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Metabotropic glutamate receptor 1 (mGluR1)

 GRM1_RAT                Reviewed;        1199 AA.
P23385;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
28-MAR-2018, entry version 175.
RecName: Full=Metabotropic glutamate receptor 1;
Short=mGluR1;
Flags: Precursor;
Name=Grm1; Synonyms=Gprc1a, Mglur1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=1847995; DOI=10.1038/349760a0;
Masu M., Tanabe Y., Tsuchida K., Shigemoto R., Nakanishi S.;
"Sequence and expression of a metabotropic glutamate receptor.";
Nature 349:760-765(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=1656524; DOI=10.1126/science.1656524;
Houamed K.M., Kuijper J.L., Gilbert T.L., Haldeman B.A., O'Hara P.J.,
Mulvihill E.R., Almers W., Hagen F.S.;
"Cloning, expression, and gene structure of a G protein-coupled
glutamate receptor from rat brain.";
Science 252:1318-1321(1991).
[3]
ALTERNATIVE SPLICING (ISOFORM 1B).
TISSUE=Brain;
PubMed=1309649; DOI=10.1016/0896-6273(92)90118-W;
Tanabe Y., Masu M., Ishii T., Shigemoto R., Nakanishi S.;
"A family of metabotropic glutamate receptors.";
Neuron 8:169-179(1992).
[4]
ALTERNATIVE SPLICING (ISOFORM 1C), AND FUNCTION.
TISSUE=Brain;
PubMed=1438218; DOI=10.1073/pnas.89.21.10331;
Pin J.-P., Waeber C., Prezeau L., Bockaert J., Heinemann S.F.;
"Alternative splicing generates metabotropic glutamate receptors
inducing different patterns of calcium release in Xenopus oocytes.";
Proc. Natl. Acad. Sci. U.S.A. 89:10331-10335(1992).
[5]
INTERACTION WITH SIAH1.
PubMed=10469171; DOI=10.1046/j.1365-2443.1999.00269.x;
Ishikawa K., Nash S.R., Nishimune A., Neki A., Kaneko S.,
Nakanishi S.;
"Competitive interaction of seven in absentia homolog-1A and
Ca2+/calmodulin with the cytoplasmic tail of group 1 metabotropic
glutamate receptors.";
Genes Cells 4:381-390(1999).
[6]
FUNCTION, INTERCHAIN DISULFIDE BOND, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF CYS-67; CYS-109 AND CYS-140.
PubMed=10945991; DOI=10.1074/jbc.M005581200;
Ray K., Hauschild B.C.;
"Cys-140 is critical for metabotropic glutamate receptor-1
dimerization.";
J. Biol. Chem. 275:34245-34251(2000).
[7]
INTERACTION WITH GRASP.
PubMed=11850456;
Kitano J., Kimura K., Yamazaki Y., Soda T., Shigemoto R., Nakajima Y.,
Nakanishi S.;
"Tamalin, a PDZ domain-containing protein, links a protein complex
formation of group 1 metabotropic glutamate receptors and the guanine
nucleotide exchange factor cytohesins.";
J. Neurosci. 22:1280-1289(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-894; SER-1147 AND
THR-1151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[9]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 33-522 ALONE AND IN COMPLEX
WITH GLUTAMATE, SUBUNIT, GLYCOSYLATION AT ASN-98 AND ASN-223,
GLUTAMATE-BINDING SITES, AND DISULFIDE BONDS.
PubMed=11069170; DOI=10.1038/35039564;
Kunishima N., Shimada Y., Tsuji Y., Sato T., Yamamoto M., Kumasaka T.,
Nakanishi S., Jingami H., Morikawa K.;
"Structural basis of glutamate recognition by a dimeric metabotropic
glutamate receptor.";
Nature 407:971-977(2000).
[10]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 33-522 IN COMPLEX WITH
GLUTAMATE AND ANTAGONIST, SUBUNIT, AND DISULFIDE BONDS.
PubMed=11867751; DOI=10.1073/pnas.052708599;
Tsuchiya D., Kunishima N., Kamiya N., Jingami H., Morikawa K.;
"Structural views of the ligand-binding cores of a metabotropic
glutamate receptor complexed with an antagonist and both glutamate and
Gd3+.";
Proc. Natl. Acad. Sci. U.S.A. 99:2660-2665(2002).
