protein

Recombinant Human ATP-sensitive inward rectifier potassium channel 10

MBS953103

0.05 mg (E-Coli)

185 USD

Recombinant Protein

Recombinant Human ATP-sensitive inward rectifier potassium channel 10

ATP-sensitive inward rectifier potassium channel 10

ATP-dependent inwardly rectifying potassium channel Kir4.1; Inward rectifier K(+) channel Kir1.2; Potassium channel, inwardly rectifying subfamily J member 10

ATP-sensitive inward rectifier potassium channel 10; ATP-sensitive inward rectifier potassium channel 10; ATP-sensitive inward rectifier potassium channel 10; potassium voltage-gated channel subfamily J member 10; ATP-dependent inwardly rectifying potassium channel Kir4.1; Inward rectifier K(+) channel Kir1.2; Potassium channel, inwardly rectifying subfamily J member 10

KCNJ10

KCNJ10; KCNJ10; KIR1.2; KIR4.1; SESAME; BIRK-10; KCNJ13-PEN

KCJ10_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

165-379

379

FLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANM
RKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDT
ASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVL
ILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSAS
GKYIADFSLFDQVVKVASPSGLRDSTVRYGDPEKLKLEE
SLREQAEKEGSALSVRISNV

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Transport

May be responsible for potassium buffering action of glial cells in the brain. 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 and cesium.

Cloning and characterization of two K+ inward rectifier (Kir) 1.1 potassium channel homologs from human kidney (Kir1.2 and Kir1.3) .Shuck M.E., Piser T.M., Bock J.H., Slightom J.L., Lee K.S., Bienkowski M.J.J. Biol. Chem. 272:586-593(1997) Co-expression of human Kir3 subunits can yield channels with different functional properties.Schoots O., Wilson J.M., Ethier N., Bigras E., Hebert T.E., Van Tol H.H.M.Cell. Signal. 11:871-883(1999) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006)

25121966

NP_002232.2

NM_002241.4

P78508

39.8kD

Activation Of G Protein Gated Potassium Channels Pathway (1268826); Activation Of GABAB Receptors Pathway (1268816); G Protein Gated Potassium Channels Pathway (1268825); GABA B Receptor Activation Pathway (1268815); GABA Receptor Activation Pathway (1268813); Gastric Acid Secretion Pathway (154409); Gastric Acid Secretion Pathway (154383); Inhibition Of Voltage Gated Ca2+ Channels Via Gbeta/gamma Subunits Pathway (1268819); Inwardly Rectifying K+ Channels Pathway (1268824); Neuronal System Pathway (1268763)

This gene encodes a member of the inward rectifier-type potassium channel family, characterized by having a greater tendency to allow potassium to flow into, rather than out of, a cell. The encoded protein may form a heterodimer with another potassium channel protein and may be responsible for the potassium buffering action of glial cells in the brain. Mutations in this gene have been associated with seizure susceptibility of common idiopathic generalized epilepsy syndromes. [provided by RefSeq, Jul 2008]

Kir4.1: May be responsible for potassium buffering action of glial cells in the brain. 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 and cesium. Defects in KCNJ10 are the cause of seizures, sensorineural deafness, ataxia, mental retardation, and electrolyte imbalance (SESAMES). A complex disorder characterized by generalized seizures with onset in infancy, delayed psychomotor development, ataxia, sensorineural hearing loss, hypokalemia, metabolic alkalosis, and hypomagnesemia. Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ10 subfamily. Protein type: Membrane protein, integral; Membrane protein, multi-pass; Channel, ligand-gated; Channel, potassium. Chromosomal Location of Human Ortholog: 1q23.2. Cellular Component: basolateral plasma membrane; integral to plasma membrane; plasma membrane. Molecular Function: ATP binding; ATP-activated inward rectifier potassium channel activity; protein binding. Biological Process: adult walking behavior; glutamate uptake during transmission of nerve impulse; myelination in the central nervous system; potassium ion homeostasis; potassium ion import; potassium ion transport; regulation of long-term neuronal synaptic plasticity; regulation of resting membrane potential; synaptic transmission; visual perception. Disease: Deafness, Autosomal Recessive 4, With Enlarged Vestibular Aqueduct; Pendred Syndrome; Seizures, Sensorineural Deafness, Ataxia, Mental Retardation, And Electrolyte Imbalance

0.05 mg (E-Coli)

185 USD

0.2 mg (E-Coli)

420

0.5 mg (E-Coli)

680

1 mg (E-Coli)

1070