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Beta-1 adrenergic receptor (Beta-1 adrenoreceptor) (Beta-1 adrenoceptor)

 ADRB1_HUMAN             Reviewed;         477 AA.
P08588; B0LPE2; Q5T5Y4; Q9UKG7; Q9UKG8;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 2.
18-JUL-2018, entry version 190.
RecName: Full=Beta-1 adrenergic receptor;
AltName: Full=Beta-1 adrenoreceptor;
Short=Beta-1 adrenoceptor;
Name=ADRB1; Synonyms=ADRB1R, B1AR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=2825170; DOI=10.1073/pnas.84.22.7920;
Frielle T., Collins S., Daniel K.W., Caron M.G., Lefkowitz R.J.,
Kobilka B.K.;
"Cloning of the cDNA for the human beta 1-adrenergic receptor.";
Proc. Natl. Acad. Sci. U.S.A. 84:7920-7924(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-49 AND GLY-389.
PubMed=10477438;
DOI=10.1002/(SICI)1098-1004(1999)14:3<271::AID-HUMU14>3.3.CO;2-H;
Moore J.D., Mason D.A., Green S.A., Hsu J., Liggett S.B.;
"Racial differences in the frequencies of cardiac beta(1)-adrenergic
receptor polymorphisms: analysis of c145A>G and c1165G>C.";
Hum. Mutat. 14:271-271(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-49; GLY-389 AND
LEU-389.
SeattleSNPs variation discovery resource;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-389.
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
FUNCTION, INTERACTION WITH RAPGEF2, AND MUTAGENESIS OF SER-475 AND
VAL-477.
PubMed=12391161; DOI=10.1128/MCB.22.22.7942-7952.2002;
Pak Y., Pham N., Rotin D.;
"Direct binding of the beta1 adrenergic receptor to the cyclic AMP-
dependent guanine nucleotide exchange factor CNrasGEF leads to Ras
activation.";
Mol. Cell. Biol. 22:7942-7952(2002).
[7]
INTERACTION WITH GOPC AND DLG4, MUTAGENESIS OF GLU-474; SER-475;
LYS-476 AND VAL-477, AND SUBCELLULAR LOCATION.
PubMed=15358775; DOI=10.1074/jbc.M404876200;
He J., Bellini M., Xu J., Castleberry A.M., Hall R.A.;
"Interaction with cystic fibrosis transmembrane conductance regulator-
associated ligand (CAL) inhibits beta1-adrenergic receptor surface
expression.";
J. Biol. Chem. 279:50190-50196(2004).
[8]
SUBCELLULAR LOCATION.
PubMed=21540189; DOI=10.1074/jbc.M111.224071;
Cheng S.B., Quinn J.A., Graeber C.T., Filardo E.J.;
"Down-modulation of the G-protein-coupled estrogen receptor, GPER,
from the cell surface occurs via a trans-Golgi-proteasome pathway.";
J. Biol. Chem. 286:22441-22455(2011).
[9]
VARIANT GLY-389.
PubMed=10212248; DOI=10.1074/jbc.274.18.12670;
Mason D.A., Moore J.D., Green S.A., Liggett S.B.;
"A gain-of-function polymorphism in a G-protein coupling domain of the
human beta1-adrenergic receptor.";
J. Biol. Chem. 274:12670-12674(1999).
[10]
VARIANT GLY-49.
PubMed=11052857; DOI=10.1053/euhj.1999.1994;
Borjesson M., Magnusson Y., Hjalmarson A., Andersson B.;
"A novel polymorphism in the gene coding for the beta(1)-adrenergic
receptor associated with survival in patients with heart failure.";
Eur. Heart J. 21:1853-1858(2000).
[11]
VARIANT GLY-49.
