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Merck

SML3971

Sigma-Aldrich

A1899

≥97% (HPLC)

Sinónimos:

A 1899, A-1899, N-[(2,4-Difluorophenyl)methyl]-2′-[[[2-(4-methoxyphenyl)acetyl]amino]methyl][1,1′-biphenyl]-2-carboxamide, S 20951, S-20951, S20951

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About This Item

Fórmula empírica (notación de Hill):
C30H26F2N2O3
Número de CAS:
Peso molecular:
500.54
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.77

Quality Level

assay

≥97% (HPLC)

form

powder

color

white to beige

solubility

DMSO: 2 mg/mL, clear

storage temp.

-10 to -25°C

Biochem/physiol Actions

Potent and selective TASK-1 potassium channel blocker that induces lasting respiratory alkalosis and stimulates breathing in anesthetized rats.




A1899 is a highly potent and selective non-voltage-dependent two-pore domain potassium channel K 2P 3.1 blocker (TASK-1, KCNK3, IC50 = 7 nM in CHO cells) with 10-fold selectivity over TASK-3 and much reduced or little potency towards TASK-2/4 (>8 µM in Xenopus oocytes) and other potassium channels. A1899 specifically blocks TASK-1 currents by 74% in Xenopus oocytes at 100 nM via an open-channel block mechanism. A1899 induces lasting respiratory alkalosis and stimulates breathing in anesthetized rats in vivo (5-25 mg/kg, i.v.). Also mitigates the endothelin-1 induced prolonged action potential duration in cardiomyocytes (at 200 nM).

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Identification of the A293 (AVE1231) Binding Site in the Cardiac Two-Pore-Domain Potassium Channel TASK-1: a Common Low Affinity Antiarrhythmic Drug Binding Site.
Cellular Physiology and Biochemistry, 52(5), 1223-1235 (2019)
Peadar B O'Donohoe et al.
Physiological reports, 6(19), e13876-e13876 (2018-10-05)
Sensing of hypoxia and acidosis in arterial chemoreceptors is thought to be mediated through the inhibition of TASK and possibly other (e.g., BKCa ) potassium channels which leads to membrane depolarization, voltage-gated Ca-entry, and neurosecretion. Here, we investigate the effects
A specific two-pore domain potassium channel blocker defines the structure of the TASK-1 open pore.
The Journal of Biological Chemistry, 286(16), 13977-13984 (2011)

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