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

Inward rectifier potassium channel 2 (Cardiac inward rectifier potassium channel) (Inward rectifier K( ) channel Kir2.1) (IRK-1) (hIRK1) (Potassium channel, inwardly rectifying subfamily J member 2)

 KCNJ2_HUMAN             Reviewed;         427 AA.
P63252; O15110; P48049;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
25-OCT-2017, entry version 143.
RecName: Full=Inward rectifier potassium channel 2;
AltName: Full=Cardiac inward rectifier potassium channel;
AltName: Full=Inward rectifier K(+) channel Kir2.1;
Short=IRK-1;
Short=hIRK1;
AltName: Full=Potassium channel, inwardly rectifying subfamily J member 2;
Name=KCNJ2; Synonyms=IRK1;
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=Heart;
PubMed=7696590;
Raab-Graham K.F., Radeke C.M., Vandenberg C.A.;
"Molecular cloning and expression of a human heart inward rectifier
potassium channel.";
NeuroReport 5:2501-2505(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Tang W., Qin C.L., Yang X.C.;
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=7590287; DOI=10.1016/0378-1119(95)00244-Z;
Wood L.S., Tsai T.-D., Lee K.S., Vogeli G.;
"Cloning and functional expression of a human gene, hIRK1, encoding
the heart inward rectifier K+-channel.";
Gene 163:313-317(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
PubMed=9490857; DOI=10.1111/j.1469-7793.1998.303bw.x;
Tare M., Prestwich S.A., Gordienko D.V., Parveen S., Carver J.E.,
Robinson C., Bolton T.B.;
"Inwardly rectifying whole cell potassium current in human blood
eosinophils.";
J. Physiol. (Lond.) 506:303-318(1998).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=11240146; DOI=10.1016/S0014-5793(01)02202-5;
Derst C., Karschin C., Wischmeyer E., Hirsch J.R., Preisig-Muller R.,
Rajan S., Engel H., Grzeschik K., Daut J., Karschin A.;
"Genetic and functional linkage of Kir5.1 and Kir2.1 channel
subunits.";
FEBS Lett. 491:305-311(2001).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-143.
TISSUE=Fetal brain, and Heart;
PubMed=7840300;
Ashen M.D., O'Rourke B., Kluge K.A., Johns D.C., Tomaselli G.F.;
"Inward rectifier K+ channel from human heart and brain: cloning and
stable expression in a human cell line.";
Am. J. Physiol. 268:H506-H511(1995).
[7]
INTERACTION WITH KCNJ4.
PubMed=12032359; DOI=10.1073/pnas.102609499;
Preisig-Muller R., Schlichthorl G., Goerge T., Heinen S.,
Bruggemann A., Rajan S., Derst C., Veh R.W., Daut J.;
"Heteromerization of Kir2.x potassium channels contributes to the
phenotype of Andersen's syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 99:7774-7779(2002).
[8]
S-NITROSYLATION AT CYS-76.
PubMed=19608980; DOI=10.1161/CIRCRESAHA.109.197558;
Gomez R., Caballero R., Barana A., Amoros I., Calvo E., Lopez J.A.,
Klein H., Vaquero M., Osuna L., Atienza F., Almendral J., Pinto A.,
Tamargo J., Delpon E.;
"Nitric oxide increases cardiac IK1 by nitrosylation of cysteine 76 of
Kir2.1 channels.";
Circ. Res. 105:383-392(2009).
[9]
MYRISTOYLATION AT GLY-2, AND SUBCELLULAR LOCATION.
PubMed=25043870; DOI=10.1016/j.ab.2014.07.006;
Takamitsu E., Fukunaga K., Iio Y., Moriya K., Utsumi T.;
"Cell-free identification of novel N-myristoylated proteins from
complementary DNA resources using bioorthogonal myristic acid
analogues.";
Anal. Biochem. 464:83-93(2014).
[10]
CHARACTERIZATION OF VARIANTS LQT7 VAL-71 AND TRP-218, AND VARIANTS
LQT7 VAL-300; 95-SER--PHE-98 DEL AND SER-314-315-TYR DEL.
