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Glutamate receptor ionotropic, NMDA 1 (GluN1) (Glutamate [NMDA] receptor subunit zeta-1) (N-methyl-D-aspartate receptor subunit NR1) (NMD-R1)

 NMDZ1_MOUSE             Reviewed;         938 AA.
P35438; A2AI15; A2AI18; Q8CFS4;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
25-OCT-2017, entry version 186.
RecName: Full=Glutamate receptor ionotropic, NMDA 1;
Short=GluN1;
AltName: Full=Glutamate [NMDA] receptor subunit zeta-1;
AltName: Full=N-methyl-D-aspartate receptor subunit NR1;
Short=NMD-R1;
Flags: Precursor;
Name=Grin1; Synonyms=Glurz1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=1532151; DOI=10.1016/0014-5793(92)80160-I;
Yamazaki M., Mori H., Araki K., Mori K.J., Mishina M.;
"Cloning, expression and modulation of a mouse NMDA receptor
subunit.";
FEBS Lett. 300:39-45(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Eye;
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).
[4]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=8060614;
Forrest D., Yuzaki M., Soares H.D., Ng L., Luk D.C., Sheng M.,
Stewart C.L., Morgan J.I., Connor J.A., Curran T.;
"Targeted disruption of NMDA receptor 1 gene abolishes NMDA response
and results in neonatal death.";
Neuron 13:325-338(1994).
[5]
IDENTIFICATION IN A COMPLEX WITH GRIN2A OR GRIN2B AND GRIN3B,
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=12008020; DOI=10.1016/S0169-328X(02)00173-0;
Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.;
"Cloning and characterization of a novel NMDA receptor subunit NR3B: a
dominant subunit that reduces calcium permeability.";
Brain Res. Mol. Brain Res. 100:43-52(2002).
[6]
SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH GRIN2A OR
GRIN2B AND GRIN3B.
PubMed=14602821;
Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.;
"Specific assembly with the NMDA receptor 3B subunit controls surface
expression and calcium permeability of NMDA receptors.";
J. Neurosci. 23:10064-10073(2003).
[7]
INTERACTION WITH MYZAP.
PubMed=18849881; DOI=10.1097/WNR.0b013e328317f05f;
Roginski R.S., Goubaeva F., Mikami M., Fried-Cassorla E., Nair M.R.,
Yang J.;
"GRINL1A colocalizes with N-methyl D-aspartate receptor NR1 subunit
and reduces N-methyl D-aspartate toxicity.";
NeuroReport 19:1721-1726(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
INTERACTION WITH SNX27.
PubMed=23524343; DOI=10.1038/nm.3117;
Wang X., Zhao Y., Zhang X., Badie H., Zhou Y., Mu Y., Loo L.S.,
Cai L., Thompson R.C., Yang B., Chen Y., Johnson P.F., Wu C., Bu G.,
Mobley W.C., Zhang D., Gage F.H., Ranscht B., Zhang Y.W., Lipton S.A.,
Hong W., Xu H.;
"Loss of sorting nexin 27 contributes to excitatory synaptic
dysfunction by modulating glutamate receptor recycling in Down's
syndrome.";
Nat. Med. 19:473-480(2013).
-!- FUNCTION: Component of NMDA receptor complexes that function as
heterotetrameric, ligand-gated ion channels with high calcium
permeability and voltage-dependent sensitivity to magnesium.
Channel activation requires binding of the neurotransmitter
glutamate to the epsilon subunit, glycine binding to the zeta
subunit, plus membrane depolarization to eliminate channel
inhibition by Mg(2+) (PubMed:1532151, PubMed:8060614,
PubMed:12008020). Sensitivity to glutamate and channel kinetics
depend on the subunit composition (PubMed:12008020).
{ECO:0000269|PubMed:12008020, ECO:0000269|PubMed:1532151,
ECO:0000269|PubMed:8060614}.