PubMed=11854867; DOI=10.1086/339621;
Ranade K., Jorgenson E., Sheu W.H.-H., Pei D., Hsiung C.A.,
Chiang F.-T., Chen Y.-D.I., Pratt R., Olshen R.A., Curb D., Cox D.R.,
Botstein D., Risch N.;
"A polymorphism in the beta1 adrenergic receptor is associated with
resting heart rate.";
Am. J. Hum. Genet. 70:935-942(2002).
-!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine-
induced activation of adenylate cyclase through the action of G
proteins. This receptor binds epinephrine and norepinephrine with
approximately equal affinity. Mediates Ras activation through
G(s)-alpha- and cAMP-mediated signaling.
{ECO:0000269|PubMed:12391161}.
-!- SUBUNIT: Interacts (via C-terminus PDZ motif) with RAPGEF2; the
interaction is direct. Interacts with GOPC, MAGI3 and DLG4.
{ECO:0000269|PubMed:12391161, ECO:0000269|PubMed:15358775}.
-!- INTERACTION:
P21917:DRD4; NbExp=2; IntAct=EBI-991009, EBI-8592297;
Q86UL8:MAGI2; NbExp=7; IntAct=EBI-991009, EBI-311035;
Q5TCQ9:MAGI3; NbExp=5; IntAct=EBI-991009, EBI-310506;
P14270:Pde4d (xeno); NbExp=2; IntAct=EBI-991009, EBI-8333209;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Early endosome. Note=Colocalizes with RAPGEF2 at the plasma
membrane (By similarity). Localized at the plasma membrane. Found
in the Golgi upon GOPC overexpression. {ECO:0000250}.
-!- DOMAIN: The PDZ domain-binding motif mediates competitive
interactions with GOPC, MAGI3 and DLG4 and plays a role in
subcellular location of the receptor.
-!- PTM: Homologous desensitization of the receptor is mediated by its
phosphorylation by beta-adrenergic receptor kinase.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
Adrenergic receptor subfamily. ADRB1 sub-subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/adrb1/";
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EMBL; J03019; AAA51667.1; -; mRNA.
EMBL; AF169006; AAD53696.1; -; Genomic_DNA.
EMBL; AF169007; AAD53697.1; -; Genomic_DNA.
EMBL; AY567837; AAS66983.1; -; Genomic_DNA.
EMBL; EU332832; ABY87521.1; -; Genomic_DNA.
EMBL; AL355543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS7586.1; -.
PIR; A39911; QRHUB1.
RefSeq; NP_000675.1; NM_000684.2.
UniGene; Hs.99913; -.
PDB; 2LSQ; NMR; -; A=197-221.
PDBsum; 2LSQ; -.
ProteinModelPortal; P08588; -.
SMR; P08588; -.
BioGrid; 106662; 8.
CORUM; P08588; -.
DIP; DIP-36294N; -.
IntAct; P08588; 13.
MINT; P08588; -.
STRING; 9606.ENSP00000358301; -.
BindingDB; P08588; -.
ChEMBL; CHEMBL213; -.
DrugBank; DB08347; 4-{[(2S)-3-(tert-butylamino)-2-hydroxypropyl]oxy}-3H-indole-2-carbonitrile.
DrugBank; DB01193; Acebutolol.
DrugBank; DB00866; Alprenolol.
DrugBank; DB01118; Amiodarone.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB00182; Amphetamine.
DrugBank; DB01102; Arbutamine.
DrugBank; DB06216; Asenapine.
DrugBank; DB00335; Atenolol.
DrugBank; DB00195; Betaxolol.
DrugBank; DB00217; Bethanidine.
DrugBank; DB01295; Bevantolol.
DrugBank; DB00612; Bisoprolol.
DrugBank; DB08807; Bopindolol.
DrugBank; DB06726; Bufuralol.
DrugBank; DB08808; Bupranolol.
DrugBank; DB00248; Cabergoline.
DrugBank; DB00521; Carteolol.
DrugBank; DB01136; Carvedilol.
DrugBank; DB04846; Celiprolol.