PubMed=11371347; DOI=10.1016/S0092-8674(01)00342-7;
Plaster N.M., Tawil R., Tristani-Firouzi M., Canun S., Bendahhou S.,
Tsunoda A., Donaldson M.R., Iannaccone S.T., Brunt E., Barohn R.,
Clark J., Deymeer F., George A.L. Jr., Fish F.A., Hahn A., Nitu A.,
Ozdemir C., Serdaroglu P., Subramony S.H., Wolfe G., Fu Y.-H.,
Ptacek L.J.;
"Mutations in Kir2.1 cause the developmental and episodic electrical
phenotypes of Andersen's syndrome.";
Cell 105:511-519(2001).
[11]
VARIANT LQT7 TRP-67.
PubMed=12148092; DOI=10.1086/342360;
Andelfinger G., Tapper A.R., Welch R.C., Vanoye C.G., George A.L. Jr.,
Benson D.W.;
"KCNJ2 mutation results in Andersen syndrome with sex-specific cardiac
and skeletal muscle phenotypes.";
Am. J. Hum. Genet. 71:663-668(2002).
[12]
VARIANTS LQT7 LEU-186; HIS-216 AND MET-302.
PubMed=12163457; DOI=10.1172/JCI15183;
Tristani-Firouzi M., Jensen J.L., Donaldson M.R., Sansone V.,
Meola G., Hahn A., Bendahhou S., Kwiecinski H., Fidzianska A.,
Plaster N., Fu Y.-H., Ptacek L.J., Tawil R.;
"Functional and clinical characterization of KCNJ2 mutations
associated with LQT7 (Andersen syndrome).";
J. Clin. Invest. 110:381-388(2002).
[13]
VARIANT ATFB9 ILE-93, AND CHARACTERIZATION OF VARIANT ATFB9 ILE-93.
PubMed=15922306; DOI=10.1016/j.bbrc.2005.05.054;
Xia M., Jin Q., Bendahhou S., He Y., Larroque M.M., Chen Y., Zhou Q.,
Yang Y., Liu Y., Liu B., Zhu Q., Zhou Y., Lin J., Liang B., Li L.,
Dong X., Pan Z., Wang R., Wan H., Qiu W., Xu W., Eurlings P.,
Barhanin J., Chen Y.;
"A Kir2.1 gain-of-function mutation underlies familial atrial
fibrillation.";
Biochem. Biophys. Res. Commun. 332:1012-1019(2005).
[14]
VARIANT SQT3 ASN-172, AND CHARACTERIZATION OF VARIANT SQT3 ASN-172.
PubMed=15761194; DOI=10.1161/01.RES.0000162101.76263.8c;
Priori S.G., Pandit S.V., Rivolta I., Berenfeld O., Ronchetti E.,
Dhamoon A., Napolitano C., Anumonwo J., di Barletta M.R.,
Gudapakkam S., Bosi G., Stramba-Badiale M., Jalife J.;
"A novel form of short QT syndrome (SQT3) is caused by a mutation in
the KCNJ2 gene.";
Circ. Res. 96:800-807(2005).
[15]
VARIANT LQT7 ARG-75, AND CHARACTERIZATION OF VARIANT LQT7 ARG-75.
PubMed=16571646; DOI=10.1136/jmg.2006.040816;
Lu C.W., Lin J.H., Rajawat Y.S., Jerng H., Rami T.G., Sanchez X.,
DeFreitas G., Carabello B., DeMayo F., Kearney D.L., Miller G., Li H.,
Pfaffinger P.J., Bowles N.E., Khoury D.S., Towbin J.A.;
"Functional and clinical characterization of a mutation in KCNJ2
associated with Andersen-Tawil syndrome.";
J. Med. Genet. 43:653-659(2006).
[16]
VARIANTS LQT7 PHE-54 AND PRO-305, AND CHARACTERIZATION OF VARIANTS
LQT7 PHE-54 AND PRO-305.
PubMed=17324964; DOI=10.1093/hmg/ddm034;
Bendahhou S., Fournier E., Gallet S., Menard D., Larroque M.M.,
Barhanin J.;
"Corticosteroid-exacerbated symptoms in an Andersen's syndrome
kindred.";
Hum. Mol. Genet. 16:900-906(2007).