-!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a
epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third
subunit (GRIN3A or GRIN3B) (PubMed:12008020, PubMed:14602821).
Found in a complex with GRIN2A or GRIN2B and GRIN3B
(PubMed:12008020, PubMed:14602821). Found in a complex with GRIN2A
or GRIN2B, GRIN3A and PPP2CB (By similarity). Interacts with DLG4
and MPDZ (By similarity). Interacts with LRFN1 and LRFN2 (By
similarity). Interacts with MYZAP (PubMed:18849881). Interacts
with SNX27 (via PDZ domain); the interaction is required for
recycling to the plasma membrane when endocytosed and prevent
degradation in lysosomes (PubMed:23524343). Found in a complex
with DLG4 and PRR7 (By similarity). Found in a complex with GRIN2B
and PRR7 (By similarity). Interacts with PRR7; the interaction is
reduced following NMDA receptor activity (By similarity).
{ECO:0000250|UniProtKB:P35439, ECO:0000269|PubMed:12008020,
ECO:0000269|PubMed:14602821, ECO:0000269|PubMed:18849881,
ECO:0000269|PubMed:23524343}.
-!- INTERACTION:
Q62108:Dlg4; NbExp=15; IntAct=EBI-400084, EBI-300895;
Q924X6:Lrp8; NbExp=4; IntAct=EBI-400084, EBI-432319;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12008020,
ECO:0000269|PubMed:1532151, ECO:0000269|PubMed:8060614}; Multi-
pass membrane protein {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density {ECO:0000250}.
Note=Enriched in postsynaptic plasma membrane and postsynaptic
densities. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P35438-1; Sequence=Displayed;
Name=2;
IsoId=P35438-2; Sequence=VSP_014222, VSP_014223;
-!- TISSUE SPECIFICITY: Detected in brain (at protein level). Detected
in brain. {ECO:0000269|PubMed:8060614}.
-!- DOMAIN: A hydrophobic region that gives rise to the prediction of
a transmembrane span does not cross the membrane, but is part of a
discontinuously helical region that dips into the membrane and is
probably part of the pore and of the selectivity filter.
{ECO:0000250|UniProtKB:A0A1L8F5J9}.
-!- PTM: NMDA is probably regulated by C-terminal phosphorylation of
an isoform of NR1 by PKC. Dephosphorylated on Ser-897 probably by
protein phosphatase 2A (PPP2CB). Its phosphorylated state is
influenced by the formation of the NMDAR-PPP2CB complex and the
NMDAR channel activity (By similarity).
{ECO:0000250|UniProtKB:P35439}.
-!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected
Mendelian rate, appear grossly normal and have apparently normal
brain structure, but the pups do not feed and all die during the
first day after birth. Cerebellum granule cells and hippocampus
pyramidal neurons from mutants lack NMDA-induced Ca(2+)influx and
membrane currents, contrary to wild-type.
{ECO:0000269|PubMed:8060614}.
-!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC
1.A.10.1) family. NR1/GRIN1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D10028; BAA00920.1; -; mRNA.
EMBL; AL732309; CAM14685.1; -; Genomic_DNA.
EMBL; AL732309; CAM14688.1; -; Genomic_DNA.
EMBL; BC039157; AAH39157.1; -; mRNA.
CCDS; CCDS15764.1; -. [P35438-1]
CCDS; CCDS50528.1; -. [P35438-2]
PIR; S21104; S21104.
RefSeq; NP_001171127.1; NM_001177656.2.
RefSeq; NP_001171128.1; NM_001177657.2. [P35438-2]
RefSeq; NP_032195.1; NM_008169.3. [P35438-1]
UniGene; Mm.278672; -.
ProteinModelPortal; P35438; -.
SMR; P35438; -.
BioGrid; 200067; 82.
DIP; DIP-31577N; -.
IntAct; P35438; 126.
MINT; MINT-135802; -.
STRING; 10090.ENSMUSP00000028335; -.