-!- FUNCTION: G-protein coupled receptor for glutamate. Ligand binding
causes a conformation change that triggers signaling via guanine
nucleotide-binding proteins (G proteins) and modulates the
activity of down-stream effectors. Signaling activates a
phosphatidylinositol-calcium second messenger system. May
participate in the central action of glutamate in the CNS, such as
long-term potentiation in the hippocampus and long-term depression
in the cerebellum. {ECO:0000269|PubMed:10945991,
ECO:0000269|PubMed:1438218, ECO:0000269|PubMed:1656524,
ECO:0000269|PubMed:1847995}.
-!- SUBUNIT: The PPXXF motif binds HOMER1, HOMER2 and HOMER3.
Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3 (By
similarity). Interacts with SIAH1 and GRASP. Homodimer; disulfide-
linked. {ECO:0000250, ECO:0000269|PubMed:10469171,
ECO:0000269|PubMed:11069170, ECO:0000269|PubMed:11850456,
ECO:0000269|PubMed:11867751}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-4410410, EBI-4410410;
P63088:Ppp1cc; NbExp=15; IntAct=EBI-4410410, EBI-80049;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10945991};
Multi-pass membrane protein {ECO:0000269|PubMed:10945991}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1A;
IsoId=P23385-1; Sequence=Displayed;
Name=1B;
IsoId=P23385-2; Sequence=VSP_002026, VSP_002027;
Note=C-terminally truncated forms of isoform 1A.;
Name=1C;
IsoId=P23385-3; Sequence=VSP_002028, VSP_002029;
Note=C-terminally truncated forms of isoform 1A.;
-!- TISSUE SPECIFICITY: Predominantly expressed in cerebellar Purkinje
cells, CA2-CA3 pyramidal cells of the hippocampus, and mitral and
tufted cells of the olfactory bulb. {ECO:0000269|PubMed:1656524,
ECO:0000269|PubMed:1847995}.
-!- MISCELLANEOUS: Activated by quisqualate > glutamate > ibotenate >
trans-1- aminocyclopentyl-1,3-dicarboxylate; inhibited by 2-amino-
3-phosphonopropionate.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
{ECO:0000305}.
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EMBL; X57569; CAA40799.1; -; mRNA.
EMBL; M61099; AAA19497.1; -; mRNA.
EMBL; S48085; AAB24138.1; -; mRNA.
PIR; A41939; A41939.
RefSeq; NP_001107802.1; NM_001114330.1. [P23385-2]
RefSeq; NP_058707.1; NM_017011.1. [P23385-1]
UniGene; Rn.87787; -.
PDB; 1EWK; X-ray; 2.20 A; A/B=33-522.
PDB; 1EWT; X-ray; 3.70 A; A/B=33-522.
PDB; 1EWV; X-ray; 4.00 A; A/B=33-522.
PDB; 1ISR; X-ray; 4.00 A; A=33-522.
PDB; 1ISS; X-ray; 3.30 A; A/B=33-522.
PDBsum; 1EWK; -.
PDBsum; 1EWT; -.
PDBsum; 1EWV; -.
PDBsum; 1ISR; -.
PDBsum; 1ISS; -.
ProteinModelPortal; P23385; -.
SMR; P23385; -.
BioGrid; 246579; 9.
CORUM; P23385; -.
DIP; DIP-44897N; -.
ELM; P23385; -.
IntAct; P23385; 5.
MINT; P23385; -.
STRING; 10116.ENSRNOP00000019319; -.
BindingDB; P23385; -.
ChEMBL; CHEMBL4477; -.
GuidetoPHARMACOLOGY; 289; -.
iPTMnet; P23385; -.
PhosphoSitePlus; P23385; -.
PaxDb; P23385; -.
PRIDE; P23385; -.
Ensembl; ENSRNOT00000044325; ENSRNOP00000047790; ENSRNOG00000014290. [P23385-2]
GeneID; 24414; -.
KEGG; rno:24414; -.
UCSC; RGD:2742; rat. [P23385-1]
CTD; 2911; -.
RGD; 2742; Grm1.
eggNOG; KOG1056; Eukaryota.
eggNOG; ENOG410XR6W; LUCA.
GeneTree; ENSGT00760000118884; -.
