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Potassium channel subfamily K member 4 (TWIK-related arachidonic acid-stimulated potassium channel protein) (TRAAK) (Two pore potassium channel KT4.1) (Two pore K( ) channel KT4.1)

 KCNK4_HUMAN             Reviewed;         393 AA.
Q9NYG8; B5TJL1; Q96T94;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
12-SEP-2018, entry version 155.
RecName: Full=Potassium channel subfamily K member 4;
AltName: Full=TWIK-related arachidonic acid-stimulated potassium channel protein {ECO:0000303|PubMed:23341632};
Short=TRAAK {ECO:0000303|PubMed:23341632};
AltName: Full=Two pore potassium channel KT4.1;
Short=Two pore K(+) channel KT4.1;
Name=KCNK4; Synonyms=TRAAK;
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 1).
TISSUE=Brain;
PubMed=11042359; DOI=10.1016/S0169-328X(00)00183-2;
Chapman C.G., Meadows H.J., Godden R.J., Campbell D.A., Duckworth M.,
Kelsell R.E., Murdock P.R., Randall A.D., Rennie G.I., Gloger I.S.;
"Cloning, localisation and functional expression of a novel human,
cerebellum specific, two pore domain potassium channel.";
Brain Res. Mol. Brain Res. 82:74-83(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-328.
TISSUE=Frontal cortex;
Gray A.T.;
"Assignment of KCNK4 encoding the human potassium channel TRAAK to
chromosome 11.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10767409; DOI=10.1016/S0014-5793(00)01388-0;
Lesage F., Maingret F., Lazdunski M.;
"Cloning and expression of human TRAAK, a polyunsaturated fatty acids-
activated and mechano-sensitive K(+) channel.";
FEBS Lett. 471:137-140(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=12191490; DOI=10.1016/S0169-328X(02)00157-2;
Ozaita A., Vega-Saenz de Miera E.;
"Cloning of two transcripts, HKT4.1a and HKT4.1b, from the human two-
pore K+ channel gene KCNK4. Chromosomal localization, tissue
distribution and functional expression.";
Brain Res. Mol. Brain Res. 102:18-27(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[8]
X-RAY CRYSTALLOGRAPHY (3.31 ANGSTROMS) OF 1-274, FUNCTION, ACTIVITY
REGULATION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION,
AND DISULFIDE BOND.
PubMed=22282805; DOI=10.1126/science.1213808;
Brohawn S.G., del Marmol J., MacKinnon R.;
"Crystal structure of the human K2P TRAAK, a lipid- and mechano-
sensitive K+ ion channel.";
Science 335:436-441(2012).
[9] {ECO:0000244|PDB:4I9W}
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-274, SUBCELLULAR LOCATION,
SUBUNIT, TOPOLOGY, AND DISULFIDE BOND.
PubMed=23341632; DOI=10.1073/pnas.1218950110;
Brohawn S.G., Campbell E.B., MacKinnon R.;
"Domain-swapped chain connectivity and gated membrane access in a Fab-
mediated crystal of the human TRAAK K+ channel.";
Proc. Natl. Acad. Sci. U.S.A. 110:2129-2134(2013).
[10] {ECO:0000244|PDB:4WFE}
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-264, FUNCTION, SUBCELLULAR
LOCATION, SUBUNIT, TOPOLOGY, DISULFIDE BOND, AND DOMAIN.
PubMed=25471887; DOI=10.1038/nature14013;
Brohawn S.G., Campbell E.B., MacKinnon R.;
"Physical mechanism for gating and mechanosensitivity of the human
TRAAK K+ channel.";
Nature 516:126-130(2014).
[11] {ECO:0000244|PDB:4RUE, ECO:0000244|PDB:4RUF}
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-274 OF MUTANTS ILE-98 AND
SER-236, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, SUBUNIT,
TOPOLOGY, DISULFIDE BOND, DOMAIN, AND MUTAGENESIS OF GLY-98 AND
TRP-236.
PubMed=25500157; DOI=10.1016/j.neuron.2014.11.017;
Lolicato M., Riegelhaupt P.M., Arrigoni C., Clark K.A.,
Minor D.L. Jr.;
"Transmembrane helix straightening and buckling underlies activation
of mechanosensitive and thermosensitive K(2P) channels.";
Neuron 84:1198-1212(2014).
-!- FUNCTION: Voltage-insensitive potassium channel (PubMed:22282805).
