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Synaptosomal-associated protein 23 (SNAP-23) (Vesicle-membrane fusion protein SNAP-23)

 SNP23_HUMAN             Reviewed;         211 AA.
O00161; O00162; Q13602; Q6IAE3;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
22-NOV-2017, entry version 184.
RecName: Full=Synaptosomal-associated protein 23;
Short=SNAP-23;
AltName: Full=Vesicle-membrane fusion protein SNAP-23;
Name=SNAP23;
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 SNAP-23A).
TISSUE=B-cell;
PubMed=8663154; DOI=10.1074/jbc.271.23.13300;
Ravichandran V., Chawla A., Roche P.A.;
"Identification of a novel syntaxin- and synaptobrevin/VAMP-binding
protein, SNAP-23, expressed in non-neuronal tissues.";
J. Biol. Chem. 271:13300-13303(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SNAP-23A AND SNAP-23B).
TISSUE=Neutrophil;
PubMed=9070898; DOI=10.1006/bbrc.1997.6196;
Mollinedo F., Lazo P.A.;
"Identification of two isoforms of the vesicle-membrane fusion protein
SNAP-23 in human neutrophils and HL-60 cells.";
Biochem. Biophys. Res. Commun. 231:808-812(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
PubMed=11354632; DOI=10.1007/s004390100480;
Lazo P.A., Nadal M., Ferrer M., Area E., Hernandez-Torres J.,
Nabokina S.M., Mollinedo F., Estivill X.;
"Genomic organization, chromosomal localization, alternative splicing,
and isoforms of human Synaptosome associated protein-23 gene
implicated in vesicle-membrane fusion.";
Hum. Genet. 108:211-215(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
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 MRNA] (ISOFORM SNAP-23A).
TISSUE=Cervix, Placenta, and Testis;
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).
[7]
PROTEIN SEQUENCE OF 1-12, AND ACETYLATION AT MET-1.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
PROTEIN SEQUENCE OF 1-12 AND 55-64, ACETYLATION AT MET-1, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[9]
IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX1A.
PubMed=12130530; DOI=10.1182/blood.V100.3.1081;
Polgar J., Chung S.H., Reed G.L.;
"Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present
in human platelets and are required for granule secretion.";
Blood 100:1081-1083(2002).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PALMITOYLATION AT CYS-79; CYS-80; CYS-83; CYS-85; CYS-87 AND CYS-112.
PubMed=21044946; DOI=10.1194/jlr.D011106;
Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,
Stamler J.S., Casey P.J.;
"Site-specific analysis of protein S-acylation by resin-assisted
capture.";
J. Lipid Res. 52:393-398(2011).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-34 AND SER-110, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-6; SER-20; SER-34
AND SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-110 AND SER-161,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND 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).
[21]
INTERACTION WITH ZDHHC17.
PubMed=28882895; DOI=10.1074/jbc.M117.799650;
Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
"Peptide array based screening reveals a large number of proteins
interacting with the ankyrin repeat domain of the zDHHC17 S-
acyltransferase.";
J. Biol. Chem. 0:0-0(2017).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-76, COILED-COIL DOMAIN,
AND SUBUNIT.
PubMed=12556468; DOI=10.1074/jbc.M210483200;
Freedman S.J., Song H.K., Xu Y., Sun Z.Y., Eck M.J.;
"Homotetrameric structure of the SNAP-23 N-terminal coiled-coil
domain.";
J. Biol. Chem. 278:13462-13467(2003).
-!- FUNCTION: Essential component of the high affinity receptor for
the general membrane fusion machinery and an important regulator
of transport vesicle docking and fusion.
-!- SUBUNIT: Homotetramer (via coiled-coil domain), also forms
heterotetramers with STX4 and VAMP3 (PubMed:12556468). Found in a
complex with VAMP8 and STX1A (PubMed:12130530). Found in a complex
with VAMP8 and STX4 in pancreas (By similarity). Interacts
simultaneously with SNAPIN and SYN4 (By similarity). Interacts
with STX1A (By similarity). Interacts with STX12 (By similarity).
Interacts tightly to multiple syntaxins and synaptobrevins/VAMPs
(By similarity). Interacts with ZDHHC13 (via ANK repeats) (By
similarity). Interacts with ZDHHC17 (via ANK repeats)
(PubMed:28882895). {ECO:0000250|UniProtKB:O09044,
ECO:0000250|UniProtKB:O70377, ECO:0000269|PubMed:12130530,
ECO:0000269|PubMed:12556468, ECO:0000269|PubMed:28882895}.
-!- INTERACTION:
P54920:NAPA; NbExp=2; IntAct=EBI-745000, EBI-749652;
Q9H115:NAPB; NbExp=3; IntAct=EBI-745000, EBI-3921185;
O75558:STX11; NbExp=7; IntAct=EBI-745000, EBI-714135;
Q15836:VAMP3; NbExp=2; IntAct=EBI-745000, EBI-722343;
Q8IUH5:ZDHHC17; NbExp=4; IntAct=EBI-745000, EBI-524753;
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
Cell membrane; Lipid-anchor. Cell junction, synapse, synaptosome.