HOGENOM; HOG000218636; -.
HOVERGEN; HBG107965; -.
InParanoid; P23385; -.
KO; K04603; -.
PhylomeDB; P23385; -.
Reactome; R-RNO-416476; G alpha (q) signalling events.
Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
Reactome; R-RNO-6794361; Neurexins and neuroligins.
EvolutionaryTrace; P23385; -.
PMAP-CutDB; P23385; -.
PRO; PR:P23385; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000014290; -.
ExpressionAtlas; P23385; baseline and differential.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0038037; C:G-protein coupled receptor dimeric complex; ISO:RGD.
GO; GO:0038038; C:G-protein coupled receptor homodimeric complex; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISO:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IPI:RGD.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:RGD.
GO; GO:0099530; F:G-protein coupled receptor activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
GO; GO:0008066; F:glutamate receptor activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0099583; F:neurotransmitter receptor activity involved in regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD.
GO; GO:0001639; F:PLC activating G-protein coupled glutamate receptor activity; TAS:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; ISO:RGD.
GO; GO:0000186; P:activation of MAPKK activity; ISO:RGD.
GO; GO:0007196; P:adenylate cyclase-inhibiting G-protein coupled glutamate receptor signaling pathway; IBA:GO_Central.
GO; GO:0019722; P:calcium-mediated signaling; IDA:RGD.
GO; GO:0071257; P:cellular response to electrical stimulus; ISO:RGD.
GO; GO:0007268; P:chemical synaptic transmission; IEP:RGD.
GO; GO:0038042; P:dimeric G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007216; P:G-protein coupled glutamate receptor signaling pathway; IMP:SynGO.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007626; P:locomotory behavior; ISO:RGD.
GO; GO:0051899; P:membrane depolarization; TAS:UniProtKB.
GO; GO:0007206; P:phospholipase C-activating G-protein coupled glutamate receptor signaling pathway; TAS:UniProtKB.
GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway; ISS:UniProtKB.
GO; GO:0014048; P:regulation of glutamate secretion; TAS:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; ISO:RGD.
GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD.
GO; GO:0051930; P:regulation of sensory perception of pain; ISO:RGD.
GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IDA:UniProtKB.
GO; GO:0019233; P:sensory perception of pain; IEP:RGD.
GO; GO:0051932; P:synaptic transmission, GABAergic; TAS:UniProtKB.
Gene3D; 2.10.50.30; -; 1.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR000337; GPCR_3.
InterPro; IPR011500; GPCR_3_9-Cys_dom.
InterPro; IPR038550; GPCR_3_9-Cys_sf.
InterPro; IPR017978; GPCR_3_C.
InterPro; IPR017979; GPCR_3_CS.
InterPro; IPR000162; GPCR_3_mtglu_rcpt.
InterPro; IPR001256; GPCR_3_mtglu_rcpt_1.
InterPro; IPR019588; Metabotropic_Glu_rcpt_Homer-bd.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF00003; 7tm_3; 1.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF10606; GluR_Homer-bdg; 1.
Pfam; PF07562; NCD3G; 1.
PRINTS; PR00248; GPCRMGR.
PRINTS; PR01051; MTABOTROPC1R.
PRINTS; PR00593; MTABOTROPICR.
SMART; SM01229; GluR_Homer-bdg; 1.
SUPFAM; SSF53822; SSF53822; 1.
PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
Transmembrane; Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 1199 Metabotropic glutamate receptor 1.
/FTId=PRO_0000012924.
TOPO_DOM 19 592 Extracellular. {ECO:0000250}.
TRANSMEM 593 615 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 616 629 Cytoplasmic. {ECO:0000250}.
TRANSMEM 630 650 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 651 658 Extracellular. {ECO:0000250}.
TRANSMEM 659 680 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 681 703 Cytoplasmic. {ECO:0000250}.
TRANSMEM 704 727 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 728 750 Extracellular. {ECO:0000250}.
TRANSMEM 751 772 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 773 785 Cytoplasmic. {ECO:0000250}.
TRANSMEM 786 807 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 808 815 Extracellular. {ECO:0000250}.
TRANSMEM 816 840 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 841 1199 Cytoplasmic. {ECO:0000250}.
REGION 186 188 Glutamate binding.