Channel opening is triggered by mechanical forces that deform the
membrane (PubMed:22282805, PubMed:25471887, PubMed:25500157).
Channel opening is triggered by raising the intracellular pH to
basic levels (By similarity). The channel is inactive at 24
degrees Celsius (in vitro); raising the temperature to 37 degrees
Celsius increases the frequency of channel opening, with a further
increase in channel activity when the temperature is raised to 42
degrees Celsius (By similarity). Plays a role in the perception of
pain caused by heat (By similarity). Plays a role in the sensory
perception of pain caused by pressure (By similarity).
{ECO:0000250|UniProtKB:G3V8V5, ECO:0000250|UniProtKB:O88454,
ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
-!- ACTIVITY REGULATION: Activated by arachidonic acid.
{ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:25500157}.
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632, ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}; Multi-pass membrane protein
{ECO:0000269|PubMed:22282805, ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=KT4.1a;
IsoId=Q9NYG8-1; Sequence=Displayed;
Name=2; Synonyms=KT4.1b;
IsoId=Q9NYG8-2; Sequence=VSP_006689;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- DOMAIN: Channel opening is brought about by a conformation change
that involves buckling of the second transmembrane helix and
affects the position and orientation of the fourth transmembrane
helix. {ECO:0000269|PubMed:25471887, ECO:0000269|PubMed:25500157}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:22282805}.
-!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
1.A.1.8) family. {ECO:0000305}.
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EMBL; AF248242; AAG31731.1; -; mRNA.
EMBL; AF247042; AAF64062.1; -; mRNA.
EMBL; AF259500; AAK49389.1; -; mRNA.
EMBL; AF259501; AAK49390.1; -; mRNA.
EMBL; EU978935; ACH86094.1; -; mRNA.
EMBL; CH471076; EAW74242.1; -; Genomic_DNA.
CCDS; CCDS8067.1; -. [Q9NYG8-1]
RefSeq; NP_001304019.1; NM_001317090.1. [Q9NYG8-1]
RefSeq; NP_201567.1; NM_033310.2. [Q9NYG8-1]
UniGene; Hs.647233; -.
PDB; 3UM7; X-ray; 3.31 A; A/B=1-274.
PDB; 4I9W; X-ray; 2.75 A; A/B=1-274.
PDB; 4RUE; X-ray; 3.30 A; A/B=1-274.
PDB; 4RUF; X-ray; 3.40 A; A/B=1-274.
PDB; 4WFE; X-ray; 2.50 A; A/B=1-264.
PDB; 4WFF; X-ray; 2.50 A; A/B=1-264.
PDB; 4WFG; X-ray; 3.00 A; A/B=1-264.
PDB; 4WFH; X-ray; 3.01 A; A/B=1-264.
PDBsum; 3UM7; -.
PDBsum; 4I9W; -.
PDBsum; 4RUE; -.
PDBsum; 4RUF; -.
PDBsum; 4WFE; -.
PDBsum; 4WFF; -.
PDBsum; 4WFG; -.
PDBsum; 4WFH; -.
ProteinModelPortal; Q9NYG8; -.
SMR; Q9NYG8; -.
BioGrid; 119122; 2.
DIP; DIP-61343N; -.
IntAct; Q9NYG8; 3.
STRING; 9606.ENSP00000378033; -.
BindingDB; Q9NYG8; -.
ChEMBL; CHEMBL3714486; -.
GuidetoPHARMACOLOGY; 516; -.
iPTMnet; Q9NYG8; -.
PhosphoSitePlus; Q9NYG8; -.
BioMuta; KCNK4; -.
DMDM; 13124080; -.
PaxDb; Q9NYG8; -.
PeptideAtlas; Q9NYG8; -.
PRIDE; Q9NYG8; -.
ProteomicsDB; 83229; -.
ProteomicsDB; 83230; -. [Q9NYG8-2]
DNASU; 50801; -.
Ensembl; ENST00000394525; ENSP00000378033; ENSG00000182450. [Q9NYG8-1]
Ensembl; ENST00000422670; ENSP00000402797; ENSG00000182450. [Q9NYG8-1]
Ensembl; ENST00000539216; ENSP00000444948; ENSG00000182450. [Q9NYG8-1]
GeneID; 50801; -.
KEGG; hsa:50801; -.
UCSC; uc001nzj.2; human. [Q9NYG8-1]
CTD; 50801; -.
EuPathDB; HostDB:ENSG00000182450.12; -.
GeneCards; KCNK4; -.
