P0981
Anti-Potassium Channel TASK-1 antibody produced in rabbit
affinity isolated antibody, lyophilized powder
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0.2 ML
$976.00
About This Item
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
lyophilized powder
species reactivity
human, rat
technique(s)
western blot (chemiluminescent): 1:200
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... KCNK3(3777)
mouse ... Kcnk3(16527)
rat ... Kcnk3(29553)
Immunogen
synthetic peptide corresponding to amino acid residues 252-269 of human TASK-1 (with additional C-terminal cysteine). The epitope is highly conserved in mouse and rat TASK-1.
Physical form
Lyophilized at ~0.6 mg/ml from phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin, 5% sucrose, 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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Storage Class
11 - Combustible Solids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
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Victoria García-Morales et al.
Nature communications, 10(1), 3784-3784 (2019-08-24)
Disruption in membrane excitability contributes to malfunction and differential vulnerability of specific neuronal subpopulations in a number of neurological diseases. The adaptor protein p11, and background potassium channel TASK1, have overlapping distributions in the CNS. Here, we report that the
Alexandra Mant et al.
Channels (Austin, Tex.), 7(4), 288-302 (2013-06-29)
Acid-sensitive, two-pore domain potassium channels, K(2P)3.1 and K(2P)9.1, are implicated in cardiac and nervous tissue responses to hormones, neurotransmitters and drugs. K(2P)3.1 and K(2P)9.1 leak potassium from the cell at rest and directly impact membrane potential. Hence altering channel number
Constanze Schmidt et al.
Circulation, 132(2), 82-92 (2015-05-09)
Antiarrhythmic management of atrial fibrillation (AF) remains a major clinical challenge. Mechanism-based approaches to AF therapy are sought to increase effectiveness and to provide individualized patient care. K(2P)3.1 (TASK-1 [tandem of P domains in a weak inward-rectifying K+ channel-related acid-sensitive
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