DrugBank; DB01407; Clenbuterol.
DrugBank; DB01151; Desipramine.
DrugBank; DB00841; Dobutamine.
DrugBank; DB04855; Dronedarone.
DrugBank; DB06262; Droxidopa.
DrugBank; DB01363; Ephedra.
DrugBank; DB00668; Epinephrine.
DrugBank; DB00187; Esmolol.
DrugBank; DB01288; Fenoterol.
DrugBank; DB00221; Isoetarine.
DrugBank; DB01064; Isoprenaline.
DrugBank; DB00598; Labetalol.
DrugBank; DB01210; Levobunolol.
DrugBank; DB00408; Loxapine.
DrugBank; DB01365; Mephentermine.
DrugBank; DB01214; Metipranolol.
DrugBank; DB00264; Metoprolol.
DrugBank; DB00370; Mirtazapine.
DrugBank; DB01203; Nadolol.
DrugBank; DB04861; Nebivolol.
DrugBank; DB00368; Norepinephrine.
DrugBank; DB00540; Nortriptyline.
DrugBank; DB00334; Olanzapine.
DrugBank; DB01580; Oxprenolol.
DrugBank; DB01359; Penbutolol.
DrugBank; DB00397; Phenylpropanolamine.
DrugBank; DB00960; Pindolol.
DrugBank; DB01291; Pirbuterol.
DrugBank; DB01297; Practolol.
DrugBank; DB00571; Propranolol.
DrugBank; DB00852; Pseudoephedrine.
DrugBank; DB01001; Salbutamol.
DrugBank; DB00489; Sotalol.
DrugBank; DB00373; Timolol.
DrugBank; DB00726; Trimipramine.
DrugBank; DB09068; Vortioxetine.
GuidetoPHARMACOLOGY; 28; -.
TCDB; 9.A.14.3.11; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P08588; -.
PhosphoSitePlus; P08588; -.
SwissPalm; P08588; -.
BioMuta; ADRB1; -.
DMDM; 48429211; -.
PaxDb; P08588; -.
PeptideAtlas; P08588; -.
PRIDE; P08588; -.
ProteomicsDB; 52133; -.
Ensembl; ENST00000369295; ENSP00000358301; ENSG00000043591.
GeneID; 153; -.
KEGG; hsa:153; -.
UCSC; uc001lba.4; human.
CTD; 153; -.
DisGeNET; 153; -.
EuPathDB; HostDB:ENSG00000043591.5; -.
GeneCards; ADRB1; -.
H-InvDB; HIX0035626; -.
HGNC; HGNC:285; ADRB1.
HPA; HPA067972; -.
MalaCards; ADRB1; -.
MIM; 109630; gene.
MIM; 607276; phenotype.
neXtProt; NX_P08588; -.
PharmGKB; PA38; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
HOGENOM; HOG000239242; -.
HOVERGEN; HBG106962; -.
InParanoid; P08588; -.
KO; K04141; -.
OrthoDB; EOG091G06VI; -.
PhylomeDB; P08588; -.
TreeFam; TF316350; -.
Reactome; R-HSA-390696; Adrenoceptors.
Reactome; R-HSA-418555; G alpha (s) signalling events.
SignaLink; P08588; -.
SIGNOR; P08588; -.
GeneWiki; Beta-1_adrenergic_receptor; -.
GenomeRNAi; 153; -.
PRO; PR:P08588; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000043591; -.
CleanEx; HS_ADRB1; -.
Genevisible; P08588; HS.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031694; F:alpha-2A adrenergic receptor binding; IPI:BHF-UCL.
GO; GO:0004939; F:beta-adrenergic receptor activity; TAS:ProtInc.
GO; GO:0004940; F:beta1-adrenergic receptor activity; IBA:GO_Central.
GO; GO:0051379; F:epinephrine binding; IBA:GO_Central.