HGNC; HGNC:6279; KCNK4.
MIM; 605720; gene.
neXtProt; NX_Q9NYG8; -.
OpenTargets; ENSG00000182450; -.
PharmGKB; PA30061; -.
eggNOG; KOG1418; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118858; -.
HOGENOM; HOG000013106; -.
HOVERGEN; HBG052234; -.
InParanoid; Q9NYG8; -.
KO; K04915; -.
OMA; LDYPSEN; -.
OrthoDB; EOG091G0E3R; -.
PhylomeDB; Q9NYG8; -.
TreeFam; TF313947; -.
Reactome; R-HSA-1299503; TWIK related potassium channel (TREK).
Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
GeneWiki; KCNK4; -.
GenomeRNAi; 50801; -.
PRO; PR:Q9NYG8; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000182450; Expressed in 38 organ(s), highest expression level in amygdala.
CleanEx; HS_KCNK4; -.
ExpressionAtlas; Q9NYG8; baseline and differential.
Genevisible; Q9NYG8; HS.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0098782; F:mechanosensitived potassium channel activity; IDA:UniProtKB.
GO; GO:0005267; F:potassium channel activity; IDA:UniProtKB.
GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
GO; GO:0097604; F:temperature-gated cation channel activity; ISS:UniProtKB.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0071469; P:cellular response to alkaline pH; ISS:UniProtKB.
GO; GO:0071398; P:cellular response to fatty acid; IDA:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:UniProtKB.
GO; GO:0071502; P:cellular response to temperature stimulus; ISS:UniProtKB.
GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; ISS:UniProtKB.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
GO; GO:0050951; P:sensory perception of temperature stimulus; ISS:UniProtKB.
GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
InterPro; IPR003280; 2pore_dom_K_chnl.
InterPro; IPR008074; 2pore_dom_K_chnl_TRAAK.
InterPro; IPR013099; K_chnl_dom.
Pfam; PF07885; Ion_trans_2; 2.
PRINTS; PR01333; 2POREKCHANEL.
PRINTS; PR01691; TRAAKCHANNEL.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
Polymorphism; Potassium; Potassium channel; Potassium transport;
Reference proteome; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
CHAIN 1 393 Potassium channel subfamily K member 4.
/FTId=PRO_0000101747.
TOPO_DOM 1 3 Cytoplasmic.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
TRANSMEM 4 24 Helical. {ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
TOPO_DOM 25 87 Extracellular.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
INTRAMEM 88 102 Helical; Name=Pore helix 1.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
INTRAMEM 103 109 {ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
TOPO_DOM 110 117 Extracellular.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
TRANSMEM 118 150 Helical. {ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
TOPO_DOM 151 172 Cytoplasmic.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
TRANSMEM 173 194 Helical. {ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
TOPO_DOM 195 199 Extracellular.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
INTRAMEM 200 213 Helical; Name=Pore helix 2.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
INTRAMEM 214 219 {ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
TOPO_DOM 220 233 Extracellular.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
TRANSMEM 234 260 Helical. {ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
TOPO_DOM 261 393 Cytoplasmic.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
REGION 103 108 Selectivity filter 1.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
REGION 212 217 Selectivity filter 2.
{ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 52 52 Interchain. {ECO:0000269|PubMed:22282805,
ECO:0000269|PubMed:23341632,
ECO:0000269|PubMed:25471887,
ECO:0000269|PubMed:25500157}.
VAR_SEQ 1 1 M -> MTTAPQEPPARPLQAGSGAGPAPGRAM (in
isoform 2).
{ECO:0000303|PubMed:12191490}.
/FTId=VSP_006689.
VARIANT 328 328 P -> L (in dbSNP:rs953778).
{ECO:0000269|Ref.2}.
/FTId=VAR_020206.
MUTAGEN 98 98 G->I: Strongly increases basal level of
channel activity, decreases further
activation by pressure and abolishes
further activation by arachidonic acid.
{ECO:0000269|PubMed:25500157}.
MUTAGEN 236 236 W->S: Increases basal level of channel
activity and decreases further activation
by pressure, but has little effect on
further activation by arachidonic acid.
{ECO:0000269|PubMed:25500157}.
HELIX 3 28 {ECO:0000244|PDB:4WFE}.
HELIX 29 31 {ECO:0000244|PDB:4WFE}.
HELIX 34 49 {ECO:0000244|PDB:4WFE}.
HELIX 55 70 {ECO:0000244|PDB:4WFE}.
