P5122
Anti-Potassium Channel K2P10.1 (TREK2) antibody produced in rabbit
affinity isolated antibody, lyophilized powder
别名:
Anti-KCNK10, Anti-TWIK-Related Potassium Channel 2
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
lyophilized powder
species reactivity
human, rat
technique(s)
immunohistochemistry: suitable using rat brain sections, western blot: 1:200 using rat cerebellum lysate
UniProt accession no.
shipped in
dry ice
Gene Information
human ... KCNK10(54207)
rat ... Kcnk10(65272)
Immunogen
synthetic peptide corresponding to amino acid residues 475-494 of rat K2P10.1. This sequence has 19/20 residues identical in human.
Physical form
Lyophilized powder from phosphate buffered saline containing 1% bovine serum albumin and 0.025% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Donghee Kim
Trends in pharmacological sciences, 24(12), 648-654 (2003-12-05)
K(+) channels that are activated by free fatty acids (here called K(FA) channels) are found throughout the CNS and in some peripheral tissues. In addition to free fatty acids, membrane stretch (cell swelling), changes in intracellular pH and volatile anaesthetic
Y Kim et al.
The Journal of biological chemistry, 275(13), 9340-9347 (2000-03-29)
We have isolated from the rat cerebellum cDNA library a complementary DNA encoding a new member of the tandem pore K(+) channel family. Its amino acid sequence shares 54% identity with that of TASK-1, but less than 30% with those
F Lesage et al.
The Journal of biological chemistry, 275(37), 28398-28405 (2000-07-06)
Mechano-sensitive and fatty acid-activated K(+) belong to the structural class of K(+) channel with two pore domains. Here, we report the isolation and the characterization of a novel member of this family. This channel, called TREK2, is closely related to
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