEQUENCE 193 AA; 20838 MW; 4EB1119945365F7E CRC64;
MQSLMQAPLL IALGLLLAAP AQAHLKKPSQ LSSFSWDNCD EGKDPAVIRS LTLEPDPIIV
PGNVTLSVMG STSVPLSSPL KVDLVLEKEV AGLWIKIPCT DYIGSCTFEH FCDVLDMLIP
TGEPCPEPLR TYGLPCHCPF KEGTYSLPKS EFVVPDLELP SWLTTGNYRI ESVLSSSGKR
LGCIKIAASL KGI


Related products :

Catalog number Product name Quantity
EIAAB37274 Cerebroside sulfate activator protein,Ganglioside GM2 activator,GM2A,GM2-AP,Homo sapiens,Human,SAP-3,Shingolipid activator protein 3
EIAAB37275 Cerebroside sulfate activator protein,Ganglioside GM2 activator,Gm2a,GM2-AP,Mouse,Mus musculus,SAP-3,Shingolipid activator protein 3
E02G0009 Rat GM2 Ganglioside Activator protein ELISA 96T/kit
E04G0009 Rabbit GM2 Ganglioside Activator protein ELISA 96T/kit
E12G0009 Chicken GM2 Ganglioside Activator protein ELISA 96T/kit
E05G0009 Guinea Pig GM2 Ganglioside Activator protein ELISA 96T/kit
PE023754h Recombinant human Ganglioside GM2 activator protein 50ug
PE023754h Recombinant human Ganglioside GM2 activator protein 200ug
E07G0009 Porcine GM2 Ganglioside Activator protein ELISA 96T/kit
E02G0009 Rat GM2 Ganglioside Activator protein ELISA, GM2AP 96 Tests/kit
E06G0009 Goat GM2 Ganglioside Activator protein ELISA 96T/kit
PE023754h Recombinant human Ganglioside GM2 activator protein 1mg
E08G0009 Canine GM2 Ganglioside Activator protein ELISA 96T/kit
E11G0009 Bovine GM2 Ganglioside Activator protein ELISA 96T/kit
E14G0009 Sheep GM2 Ganglioside Activator protein ELISA 96T/kit
E01G0009 Human GM2 Ganglioside Activator protein ELISA 96T/kit
E02G0009 Rat GM2 Ganglioside Activator protein ELISA, GM2AP
PE023754h Recombinant human Ganglioside GM2 activator protein 5mg
E09G0009 Monkey GM2 Ganglioside Activator protein ELISA 96T/kit
E03G0009 Mouse GM2 Ganglioside Activator protein ELISA 96T/kit
CSB-RP023754h Recombinant human Ganglioside GM2 activator protein 500ug
E03G0009 Mouse GM2 Ganglioside Activator protein ELISA, GM2AP
E09G0009 Monkey GM2 Ganglioside Activator protein ELISA, GM2AP 96 Tests/kit
E05G0009 Guinea pig GM2 Ganglioside Activator protein ELISA, GM2AP
E04G0009 Rabbit GM2 Ganglioside Activator protein ELISA, GM2AP 96 Tests/kit


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | 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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | 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 | 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 | 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 | Gentaur