STRAND 87 89 {ECO:0000244|PDB:4WFE}.
HELIX 90 101 {ECO:0000244|PDB:4WFE}.
HELIX 114 159 {ECO:0000244|PDB:4WFE}.
HELIX 164 183 {ECO:0000244|PDB:4WFE}.
HELIX 185 195 {ECO:0000244|PDB:4WFE}.
HELIX 199 210 {ECO:0000244|PDB:4WFE}.
STRAND 216 218 {ECO:0000244|PDB:4WFE}.
STRAND 221 223 {ECO:0000244|PDB:4WFE}.
TURN 225 227 {ECO:0000244|PDB:4RUE}.
HELIX 231 259 {ECO:0000244|PDB:4WFE}.
SEQUENCE 393 AA; 42704 MW; 7F18E53A0A9AD57D CRC64;
MRSTTLLALL ALVLLYLVSG ALVFRALEQP HEQQAQRELG EVREKFLRAH PCVSDQELGL
LIKEVADALG GGADPETNST SNSSHSAWDL GSAFFFSGTI ITTIGYGNVA LRTDAGRLFC
IFYALVGIPL FGILLAGVGD RLGSSLRHGI GHIEAIFLKW HVPPELVRVL SAMLFLLIGC
LLFVLTPTFV FCYMEDWSKL EAIYFVIVTL TTVGFGDYVA GADPRQDSPA YQPLVWFWIL
LGLAYFASVL TTIGNWLRVV SRRTRAEMGG LTAQAASWTG TVTARVTQRA GPAAPPPEKE
QPLLPPPPCP AQPLGRPRSP SPPEKAQPPS PPTASALDYP SENLAFIDES SDTQSERGCP
LPRAPRGRRR PNPPRKPVRP RGPGRPRDKG VPV


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18-003-42664 Potassium voltage-gated channel subfamily KQT member 2 - Voltage-gated potassium channel subunit Kv7.2; Neuroblastoma-specific potassium channel subunit alpha KvLQT2; KQT-like 2 Polyclonal 0.1 mg Protein A
18-003-42670 Kv channel-interacting protein 2 - KChIP2; A-type potassium channel modulatory protein 2; Potassium channel-interacting protein 2; Cardiac voltage-gated potassium channel modulatory subunit Polyclonal 0.05 mg Aff Pur
18-003-42669 Kv channel-interacting protein 2 - KChIP2; A-type potassium channel modulatory protein 2; Potassium channel-interacting protein 2; Cardiac voltage-gated potassium channel modulatory subunit Polyclonal 0.05 mg Aff Pur
25-252 KCNK9 is one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. This open channel is highly expressed in the cerebellum. It is inhibited by extracel 0.05 mg
28-238 KCNK3 encodes one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. The gene product is an outwardly rectifying channel that is sensitive to change 0.1 mg
18-662-20074 Potassium voltage-gated channel subfamily C member 1 - Voltage-gated potassium channel subunit Kv3.1; Kv4; NGK2; RAW2 Polyclonal 0.1 ml
18-783-75527 RABBIT ANTI HUMAN KCNMB3 (C-TERMINAL) - POTASSIUM LARGE CONDUCTANCE CALCIUM-ACTIVATED CHANNEL. SUBFAMILY M BETA MEMBER 3; Calcium-activated potassium channel. subfamily M subunit beta-3; Maxi K channe 0.05 mg
18-662-20009 Potassium voltage-gated channel subfamily B member 2 - Voltage-gated potassium channel subunit Kv2.2; CDRK Polyclonal 0.1 ml
25-255 KCNK15 is one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. KCNK15 has not been shown to be a functional channel, however, it may require other 0.05 mg
18-003-42629 Potassium voltage-gated channel subfamily D member 3 - Voltage-gated potassium channel subunit Kv4.3 Polyclonal 0.1 mg Protein A
18-003-43133 Potassium voltage-gated channel subfamily G member 1 - Voltage-gated potassium channel subunit Kv6.1; kH2 Polyclonal 0.05 mg Aff Pur
18-003-42634 Kv channel-interacting protein 1 - KChIP1; A-type potassium channel modulatory protein 1; Potassium channel-interacting protein 1; Vesicle APC-binding protein Polyclonal 0.1 mg Protein A
28-293 The M channel is a slowly activating and deactivating potassium channel that plays a critical role in the regulation of neuronal excitability. The M channel is formed by the association of the protein 0.05 mg


 

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