-!- FUNCTION: Probably participates in establishing action potential
waveform and excitability of neuronal and muscle tissues. Inward
rectifier potassium channels are characterized by a greater
tendency to allow potassium to flow into the cell rather than out
of it. Their voltage dependence is regulated by the concentration
of extracellular potassium; as external potassium is raised, the
voltage range of the channel opening shifts to more positive
voltages. The inward rectification is mainly due to the blockage
of outward current by internal magnesium. Can be blocked by
extracellular barium or cesium.
-!- SUBUNIT: Homomultimeric and heteromultimeric association with
KCNJ4/Kir2.3. Association, via its PDZ-recognition domain, with
LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1 plays a key role in its
localization and trafficking (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
Membrane; Lipid-anchor {ECO:0000269|PubMed:25043870}.
-!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, skeletal muscle,
and kidney. Diffusely distributed throughout the brain.
-!- PTM: S-nitrosylation increases the open probability and inward
rectifying currents. {ECO:0000269|PubMed:19608980}.
-!- DISEASE: Long QT syndrome 7 (LQT7) [MIM:170390]: A heart disorder
characterized by a prolonged QT interval on the ECG and
polymorphic ventricular arrhythmias. They cause syncope and sudden
death in response to exercise or emotional stress, and can present
with a sentinel event of sudden cardiac death in infancy. Long QT
syndrome type 7 manifests itself as a clinical triad consisting of
potassium-sensitive periodic paralysis, ventricular ectopy and
dysmorphic features. {ECO:0000269|PubMed:11371347,
ECO:0000269|PubMed:12148092, ECO:0000269|PubMed:12163457,
ECO:0000269|PubMed:16571646, ECO:0000269|PubMed:17324964}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Short QT syndrome 3 (SQT3) [MIM:609622]: A heart disorder
characterized by idiopathic persistently and uniformly short QT
interval on ECG in the absence of structural heart disease in
affected individuals. It causes syncope and sudden death. SQT3 has
a unique ECG phenotype characterized by asymmetrical T waves.
{ECO:0000269|PubMed:15761194}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Atrial fibrillation, familial, 9 (ATFB9) [MIM:613980]: A
familial form of atrial fibrillation, a common sustained cardiac
rhythm disturbance. Atrial fibrillation is characterized by
disorganized atrial electrical activity and ineffective atrial
contraction promoting blood stasis in the atria and reduces
ventricular filling. It can result in palpitations, syncope,
thromboembolic stroke, and congestive heart failure.
{ECO:0000269|PubMed:15922306}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
(TC 1.A.2.1) family. KCNJ2 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U24055; AAB50277.1; -; mRNA.
EMBL; U12507; AAC50072.1; -; mRNA.
EMBL; U16861; AAA91781.1; -; mRNA.
EMBL; AF153819; AAF73242.1; -; Genomic_DNA.
EMBL; AF153820; AAF73241.1; -; mRNA.
EMBL; U22413; AAA64282.1; -; mRNA.
EMBL; AF011904; AAC39555.1; -; mRNA.
EMBL; AF021139; AAB88797.1; -; mRNA.
CCDS; CCDS11688.1; -.
PIR; I38727; I38727.
RefSeq; NP_000882.1; NM_000891.2.
UniGene; Hs.1547; -.
ProteinModelPortal; P63252; -.
SMR; P63252; -.
BioGrid; 109961; 3.
IntAct; P63252; 5.
STRING; 9606.ENSP00000243457; -.
BindingDB; P63252; -.
ChEMBL; CHEMBL1914276; -.
TCDB; 1.A.2.1.2; the inward rectifier k(+) channel (irk-c) family.
iPTMnet; P63252; -.
PhosphoSitePlus; P63252; -.
BioMuta; KCNJ2; -.
DMDM; 54037433; -.
PaxDb; P63252; -.
PeptideAtlas; P63252; -.
PRIDE; P63252; -.
DNASU; 3759; -.
Ensembl; ENST00000243457; ENSP00000243457; ENSG00000123700.
Ensembl; ENST00000535240; ENSP00000441848; ENSG00000123700.
GeneID; 3759; -.
KEGG; hsa:3759; -.
UCSC; uc002jir.4; human.
CTD; 3759; -.
DisGeNET; 3759; -.
EuPathDB; HostDB:ENSG00000123700.4; -.
GeneCards; KCNJ2; -.
GeneReviews; KCNJ2; -.