GO; GO:0051380; F:norepinephrine binding; IBA:GO_Central.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IDA:UniProtKB.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
GO; GO:0042596; P:fear response; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0031649; P:heat generation; IEA:Ensembl.
GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0002025; P:norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure; IBA:GO_Central.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IBA:GO_Central.
GO; GO:0001997; P:positive regulation of the force of heart contraction by epinephrine-norepinephrine; IEA:Ensembl.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0001659; P:temperature homeostasis; IBA:GO_Central.
InterPro; IPR002233; ADR_fam.
InterPro; IPR000507; ADRB1_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR01103; ADRENERGICR.
PRINTS; PR00561; ADRENRGCB1AR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Endosome; G-protein coupled receptor; Glycoprotein; Lipoprotein;
Membrane; Palmitate; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 477 Beta-1 adrenergic receptor.
/FTId=PRO_0000069118.
TOPO_DOM 1 55 Extracellular. {ECO:0000250}.
TRANSMEM 56 84 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 85 93 Cytoplasmic. {ECO:0000250}.
TRANSMEM 94 120 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 121 132 Extracellular. {ECO:0000250}.
TRANSMEM 133 154 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 155 172 Cytoplasmic. {ECO:0000250}.
TRANSMEM 173 196 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 197 222 Extracellular. {ECO:0000250}.
TRANSMEM 223 248 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 249 319 Cytoplasmic. {ECO:0000250}.
TRANSMEM 320 349 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 350 354 Extracellular. {ECO:0000250}.
TRANSMEM 355 377 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 378 477 Cytoplasmic. {ECO:0000250}.
REGION 218 232 Agonist and antagonist binding.
{ECO:0000250}.
REGION 337 344 Agonist and antagonist binding.
{ECO:0000250}.
REGION 363 367 Agonist and antagonist binding.
{ECO:0000250}.
MOTIF 474 477 PDZ-Binding.
BINDING 138 138 Agonist or antagonist. {ECO:0000250}.
BINDING 143 143 Agonist or antagonist. {ECO:0000250}.
MOD_RES 312 312 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 412 412 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 428 428 Phosphoserine.
{ECO:0000250|UniProtKB:P18090}.
LIPID 392 392 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 15 15 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 131 216 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 209 215 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VARIANT 26 26 A -> V (in dbSNP:rs34844626).
/FTId=VAR_055909.
VARIANT 29 29 A -> T (in dbSNP:rs35720093).
/FTId=VAR_055910.
VARIANT 31 31 R -> Q (in dbSNP:rs35230616).
/FTId=VAR_055911.
VARIANT 49 49 S -> G (associated with high mean resting
heart rate; dbSNP:rs1801252).
{ECO:0000269|PubMed:10477438,
ECO:0000269|PubMed:11052857,
ECO:0000269|PubMed:11854867,
ECO:0000269|Ref.3}.
/FTId=VAR_009879.
VARIANT 389 389 R -> G (reduced binding to G proteins;
dbSNP:rs1801253).
{ECO:0000269|PubMed:10212248,
ECO:0000269|PubMed:10477438,
ECO:0000269|PubMed:15164054,
ECO:0000269|Ref.3}.
/FTId=VAR_009880.
VARIANT 389 389 R -> L. {ECO:0000269|Ref.3}.
/FTId=VAR_018742.
VARIANT 399 399 R -> H (in dbSNP:rs36052953).
/FTId=VAR_055912.
VARIANT 405 405 H -> Y (in dbSNP:rs35705839).
/FTId=VAR_055913.
MUTAGEN 474 474 E->A,D: Loss of interaction with GOPC.
{ECO:0000269|PubMed:15358775}.
MUTAGEN 474 474 E->K: Loss of interaction with GOPC; when
associated with A-477.
{ECO:0000269|PubMed:15358775}.
MUTAGEN 475 475 S->A: Loss of interaction with GOPC. Loss
of interaction with RAPGEF2. Abolishes
agonist-induced Ras activation.
