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KCNK2 encodes one of the members of the two-pore-domain background potassium channel protein family. Zusätzlich bieten wir Ihnen KCNK2 Proteine (4) und viele weitere Produktgruppen zu diesem Protein an.
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Cow (Bovine) Polyclonal KCNK2 Primary Antibody für WB - ABIN188929
Zhang, Yin, Wang, Li, Wang: Over-expressed human TREK-1 inhibits CHO cell proliferation via inhibiting PKA and p38 MAPK pathways and subsequently inducing G1 arrest. in Acta pharmacologica Sinica 2016
ANG II inhibits bTREK-1 K(+) channels by a Ca(2+)-dependent mechanism that does not require the depletion of membrane-associated PIP(2).
Metabolites of cAMP stimulate TREK-1 expression in adrenal cortex cells by activation of a novel cAMP-independent mechanism.
TREK-1 channels may function as sensors that couple the metabolic state of the cell to membrane potential, perhaps through an associated ATP-binding protein
These results identify bTREK-1 K(+) channels as a pivotal control point where ANG II (zeige AGT Antikörper) receptor activation is transduced to depolarization-dependent Ca(2 (zeige CA2 Antikörper)+) entry and aldosterone secretion.
Data show that angiotensin II and paracrine factors that act through phospholipase C (zeige PLC Antikörper) inhibit bTREK-1 in adrenocortical cells through simultaneous activation of separate Ca2 (zeige CA2 Antikörper)+- and ATP hydrolysis-dependent signaling pathways.
Angiotensin II (ANGII) inhibits adrenocortical cell KCNK2 in an ATP dependent, PLC/PKC independent manner.
These findings demonstrate that, in addition to the well-described PKA-dependent TREK-1 inhibition, ACTH (zeige POMC Antikörper), NPS (zeige NPS Antikörper)-ACTH (zeige POMC Antikörper), forskolin, and 8-pCPT-2'-O-Me-cAMP also inhibit these K(+) channels by a PKA-independent signaling pathway.
data reveal a druggable K2P site that stabilizes the C-type gate 'leak mode' and provide direct evidence for K2P selectivity filter gating
decreased TREK-1 expression in the aganglionic and ganglionic bowel observed in Hirschsprung's disease may alter intestinal epithelial barrier function leading to the development of enterocolitis
Atrial TREK-1 expression was reduced in atrial fibrillation patients with concomitant severe heart failure
The authors identified a heterozygous point mutation in the selectivity filter of the stretch-activated K2P potassium channel (zeige KCNAB2 Antikörper) TREK-1 (KCNK2 or K2P2.1). This mutation introduces abnormal sodium permeability and stretch-activation hypersensitivity to TREK-1.
The M2-glycine hinge controls the macroscopic currents of TREK1 channels.
TREK-1 overexpression suppresses CHO (zeige COL11A1 Antikörper) cell proliferation by inhibiting the activity of PKA and p38/MAPK (zeige MAPK14 Antikörper) signaling pathways and subsequently inducing G1 phase cell arrest.
Trek1 expression facilitates the restoration of intestinal epithelial barrier functions in an allergic environment.
presence of TREK-1 variants correlated to reduced TREK-1 activity, suggesting a pathological role for TREK-1 variants in preterm labor
Data suggest that potassium channel protein (zeige KCNQ5 Antikörper) TREK-1 (TREK-1) might be a biomarker in castration resistance free survival (CRFS) judgment of prostate cancer (PCa (zeige FLVCR1 Antikörper)), as well as a potential therapeutic target.
During conductance simulation experiments, both TASK-3 (zeige KCNK9 Antikörper) and TREK-1 channels were able to repolarise the membrane once AP threshold was reached
Hyperoxia treatment of TREK-1/TREK-2 (zeige KCNK10 Antikörper)/TRAAK (zeige KCNK4 Antikörper)-deficient mice is associated with a reduction in surfactant proteins
TREK-1 deficiency promoted neurons and oligodendrocytes apoptosis, aggravated demyelination and retarded motor recovery following spinal cord injury.
Formation of TREK-1/TREK-2 (zeige KCNK10 Antikörper) channels was also demonstrated in native dorsal root ganglion neurons indicating that heterodimerization may provide greater diversity of leak K(+) conductances also in native tissues.
Data suggest that porosome-associated proteins SNAP25 (zeige SNAP25 Antikörper), TREK-1, syntaxin-1A (zeige STX1A Antikörper), and Gai3 exhibit stability and functionality such that isolated proteins can be reconstituted as insulin (zeige INS Antikörper)-secreting porosomes in cell membrane of live cells.
Data indicate that arginine vasopressin (AVP (zeige AVP Antikörper)) and corticotropin-releasing hormone (CRH (zeige CRH Antikörper)) show additive effects on the suppression of the potassium channel subfamily K member 2 TREK-1 current via protein kinase C (zeige PKC Antikörper).
TWIK-1 (zeige KCNK1 Antikörper)/TREK-1 heterodimers mediate astrocytic passive conductance and cannabinoid-induced glutamate (zeige GRIN1 Antikörper) release from astrocytes.
In TREK1-deficient mice, brain endothelial cells displayed an inflammatory phenotype.
provide new insight into membrane targeting of TREK-1 in the heart and establish a broader role for beta(IV)-spectrin (zeige SPTBN4 Antikörper) in organizing functional membrane domains critical for normal heart function
This gene encodes one of the members of the two-pore-domain background potassium channel protein family. This type of potassium channel is formed by two homodimers that create a channel that leaks potassium out of the cell to control resting membrane potential. The channel can be opened, however, by certain anesthetics, membrane stretching, intracellular acidosis, and heat. Three transcript variants encoding different isoforms have been found for this gene.
potassium channel subfamily K member 2
, potassium channel, subfamily K, member 2
, potassium channel subfamily K member 2-like
, K2P2.1 potassium channel
, TREK-1 K(+) channel subunit
, TWIK-related potassium channel 1
, outward rectifying potassium channel protein TREK-1
, potassium inwardly-rectifying channel, subfamily K, member 2
, tandem-pore-domain potassium channel TREK-1
, two pore domain potassium channel TREK-1
, two pore potassium channel TPKC1
, two-pore potassium channel 1
, arachidonic acid sensitive tandem pore domain potassium channel
, ion transport membrane protein