HGNC; HGNC:6263; KCNJ2.
HPA; HPA029109; -.
MalaCards; KCNJ2; -.
MIM; 170390; phenotype.
MIM; 600681; gene.
MIM; 609622; phenotype.
MIM; 613980; phenotype.
neXtProt; NX_P63252; -.
OpenTargets; ENSG00000123700; -.
Orphanet; 37553; Cardiodysrhythmic potassium-sensitive periodic paralysis.
Orphanet; 334; Familial atrial fibrillation.
Orphanet; 51083; Familial short QT syndrome.
PharmGKB; PA214; -.
eggNOG; KOG3827; Eukaryota.
eggNOG; ENOG410XQ62; LUCA.
GeneTree; ENSGT00760000118842; -.
HOGENOM; HOG000237325; -.
HOVERGEN; HBG006178; -.
InParanoid; P63252; -.
KO; K04996; -.
OMA; VFSHNAT; -.
OrthoDB; EOG091G08HC; -.
PhylomeDB; P63252; -.
TreeFam; TF313676; -.
Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
Reactome; R-HSA-1296053; Classical Kir channels.
Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
GeneWiki; Kir2.1; -.
GenomeRNAi; 3759; -.
PRO; PR:P63252; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000123700; -.
CleanEx; HS_KCNJ2; -.
Genevisible; P63252; HS.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0031224; C:intrinsic component of membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
GO; GO:0030315; C:T-tubule; IEA:Ensembl.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:BHF-UCL.
GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; IMP:BHF-UCL.
GO; GO:0061337; P:cardiac conduction; TAS:Reactome.
GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IMP:BHF-UCL.
GO; GO:0030007; P:cellular potassium ion homeostasis; TAS:BHF-UCL.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0015693; P:magnesium ion transport; IEA:Ensembl.
GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; TAS:BHF-UCL.
GO; GO:0086011; P:membrane repolarization during action potential; IMP:BHF-UCL.
GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IEA:Ensembl.
GO; GO:0010107; P:potassium ion import; IDA:BHF-UCL.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:BHF-UCL.
GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IEA:Ensembl.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL.
GO; GO:0060075; P:regulation of resting membrane potential; TAS:BHF-UCL.
GO; GO:0014861; P:regulation of skeletal muscle contraction via regulation of action potential; IMP:BHF-UCL.
GO; GO:0055119; P:relaxation of cardiac muscle; IMP:BHF-UCL.
GO; GO:0090076; P:relaxation of skeletal muscle; IMP:BHF-UCL.
Gene3D; 2.60.40.1400; -; 1.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR016449; K_chnl_inward-rec_Kir.
InterPro; IPR003271; K_chnl_inward-rec_Kir2.1.
InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
InterPro; IPR013673; K_chnl_inward-rec_Kir_N.
PANTHER; PTHR11767; PTHR11767; 1.
PANTHER; PTHR11767:SF43; PTHR11767:SF43; 1.
Pfam; PF01007; IRK; 1.
Pfam; PF08466; IRK_N; 1.
PIRSF; PIRSF005465; GIRK_kir; 1.
PRINTS; PR01324; KIR21CHANNEL.
PRINTS; PR01320; KIRCHANNEL.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
Atrial fibrillation; Complete proteome; Disease mutation; Ion channel;
Ion transport; Lipoprotein; Long QT syndrome; Membrane; Myristate;
Potassium; Potassium transport; Reference proteome; S-nitrosylation;
Short QT syndrome; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25043870}.
CHAIN 2 427 Inward rectifier potassium channel 2.
/FTId=PRO_0000154923.
TOPO_DOM 2 81 Cytoplasmic. {ECO:0000250}.
TRANSMEM 82 106 Helical; Name=M1. {ECO:0000250}.
TOPO_DOM 107 128 Extracellular. {ECO:0000250}.
INTRAMEM 129 140 Helical; Pore-forming; Name=H5.
{ECO:0000250}.
INTRAMEM 141 147 Pore-forming. {ECO:0000250}.
TOPO_DOM 148 156 Extracellular. {ECO:0000250}.
TRANSMEM 157 178 Helical; Name=M2. {ECO:0000250}.
TOPO_DOM 179 427 Cytoplasmic. {ECO:0000250}.