ChEMBL; CHEMBL3832634; -.
iPTMnet; P35438; -.
PhosphoSitePlus; P35438; -.
MaxQB; P35438; -.
PaxDb; P35438; -.
PeptideAtlas; P35438; -.
PRIDE; P35438; -.
Ensembl; ENSMUST00000028335; ENSMUSP00000028335; ENSMUSG00000026959. [P35438-1]
Ensembl; ENSMUST00000114312; ENSMUSP00000109951; ENSMUSG00000026959. [P35438-2]
GeneID; 14810; -.
KEGG; mmu:14810; -.
UCSC; uc008iri.3; mouse. [P35438-2]
UCSC; uc008irk.3; mouse. [P35438-1]
CTD; 2902; -.
MGI; MGI:95819; Grin1.
eggNOG; KOG1053; Eukaryota.
eggNOG; ENOG410XNUR; LUCA.
GeneTree; ENSGT00760000119186; -.
HOGENOM; HOG000231491; -.
HOVERGEN; HBG052638; -.
InParanoid; P35438; -.
KO; K05208; -.
TreeFam; TF351405; -.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-438066; Unblocking of NMDA receptor, glutamate binding and activation.
Reactome; R-MMU-442729; CREB phosphorylation through the activation of CaMKII.
Reactome; R-MMU-442982; Ras activation uopn Ca2+ infux through NMDA receptor.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
PRO; PR:P35438; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026959; -.
CleanEx; MM_GRIN1; -.
ExpressionAtlas; P35438; baseline and differential.
Genevisible; P35438; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0043197; C:dendritic spine; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0030426; C:growth cone; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IPI:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0005262; F:calcium channel activity; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IDA:MGI.
GO; GO:0005516; F:calmodulin binding; IDA:MGI.
GO; GO:0005261; F:cation channel activity; IGI:MGI.
GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
GO; GO:0016595; F:glutamate binding; ISO:MGI.
GO; GO:0016594; F:glycine binding; IMP:UniProtKB.
GO; GO:0004972; F:NMDA glutamate receptor activity; IDA:MGI.
GO; GO:0005102; F:receptor binding; IPI:MGI.
GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:0008306; P:associative learning; IMP:MGI.
GO; GO:0055074; P:calcium ion homeostasis; IDA:MGI.
GO; GO:0006816; P:calcium ion transport; IDA:MGI.
GO; GO:0006812; P:cation transport; IGI:MGI.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; TAS:MGI.
GO; GO:0001661; P:conditioned taste aversion; IMP:MGI.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:MGI.
GO; GO:0007612; P:learning; IMP:MGI.
GO; GO:0007611; P:learning or memory; IMP:MGI.
GO; GO:0007616; P:long-term memory; IMP:MGI.
GO; GO:0060179; P:male mating behavior; IMP:MGI.
GO; GO:0007613; P:memory; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0050905; P:neuromuscular process; IMP:MGI.
GO; GO:0008355; P:olfactory learning; IMP:MGI.
GO; GO:0021586; P:pons maturation; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
GO; GO:0018964; P:propylene metabolic process; IDA:BHF-UCL.
GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
GO; GO:0010646; P:regulation of cell communication; IMP:MGI.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:MGI.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
GO; GO:0043576; P:regulation of respiratory gaseous exchange; IMP:MGI.
GO; GO:0051963; P:regulation of synapse assembly; IMP:MGI.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
GO; GO:0007585; P:respiratory gaseous exchange; IMP:MGI.
GO; GO:0001975; P:response to amphetamine; IMP:MGI.
GO; GO:0045471; P:response to ethanol; ISO:MGI.
GO; GO:0043278; P:response to morphine; IMP:MGI.
GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
GO; GO:0035176; P:social behavior; IMP:MGI.
GO; GO:0001964; P:startle response; IMP:MGI.
GO; GO:0001967; P:suckling behavior; IMP:MGI.
GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
GO; GO:0008542; P:visual learning; IMP:MGI.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
InterPro; IPR019594; Glu/Gly-bd.