COMPBIAS 1014 1034 Gln/Pro-rich.
COMPBIAS 1074 1080 Gln/Pro-rich.
COMPBIAS 1126 1135 Asp/Glu-rich (acidic).
COMPBIAS 1140 1199 Ser-rich.
BINDING 74 74 Glutamate. {ECO:0000269|PubMed:11069170,
ECO:0000269|PubMed:11867751}.
BINDING 165 165 Glutamate. {ECO:0000269|PubMed:11069170,
ECO:0000269|PubMed:11867751}.
BINDING 236 236 Glutamate. {ECO:0000269|PubMed:11069170,
ECO:0000269|PubMed:11867751}.
BINDING 318 318 Glutamate. {ECO:0000269|PubMed:11069170,
ECO:0000269|PubMed:11867751}.
BINDING 409 409 Glutamate. {ECO:0000269|PubMed:11069170,
ECO:0000269|PubMed:11867751}.
MOD_RES 853 853 Phosphoserine.
{ECO:0000250|UniProtKB:P97772}.
MOD_RES 871 871 Phosphothreonine.
{ECO:0000250|UniProtKB:P97772}.
MOD_RES 894 894 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 969 969 Phosphoserine.
{ECO:0000250|UniProtKB:P97772}.
MOD_RES 1098 1098 Phosphoserine.
{ECO:0000250|UniProtKB:P97772}.
MOD_RES 1147 1147 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1151 1151 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1154 1154 Phosphoserine.
{ECO:0000250|UniProtKB:P97772}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11069170}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11069170}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 67 109
DISULFID 140 140 Interchain.
DISULFID 289 291
DISULFID 378 394
DISULFID 432 439
DISULFID 657 746 {ECO:0000250}.
VAR_SEQ 887 906 NSNGKSVSWSEPGGRQAPKG -> KKRQPEFSPSSQCPSAH
AQL (in isoform 1B). {ECO:0000305}.
/FTId=VSP_002026.
VAR_SEQ 888 897 SNGKSVSWSE -> FALDRQNTVY (in isoform 1C).
{ECO:0000305}.
/FTId=VSP_002028.
VAR_SEQ 898 1199 Missing (in isoform 1C). {ECO:0000305}.
/FTId=VSP_002029.
VAR_SEQ 907 1199 Missing (in isoform 1B). {ECO:0000305}.
/FTId=VSP_002027.
MUTAGEN 67 67 C->S: Impairs protein folding and
abolishes location at the cell surface.
{ECO:0000269|PubMed:10945991}.
MUTAGEN 109 109 C->S: Impairs protein folding and
abolishes location at the cell surface.
{ECO:0000269|PubMed:10945991}.
MUTAGEN 140 140 C->S: Impairs homodimerization.
{ECO:0000269|PubMed:10945991}.
STRAND 39 41 {ECO:0000244|PDB:1EWK}.
STRAND 44 51 {ECO:0000244|PDB:1EWK}.
TURN 59 65 {ECO:0000244|PDB:1EWK}.
TURN 72 75 {ECO:0000244|PDB:1EWK}.
HELIX 76 91 {ECO:0000244|PDB:1EWK}.
STRAND 93 96 {ECO:0000244|PDB:1EWK}.
STRAND 101 107 {ECO:0000244|PDB:1EWK}.
HELIX 112 123 {ECO:0000244|PDB:1EWK}.
STRAND 156 160 {ECO:0000244|PDB:1EWK}.
HELIX 165 175 {ECO:0000244|PDB:1EWK}.
HELIX 176 178 {ECO:0000244|PDB:1EWK}.
STRAND 182 186 {ECO:0000244|PDB:1EWK}.
HELIX 190 193 {ECO:0000244|PDB:1EWK}.
TURN 195 197 {ECO:0000244|PDB:1EWK}.
STRAND 201 205 {ECO:0000244|PDB:1EWK}.
HELIX 208 221 {ECO:0000244|PDB:1EWK}.
STRAND 226 234 {ECO:0000244|PDB:1EWK}.
HELIX 235 251 {ECO:0000244|PDB:1EWK}.
STRAND 254 261 {ECO:0000244|PDB:1EWK}.
STRAND 263 265 {ECO:0000244|PDB:1ISS}.
HELIX 267 278 {ECO:0000244|PDB:1EWK}.