MOTIF 142 147 Selectivity filter. {ECO:0000250}.
MOTIF 425 427 PDZ-binding. {ECO:0000255}.
SITE 172 172 Role in the control of polyamine-mediated
channel gating and in the blocking by
intracellular magnesium. {ECO:0000250}.
MOD_RES 76 76 S-nitrosocysteine.
{ECO:0000269|PubMed:19608980}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25043870}.
VARIANT 54 54 C -> F (in LQT7; there is loss of
function when the mutant is expressed
alone and a dominant-negative effect when
expressed with wild-type channels;
channel trafficking and assembly are not
affected; dbSNP:rs199473650).
{ECO:0000269|PubMed:17324964}.
/FTId=VAR_065861.
VARIANT 67 67 R -> W (in LQT7; dbSNP:rs104894580).
{ECO:0000269|PubMed:12148092}.
/FTId=VAR_017851.
VARIANT 71 71 D -> V (in LQT7; loss of function
mutation acting in a dominant-negative
manner; dbSNP:rs104894575).
{ECO:0000269|PubMed:11371347}.
/FTId=VAR_017852.
VARIANT 75 75 T -> R (in LQT7; loss of function
mutation acting in a dominant-negative
manner; dbSNP:rs104894585).
{ECO:0000269|PubMed:16571646}.
/FTId=VAR_065862.
VARIANT 93 93 V -> I (in ATFB9; has a gain-of-function
effect on the channels;
dbSNP:rs147750704).
{ECO:0000269|PubMed:15922306}.
/FTId=VAR_065863.
VARIANT 95 98 Missing (in LQT7).
{ECO:0000269|PubMed:11371347}.
/FTId=VAR_017853.
VARIANT 172 172 D -> N (in SQT3; gain of function;
dbSNP:rs104894584).
{ECO:0000269|PubMed:15761194}.
/FTId=VAR_023842.
VARIANT 186 186 P -> L (in LQT7; dbSNP:rs104894581).
{ECO:0000269|PubMed:12163457}.
/FTId=VAR_017854.
VARIANT 216 216 N -> H (in LQT7; dbSNP:rs104894583).
{ECO:0000269|PubMed:12163457}.
/FTId=VAR_017855.
VARIANT 218 218 R -> W (in LQT7; loss of function and
dominant-negative effect in current;
dbSNP:rs104894578).
{ECO:0000269|PubMed:11371347}.
/FTId=VAR_017856.
VARIANT 300 300 G -> V (in LQT7; dbSNP:rs104894579).
{ECO:0000269|PubMed:11371347}.
/FTId=VAR_017857.
VARIANT 302 302 V -> M (in LQT7; dbSNP:rs104894582).
{ECO:0000269|PubMed:12163457}.
/FTId=VAR_017858.
VARIANT 305 305 T -> P (in LQT7; there is loss of
function when the mutant is expressed
alone and a dominant-negative effect when
expressed with wild-type channels;
channel trafficking and assembly are not
affected; dbSNP:rs199473387).
{ECO:0000269|PubMed:17324964}.
/FTId=VAR_065864.
VARIANT 314 315 Missing (in LQT7).
/FTId=VAR_017859.
CONFLICT 330 330 L -> F (in Ref. 4; AAC39555).
{ECO:0000305}.
CONFLICT 340 340 D -> E (in Ref. 4; AAC39555).
{ECO:0000305}.