{ECO:0000269|PubMed:12391161,
ECO:0000269|PubMed:15358775}.
MUTAGEN 475 475 S->D: Loss of interaction with RAPGEF2.
{ECO:0000269|PubMed:12391161,
ECO:0000269|PubMed:15358775}.
MUTAGEN 475 475 S->T: Partial loss of interaction with
GOPC. {ECO:0000269|PubMed:12391161,
ECO:0000269|PubMed:15358775}.
MUTAGEN 476 476 K->A: Partial loss of interaction with
GOPC. {ECO:0000269|PubMed:15358775}.
MUTAGEN 477 477 V->A,F,L,I,M: Loss of interaction with
GOPC. {ECO:0000269|PubMed:12391161,
ECO:0000269|PubMed:15358775}.
MUTAGEN 477 477 V->A: Loss of interaction with RAPGEF2.
Abolishes agonist-induced Ras activation.
{ECO:0000269|PubMed:12391161,
ECO:0000269|PubMed:15358775}.
HELIX 205 208 {ECO:0000244|PDB:2LSQ}.
HELIX 209 211 {ECO:0000244|PDB:2LSQ}.
HELIX 213 215 {ECO:0000244|PDB:2LSQ}.
SEQUENCE 477 AA; 51323 MW; 0950F2684E4721B8 CRC64;
MGAGVLVLGA SEPGNLSSAA PLPDGAATAA RLLVPASPPA SLLPPASESP EPLSQQWTAG
MGLLMALIVL LIVAGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV
WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARGLVC
TVWAISALVS FLPILMHWWR AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM
AFVYLRVFRE AQKQVKKIDS CERRFLGGPA RPPSPSPSPV PAPAPPPGPP RPAAAAATAP
LANGRAGKRR PSRLVALREQ KALKTLGIIM GVFTLCWLPF FLANVVKAFH RELVPDRLFV
FFNWLGYANS AFNPIIYCRS PDFRKAFQRL LCCARRAARR RHATHGDRPR ASGCLARPGP
PPSPGAASDD DDDDVVGATP PARLLEPWAG CNGGAAADSD SSLDEPCRPG FASESKV


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E1298h ELISA kit ADRA1A,ADRA1C,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Alpha-adrenergic receptor 1c,Homo sapiens,Human 96T
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U1298Rb CLIA ADRA1A,ADRA1C,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Oryctolagus cuniculus,Rabbit 96T
E1298Rb ELISA kit ADRA1A,ADRA1C,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Oryctolagus cuniculus,Rabbit 96T
E1298r ELISA Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Rat,Rattus norvegicus 96T
U1298r CLIA Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Rat,Rattus norvegicus 96T
U1298b CLIA ADRA1A,ADRA1C,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Bos taurus,Bovine 96T
E1298b ELISA ADRA1A,ADRA1C,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Bos taurus,Bovine 96T
E1298m ELISA kit Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Mouse,Mus musculus 96T
E1298b ELISA kit ADRA1A,ADRA1C,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Bos taurus,Bovine 96T
E1298m ELISA Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Mouse,Mus musculus 96T
U1298m CLIA Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Mouse,Mus musculus 96T
E1298r ELISA kit Adra1a,Adra1c,Alpha-1A adrenergic receptor,Alpha-1A adrenoceptor,Alpha-1A adrenoreceptor,Alpha-1C adrenergic receptor,Rat,Rattus norvegicus 96T
18-461-10500 Alpha-2C adrenergic receptor - Alpha-2C adrenoceptor; Alpha-2C adrenoreceptor; Alpha-2 adrenergic receptor subtype C4 Polyclonal 0.05 ml
18-461-10552 Alpha-2C adrenergic receptor - Alpha-2C adrenoceptor; Alpha-2C adrenoreceptor; Alpha-2 adrenergic receptor subtype C4 Polyclonal 0.05 ml


 

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