TURN 279 283 {ECO:0000244|PDB:1EWK}.
STRAND 286 290 {ECO:0000244|PDB:1EWK}.
HELIX 293 306 {ECO:0000244|PDB:1EWK}.
STRAND 313 316 {ECO:0000244|PDB:1EWK}.
TURN 318 322 {ECO:0000244|PDB:1EWK}.
HELIX 324 327 {ECO:0000244|PDB:1EWK}.
HELIX 331 334 {ECO:0000244|PDB:1EWK}.
STRAND 338 342 {ECO:0000244|PDB:1EWK}.
HELIX 348 354 {ECO:0000244|PDB:1EWK}.
TURN 359 361 {ECO:0000244|PDB:1EWK}.
HELIX 368 375 {ECO:0000244|PDB:1EWK}.
TURN 400 403 {ECO:0000244|PDB:1EWK}.
HELIX 410 431 {ECO:0000244|PDB:1EWK}.
HELIX 440 442 {ECO:0000244|PDB:1EWK}.
HELIX 447 455 {ECO:0000244|PDB:1EWK}.
STRAND 458 460 {ECO:0000244|PDB:1EWK}.
STRAND 466 468 {ECO:0000244|PDB:1EWK}.
STRAND 479 486 {ECO:0000244|PDB:1EWK}.
STRAND 488 490 {ECO:0000244|PDB:1EWK}.
STRAND 492 501 {ECO:0000244|PDB:1EWK}.
STRAND 504 507 {ECO:0000244|PDB:1EWK}.
TURN 509 511 {ECO:0000244|PDB:1EWK}.
SEQUENCE 1199 AA; 133236 MW; EEE5A04C50694B9F CRC64;
MVRLLLIFFP MIFLEMSILP RMPDRKVLLA GASSQRSVAR MDGDVIIGAL FSVHHQPPAE
KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT LGSEIRDSCW HSSVALEQSI
EFIRDSLISI RDEKDGLNRC LPDGQTLPPG RTKKPIAGVI GPGSSSVAIQ VQNLLQLFDI
PQIAYSATSI DLSDKTLYKY FLRVVPSDTL QARAMLDIVK RYNWTYVSAV HTEGNYGESG
MDAFKELAAQ EGLCIAHSDK IYSNAGEKSF DRLLRKLRER LPKARVVVCF CEGMTVRGLL
SAMRRLGVVG EFSLIGSDGW ADRDEVIEGY EVEANGGITI KLQSPEVRSF DDYFLKLRLD
TNTRNPWFPE FWQHRFQCRL PGHLLENPNF KKVCTGNESL EENYVQDSKM GFVINAIYAM
AHGLQNMHHA LCPGHVGLCD AMKPIDGRKL LDFLIKSSFV GVSGEEVWFD EKGDAPGRYD
IMNLQYTEAN RYDYVHVGTW HEGVLNIDDY KIQMNKSGMV RSVCSEPCLK GQIKVIRKGE
VSCCWICTAC KENEFVQDEF TCRACDLGWW PNAELTGCEP IPVRYLEWSD IESIIAIAFS
CLGILVTLFV TLIFVLYRDT PVVKSSSREL CYIILAGIFL GYVCPFTLIA KPTTTSCYLQ
RLLVGLSSAM CYSALVTKTN RIARILAGSK KKICTRKPRF MSAWAQVIIA SILISVQLTL
VVTLIIMEPP MPILSYPSIK EVYLICNTSN LGVVAPVGYN GLLIMSCTYY AFKTRNVPAN
FNEAKYIAFT MYTTCIIWLA FVPIYFGSNY KIITTCFAVS LSVTVALGCM FTPKMYIIIA
KPERNVRSAF TTSDVVRMHV GDGKLPCRSN TFLNIFRRKK PGAGNANSNG KSVSWSEPGG
RQAPKGQHVW QRLSVHVKTN ETACNQTAVI KPLTKSYQGS GKSLTFSDAS TKTLYNVEEE
DNTPSAHFSP PSSPSMVVHR RGPPVATTPP LPPHLTAEET PLFLADSVIP KGLPPPLPQQ
QPQQPPPQQP PQQPKSLMDQ LQGVVTNFGS GIPDFHAVLA GPGTPGNSLR SLYPPPPPPQ
HLQMLPLHLS TFQEESISPP GEDIDDDSER FKLLQEFVYE REGNTEEDEL EEEEDLPTAS
KLTPEDSPAL TPPSPFRDSV ASGSSVPSSP VSESVLCTPP NVTYASVILR DYKQSSSTL


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Y108280 Glutamate Receptor, Metabotropic, 1, (mGluR1 alpha) Antibody 100ug
GWB-7AF86A Anti- Glutamate Receptor Metabotropic 1 (mGluR1 alpha) Antibody
ABP-PAB-40885 Glutamate Receptor, Metabotropic 1 (mGluR1 alpha) Polyclonal Antibody 100 ug
Y052471 Anti-mGluR1 alpha(Glutamate Receptor, Metabotropic, 1) Antibody 100 μg
18-783-78674 RABBIT ANTI METABOTROPIC GLUTAMATE RECEPTOR 2_3 (mGluR2_3) - mGluR1 Polyclonal 0.05 mg
CH23023-100 Glutamate Receptor (Metabotropic) Type 1 (mGluR1), affinity purified antibody, chicken, 100 ul.