InterPro; IPR001508; Iono_rcpt_met.
InterPro; IPR001320; Iontro_rcpt.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF10562; CaM_bdg_C0; 1.
Pfam; PF00060; Lig_chan; 1.
Pfam; PF10613; Lig_chan-Glu_bd; 1.
PRINTS; PR00177; NMDARECEPTOR.
SMART; SM00918; Lig_chan-Glu_bd; 1.
SMART; SM00079; PBPe; 1.
SUPFAM; SSF53822; SSF53822; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell junction; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
Ion transport; Ligand-gated ion channel; Magnesium; Membrane;
Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Receptor;
Reference proteome; Signal; Synapse; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 938 Glutamate receptor ionotropic, NMDA 1.
/FTId=PRO_0000011588.
TOPO_DOM 19 559 Extracellular. {ECO:0000305}.
TRANSMEM 560 580 Helical. {ECO:0000250|UniProtKB:P35439}.
TOPO_DOM 581 602 Cytoplasmic. {ECO:0000305}.
INTRAMEM 603 624 Discontinuously helical.
{ECO:0000250|UniProtKB:A0A1L8F5J9}.
TOPO_DOM 625 630 Cytoplasmic. {ECO:0000305}.
TRANSMEM 631 647 Helical. {ECO:0000250|UniProtKB:P35439}.
TOPO_DOM 648 812 Extracellular. {ECO:0000305}.
TRANSMEM 813 833 Helical. {ECO:0000250|UniProtKB:P35439}.
TOPO_DOM 834 938 Cytoplasmic. {ECO:0000305}.
REGION 516 518 Glycine binding.
{ECO:0000250|UniProtKB:P35439}.
REGION 603 624 Pore-forming.
{ECO:0000250|UniProtKB:A0A1L8F5J9}.
BINDING 523 523 Glycine. {ECO:0000250|UniProtKB:P35439}.
BINDING 688 688 Glycine. {ECO:0000250|UniProtKB:P35439}.
BINDING 732 732 Glycine. {ECO:0000250|UniProtKB:P35439}.
MOD_RES 889 889 Phosphoserine; by PKC. {ECO:0000250}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000250|UniProtKB:P35439}.
MOD_RES 896 896 Phosphoserine; by PKC. {ECO:0000250}.
MOD_RES 897 897 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P35439}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 203 203 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 471 471 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 79 308 {ECO:0000250|UniProtKB:P35439}.
DISULFID 420 454 {ECO:0000250|UniProtKB:P35439}.
DISULFID 436 455 {ECO:0000250|UniProtKB:P35439}.
DISULFID 744 798 {ECO:0000250|UniProtKB:P35439}.
VAR_SEQ 864 885 DRKSGRAEPDPKKKATFRAITS -> QYHPTDITGPLNLSD
PSVSTVV (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014222.
VAR_SEQ 886 938 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014223.
VARIANT 936 936 R -> T.