SEQUENCE 427 AA; 48288 MW; AB37CAD4B99B4050 CRC64;
MGSVRTNRYS IVSSEEDGMK LATMAVANGF GNGKSKVHTR QQCRSRFVKK DGHCNVQFIN
VGEKGQRYLA DIFTTCVDIR WRWMLVIFCL AFVLSWLFFG CVFWLIALLH GDLDASKEGK
ACVSEVNSFT AAFLFSIETQ TTIGYGFRCV TDECPIAVFM VVFQSIVGCI IDAFIIGAVM
AKMAKPKKRN ETLVFSHNAV IAMRDGKLCL MWRVGNLRKS HLVEAHVRAQ LLKSRITSEG
EYIPLDQIDI NVGFDSGIDR IFLVSPITIV HEIDEDSPLY DLSKQDIDNA DFEIVVILEG
MVEATAMTTQ CRSSYLANEI LWGHRYEPVL FEEKHYYKVD YSRFHKTYEV PNTPLCSARD
LAEKKYILSN ANSFCYENEV ALTSKEEDDS ENGVPESTST DTPPDIDLHN QASVPLEPRP
LRRESEI


Related products :

Catalog number Product name Quantity
28-297 This gene encodes a member of the potassium channel, voltage-gated, subfamily H. This member is a pore-forming (alpha) subunit of a voltage-gated non-inactivating delayed rectifier potassium channel. 0.1 mg
Y062354 Anti-Potassium Channel Kv<_SUB>1.6 (Voltage-gated, Delayed-Rectifier Potassium Channel; RCK2; KV2) produced in rabbit Antibody 100ul
18-003-42642 Potassium channel subfamily K member 10 - Outward rectifying potassium channel protein TREK-2; TREK-2 K(+) channel subunit Polyclonal 0.1 mg Protein A
18-003-42641 Potassium channel subfamily K member 10 - Outward rectifying potassium channel protein TREK-2; TREK-2 K(+) channel subunit Polyclonal 0.1 mg Protein A
18-003-42653 Potassium channel subfamily K member 10 - Outward rectifying potassium channel protein TREK-2; TREK-2 K(+) channel subunit Polyclonal 0.1 mg Protein A
E1040Ra Rat ATP-sensitive inward rectifier potassium channel 12,KCNJ12-Kir2.2 ELISA Kit 96T
E1040Ra Rat ATP-sensitive inward rectifier potassium channel 12,KCNJ12 per Kir2.2 ELISA Kit 48T
E1042Ra Rat ATP-sensitive inward rectifier potassium channel 14,KCNJ14 per Kir2.4 ELISA Kit 48T
YHB0134Ra Rat ATP-sensitive inward rectifier potassium channel 12,KCNJ12-Kir2.2 ELISA Kit 48T
E1042Ra Rat ATP-sensitive inward rectifier potassium channel 14,KCNJ14 per Kir2.4 ELISA Kit 96T
YHB0135Ra Rat ATP-sensitive inward rectifier potassium channel 14,KCNJ14-Kir2.4 ELISA Kit 96T
YHB0134Ra Rat ATP-sensitive inward rectifier potassium channel 12,KCNJ12-Kir2.2 ELISA Kit 96T
YHB0135Ra Rat ATP-sensitive inward rectifier potassium channel 14,KCNJ14-Kir2.4 ELISA Kit 48T
E1042Ra Rat ATP-sensitive inward rectifier potassium channel 14,KCNJ14-Kir2.4 ELISA Kit 96T
E1039Ra Rat ATP-sensitive inward rectifier potassium channel 12,KCNJ12-Kir2.2 ELISA Kit 48T
E1040Ra Rat ATP-sensitive inward rectifier potassium channel 12,KCNJ12 per Kir2.2 ELISA Kit 96T
E1041Ra Rat ATP-sensitive inward rectifier potassium channel 14,KCNJ14-Kir2.4 ELISA Kit 48T
E1319Mo Mouse ATP-sensitive inward rectifier potassium channel 14,KCNJ14 per Kir2.4 ELISA Kit 96T
YHB0156Mo Mouse ATP-sensitive inward rectifier potassium channel 14,KCNJ14-Kir2.4 ELISA Kit 96T
YHB0156Mo Mouse ATP-sensitive inward rectifier potassium channel 14,KCNJ14-Kir2.4 ELISA Kit 48T
E1810Hu Human ATP-sensitive inward rectifier potassium channel 14,KCNJ14 per Kir2.4 ELISA Kit 48T
E0171Bo Bovine ATP-sensitive inward rectifier potassium channel 12,KCNJ12 per Kir2.2 ELISA Kit 96T
E0170Bo Bovine ATP-sensitive inward rectifier potassium channel 12,KCNJ12-Kir2.2 ELISA Kit 48T
E0171Bo Bovine ATP-sensitive inward rectifier potassium channel 12,KCNJ12 per Kir2.2 ELISA Kit 48T
E1799Hu Human ATP-sensitive inward rectifier potassium channel 12,KCNJ12 per Kir2.2 ELISA Kit 48T


 

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 Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | 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

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | 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 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
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | 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
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

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