Y051677 Anti-mGluR1 (extracellular)(Metabotropic Glutamate receptor 1, GRM1, mGlu1) Antibody 50μl
24426 mGluR1 alpha (Metabotropic Glutamate Receptor) Antibody polyclonal Host Species Rabbit 100 µL
SCH-OBT1702 RABBIT ANTI METABOTROPIC GLUTAMATE RECEPTOR 2_3 (mGluR2_3), Product Type Polyclonal Antibody, Specificity METABOTROPIC GLUTAMATE RECEPTOR 2_3, Target Species Rat, Host Rabbit, Format Purified, Is 50 µg
AHP1871 RABBIT ANTI RAT METABOTROPIC GLUTAMATE RECEPTOR 1a , Product Type Polyclonal Antibody, Specificity METABOTROPIC GLUTAMATE RECEPTOR 1a, Target Species Rat, Host Rabbit, Format Purified, Isotypes 0.1 ml
SCH-AHP1871 RABBIT ANTI RAT METABOTROPIC GLUTAMATE RECEPTOR 1a , Product Type Polyclonal Antibody, Specificity METABOTROPIC GLUTAMATE RECEPTOR 1a, Target Species Rat, Host Rabbit, Format Purified, Isotypes 0.1 ml
SCH-AHP1549 RABBIT ANTI RAT METABOTROPIC GLUTAMATE RECEPTOR 2_3, Product Type Polyclonal Antibody, Specificity METABOTROPIC GLUTAMATE RECEPTOR 2_3, Target Species Rat, Host Rabbit, Format Purified, Isotypes 0.1 ml
AHP1549 RABBIT ANTI RAT METABOTROPIC GLUTAMATE RECEPTOR 2_3, Product Type Polyclonal Antibody, Specificity METABOTROPIC GLUTAMATE RECEPTOR 2_3, Target Species Rat, Host Rabbit, Format Purified, Isotypes 0.1 ml
OBT1702 RABBIT ANTI METABOTROPIC GLUTAMATE RECEPTOR 2_3 (mGluR2_3), Product Type Polyclonal Antibody, Specificity METABOTROPIC GLUTAMATE RECEPTOR 2_3, Target Species Rat, Host Rabbit, Format Purified, Is 50 µg
AHP1550 RABBIT ANTI RAT METABOTROPIC GLUTAMATE RECEPTOR 5_1a, Product Type Polyclonal Antibody, Specificity METABOTROPIC GLUTAMATE RECEPTOR 5_1a, Target Species Rat, Host Rabbit, Format Purified, Isotype 0.1 ml
SCH-AHP1550 RABBIT ANTI RAT METABOTROPIC GLUTAMATE RECEPTOR 5_1a, Product Type Polyclonal Antibody, Specificity METABOTROPIC GLUTAMATE RECEPTOR 5_1a, Target Species Rat, Host Rabbit, Format Purified, Isotype 0.1 ml
LF-PA40529 anti-Metabotropic Glutamate Receptor 5, Rabbit polyclonal to Metabotropic Glutamate Receptor 5, Isotype IgG, Host Rabbit 50 ug


 

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