SEQUENCE 938 AA; 105481 MW; C610632DD3E06171 CRC64;
MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL
NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG
LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL
ETLLEERESK AEKVLQFDPG TKNVTALLME ARDLEARVII LSASEDDAAT VYRAAAMLNM
TGSGYVWLVG EREISGNALR YAPDGIIGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN YSIMNLQNRK
LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI VTIHQEPFVY VKPTMSDGTC
KEEFTVNGDP VKKVICTGPN DTSPGSPRHT VPQCCYGFCV DLLIKLARTM NFTYEVHLVA
DGKFGTQERV NNSNKKEWNG MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI
LVKKEIPRST LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA
LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN LAAFLVLDRP
EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS TMYRHMEKHN YESAAEAIQA
VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH
ENGFMEDLDK TWVRYQECDS RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH
KDARRKQMQL AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT
STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES


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EIAAB27387 Canis familiaris,Canis lupus familiaris,Dog,Glutamate [NMDA] receptor subunit zeta-1,GRIN1,NMDAR1,NMD-R1,N-methyl-D-aspartate receptor 1,N-methyl-D-aspartate receptor subunit NR1
EIAAB27378 Glutamate [NMDA] receptor subunit epsilon-2,GRIN2B,hNR3,Homo sapiens,Human,NMDAR2B,NMDAR2B,N-methyl D-aspartate receptor subtype 2B,N-methyl-D-aspartate receptor subunit 3,NR2B,NR3
18-003-42615 Glutamate [NMDA] receptor subunit epsilon 3 - N-methyl D-aspartate receptor subtype 2C; NR2C; NMDAR2C Polyclonal 0.05 mg Aff Pur
EIAAB27372 Glutamate [NMDA] receptor subunit 3B,Grin3b,NMDAR3B,N-methyl-D-aspartate receptor subtype 3B,NR3B,Rat,Rattus norvegicus
EIAAB27374 Glutamate [NMDA] receptor subunit epsilon-1,Grin2a,NMDAR2A,N-methyl D-aspartate receptor subtype 2A,NR2A,Rat,Rattus norvegicus
EIAAB27380 Glutamate [NMDA] receptor subunit epsilon-2,Grin2b,Mouse,Mus musculus,NMDAR2B,N-methyl D-aspartate receptor subtype 2B,NR2B
EIAAB27381 Glutamate [NMDA] receptor subunit epsilon-3,Grin2c,NMDAR2C,N-methyl D-aspartate receptor subtype 2C,NR2C,Rat,Rattus norvegicus
EIAAB27384 Glutamate [NMDA] receptor subunit epsilon-4,Grin2d,Mouse,Mus musculus,NMDAR2D,N-methyl D-aspartate receptor subtype 2D,NR2D
EIAAB27386 Glutamate [NMDA] receptor subunit epsilon-4,Grin2d,NMDAR2D,N-methyl D-aspartate receptor subtype 2D,NR2D,Rat,Rattus norvegicus
EIAAB27379 Glutamate [NMDA] receptor subunit epsilon-2,Grin2b,NMDAR2B,N-methyl D-aspartate receptor subtype 2B,NR2B,Rat,Rattus norvegicus
EIAAB27382 Glutamate [NMDA] receptor subunit epsilon-3,Grin2c,Mouse,Mus musculus,NMDAR2C,N-methyl D-aspartate receptor subtype 2C,NR2C
EIAAB27371 Glutamate [NMDA] receptor subunit 3B,GRIN3B,Homo sapiens,Human,NMDAR3B,N-methyl-D-aspartate receptor subtype 3B,NR3B
EIAAB27376 Glutamate [NMDA] receptor subunit epsilon-1,Grin2a,Mouse,Mus musculus,NMDAR2A,N-methyl D-aspartate receptor subtype 2A,NR2A
EIAAB27369 Glutamate [NMDA] receptor subunit 3A,GRIN3A,Homo sapiens,Human,KIAA1973,NMDAR3A,NMDAR-L,N-methyl-D-aspartate receptor subtype 3A,NR3A
EIAAB27383 Glutamate [NMDA] receptor subunit epsilon-3,GRIN2C,Homo sapiens,Human,NMDAR2C,NMDAR2C,N-methyl D-aspartate receptor subtype 2C,NR2C
EIAAB27375 Glutamate [NMDA] receptor subunit epsilon-1,GRIN2A,hNR2A,Homo sapiens,Human,NMDAR2A,NMDAR2A,N-methyl D-aspartate receptor subtype 2A,NR2A
EIAAB27385 EB11,Glutamate [NMDA] receptor subunit epsilon-4,GRIN2D,Homo sapiens,Human,NMDAR2D,NMDAR2D,N-methyl D-aspartate receptor subtype 2D,NR2D
ER280 Glutamate [NMDA] receptor subunit zeta-1 Elisa Kit 96T


 

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