Note=Mainly localized to the plasma membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=SNAP-23a;
IsoId=O00161-1; Sequence=Displayed;
Name=SNAP-23b;
IsoId=O00161-2; Sequence=VSP_006187, VSP_006188;
-!- TISSUE SPECIFICITY: Ubiquitous. Highest levels where found in
placenta.
-!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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EMBL; U55936; AAC50537.1; -; mRNA.
EMBL; Y09567; CAA70760.1; -; mRNA.
EMBL; Y09568; CAA70761.1; -; mRNA.
EMBL; AJ011915; CAA09864.1; -; mRNA.
EMBL; AJ278972; CAC07504.1; -; Genomic_DNA.
EMBL; AJ278973; CAC07504.1; JOINED; Genomic_DNA.
EMBL; AJ278974; CAC07504.1; JOINED; Genomic_DNA.
EMBL; BT006916; AAP35562.1; -; mRNA.
EMBL; CR457212; CAG33493.1; -; mRNA.
EMBL; BC000148; AAH00148.1; -; mRNA.
EMBL; BC003686; AAH03686.1; -; mRNA.
EMBL; BC022890; AAH22890.1; -; mRNA.
CCDS; CCDS10087.1; -. [O00161-1]
CCDS; CCDS10088.1; -. [O00161-2]
PIR; JC5296; JC5296.
PIR; JC5297; JC5297.
RefSeq; NP_003816.2; NM_003825.3. [O00161-1]
RefSeq; NP_570710.1; NM_130798.2. [O00161-2]
UniGene; Hs.511149; -.
PDB; 1NHL; X-ray; 2.30 A; A=23-76.
PDB; 3ZUS; X-ray; 2.95 A; A/B/C/D=150-209.
PDBsum; 1NHL; -.
PDBsum; 3ZUS; -.
ProteinModelPortal; O00161; -.
SMR; O00161; -.
BioGrid; 114303; 65.
CORUM; O00161; -.
IntAct; O00161; 31.
MINT; MINT-4999382; -.
STRING; 9606.ENSP00000249647; -.
TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
iPTMnet; O00161; -.
PhosphoSitePlus; O00161; -.
SwissPalm; O00161; -.
BioMuta; SNAP23; -.
OGP; O00161; -.
EPD; O00161; -.
MaxQB; O00161; -.
PaxDb; O00161; -.
PeptideAtlas; O00161; -.
PRIDE; O00161; -.
DNASU; 8773; -.
Ensembl; ENST00000249647; ENSP00000249647; ENSG00000092531. [O00161-1]
Ensembl; ENST00000349777; ENSP00000207062; ENSG00000092531. [O00161-2]
Ensembl; ENST00000397138; ENSP00000380327; ENSG00000092531. [O00161-2]
GeneID; 8773; -.
KEGG; hsa:8773; -.
UCSC; uc001zpz.3; human. [O00161-1]
CTD; 8773; -.
DisGeNET; 8773; -.
EuPathDB; HostDB:ENSG00000092531.9; -.
GeneCards; SNAP23; -.
HGNC; HGNC:11131; SNAP23.
HPA; CAB037083; -.
HPA; CAB037317; -.
HPA; HPA001214; -.
MIM; 602534; gene.
neXtProt; NX_O00161; -.
OpenTargets; ENSG00000092531; -.
PharmGKB; PA35979; -.
eggNOG; KOG3065; Eukaryota.
eggNOG; ENOG410Y3Y0; LUCA.
GeneTree; ENSGT00390000012186; -.
HOGENOM; HOG000231599; -.
HOVERGEN; HBG056971; -.
InParanoid; O00161; -.
KO; K08508; -.
OMA; TNKDRID; -.
OrthoDB; EOG091G0N7J; -.
PhylomeDB; O00161; -.
TreeFam; TF315125; -.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-421837; Clathrin derived vesicle budding.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; O00161; -.
ChiTaRS; SNAP23; human.
EvolutionaryTrace; O00161; -.
GeneWiki; SNAP23; -.
GenomeRNAi; 8773; -.
PMAP-CutDB; O00161; -.
PRO; PR:O00161; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000092531; -.
CleanEx; HS_SNAP23; -.
ExpressionAtlas; O00161; baseline and differential.
Genevisible; O00161; HS.
GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
GO; GO:0042581; C:specific granule; IDA:UniProtKB.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0002553; P:histamine secretion by mast cell; IMP:UniProtKB.
GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
InterPro; IPR000928; SNAP-25.
InterPro; IPR000727; T_SNARE_dom.
Pfam; PF00835; SNAP-25; 1.
SMART; SM00397; t_SNARE; 2.
PROSITE; PS50192; T_SNARE; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell junction;
Cell membrane; Coiled coil; Complete proteome;
Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Protein transport; Reference proteome; Repeat;
Synapse; Synaptosome; Transport.
CHAIN 1 211 Synaptosomal-associated protein 23.
/FTId=PRO_0000213598.
DOMAIN 14 76 t-SNARE coiled-coil homology 1.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
DOMAIN 146 208 t-SNARE coiled-coil homology 2.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
COILED 23 76 {ECO:0000269|PubMed:12556468}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.8}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000250|UniProtKB:O09044}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
LIPID 79 79 S-palmitoyl cysteine.
{ECO:0000269|PubMed:21044946}.
LIPID 80 80 S-palmitoyl cysteine.
{ECO:0000269|PubMed:21044946}.
LIPID 83 83 S-palmitoyl cysteine.
{ECO:0000269|PubMed:21044946}.
LIPID 85 85 S-palmitoyl cysteine.
{ECO:0000269|PubMed:21044946}.
LIPID 87 87 S-palmitoyl cysteine.
{ECO:0000269|PubMed:21044946}.
LIPID 112 112 S-palmitoyl cysteine.
{ECO:0000269|PubMed:21044946}.
VAR_SEQ 89 89 R -> S (in isoform SNAP-23b).
{ECO:0000303|PubMed:9070898}.
/FTId=VSP_006187.
VAR_SEQ 90 142 Missing (in isoform SNAP-23b).
{ECO:0000303|PubMed:9070898}.
/FTId=VSP_006188.
CONFLICT 135 135 A -> V (in Ref. 1; AAC50537).
{ECO:0000305}.
HELIX 24 74 {ECO:0000244|PDB:1NHL}.
SEQUENCE 211 AA; 23354 MW; AC378E9786C3A239 CRC64;
MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE QLNRIEEGLD
QINKDMRETE KTLTELNKCC GLCVCPCNRT KNFESGKAYK TTWGDGGENS PCNVVSKQPG
PVTNGQLQQP TTGAASGGYI KRITNDARED EMEENLTQVG SILGNLKDMA LNIGNEIDAQ
NPQIKRITDK ADTNRDRIDI ANARAKKLID S


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EIAAB38981 Mouse,Mus musculus,Snap,Snap25,SNAP-25,SUP,Super protein,Synaptosomal-associated 25 kDa protein,Synaptosomal-associated protein 25
EIAAB38983 Rat,Rattus norvegicus,Snap,Snap25,SNAP-25,SUP,Super protein,Synaptosomal-associated 25 kDa protein,Synaptosomal-associated protein 25
10-002-38072 SNAP-25 (Synaptosomal-associated protein 25kDa. C.elegans) - SNAP-25; Synaptosomal-associated 25 kDa protein; Super protein; SUP N_A 0.5 mg
10-002-38072 SNAP-25 (Synaptosomal-associated protein 25kDa. C.elegans) - SNAP-25; Synaptosomal-associated 25 kDa protein; Super protein; SUP N_A 0.1 mg
10-663-45670 Synaptosomal-associated Protein 25kDa Celegans (SNAP-25) - SNAP-25; Synaptosomal-associated 25 kDa protein; Super protein; SUP N_A 0.01 mg
10-663-45670 Synaptosomal-associated Protein 25kDa Celegans (SNAP-25) - SNAP-25; Synaptosomal-associated 25 kDa protein; Super protein; SUP N_A 1 mg
10-663-45670 Synaptosomal-associated Protein 25kDa Celegans (SNAP-25) - SNAP-25; Synaptosomal-associated 25 kDa protein; Super protein; SUP N_A 0.05 mg
EIAAB38985 Chicken,Gallus gallus,SNAP,SNAP25,SNAP-25,SUP,Super protein,Synaptosomal-associated 25 kDa protein,Synaptosomal-associated protein 25
EIAAB38993 C1orf142,Epididymis luminal protein 170,HEL170,Homo sapiens,Human,SNAP47,SNAP-47,SVAP1,Synaptosomal-associated 47 kDa protein,Synaptosomal-associated protein 47
orb81864 Synaptosomal Protein 25kDa (SNAP-25) (183-197) peptide This is Synaptosomal Protein 25kDa (SNAP-25) (183-197) peptide. For research use only. 0.5 mg
EIAAB38982 Bos taurus,Bovine,SNAP25,SNAP-25,Synaptosomal-associated 25 kDa protein,Synaptosomal-associated protein 25
EIAAB38990 Bos taurus,Bovine,SNAP47,SNAP-47,Synaptosomal-associated 47 kDa protein,Synaptosomal-associated protein 47
EIAAB38991 Mouse,Mus musculus,Snap47,SNAP-47,Synaptosomal-associated 47 kDa protein,Synaptosomal-associated protein 47
EIAAB38992 Rat,Rattus norvegicus,Snap47,SNAP-47,Synaptosomal-associated 47 kDa protein,Synaptosomal-associated protein 47
18-003-43300 Synaptosomal-associated protein 25 - SNAP-25; Synaptosomal-associated 25 kDa protein; Super protein; SUP Polyclonal 0.05 mg Aff Pur
MD-19-0036P Synaptosomal Protein, 25kDa (SNAP-25; aa 183-197) 500


 

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