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PKD2L1 encodes a member of the polycystin protein family. Zusätzlich bieten wir Ihnen PKD2L1 Antikörper (34) und viele weitere Produktgruppen zu diesem Protein an.
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In epileptic seizures mouse model, Pkdl deficiency leads to the loss of beta2AR (zeige ADRB2 Proteine) on neuronal cilia, reduction in cAMP levels in the central nervous system, and reduction in the activation of cAMP response element-binding protein.
This study demonstrated that spontaneously active unitary currents in CSF (zeige CSF2 Proteine)-cNs are due to PKD2L1 channels that are capable, with a single opening, of triggering action potentials
sour taste cells in the posterior tongue express a proton current; the current is present in PKD2L1-expressing taste cells from circumvallate, foliate, and fungiform papillae but not in a variety of other cells
findings suggest that PKD2L1 partly contributes to sour taste responses in mice and that receptors other than PKDs would be involved in sour detection
All channel-forming isoforms of TRPP channels (polycystin-2 (zeige PKD2 Proteine), polycystin-L, and polycystin-2L2 (zeige PKD2L2 Proteine)) were expressed in adult mouse lacrimal gland.
These results demonstrate that Asp (zeige C3 Proteine)(523) in PKD2L1 is a key determinant of Ca(2 (zeige CA2 Proteine)+) permeation into the PKD1L3 (zeige PKD1L3 Proteine)/PKD2L1 complex and that PKD2L1 contributes to forming the pore of the PKD1L3 (zeige PKD1L3 Proteine)/PKD2L1 channel.
the PKD2L1-PKD1L3 (zeige PKD1L3 Proteine) complex is involved in acid sensing in vivo
PKD2L1 forms functional cation channels on the plasma membrane by interacting with PKD1 (zeige PKD1 Proteine)
Pkd1l3 (zeige PKD1L3 Proteine) and Pkd2l1 are co-expressed in a select subset of taste receptor cells and therefore may, like other PKD (zeige PRKD1 Proteine) channels, function as a heteromer.
These results suggest that PKD1L3 (zeige PKD1L3 Proteine) and PKD2L1 heteromers may function as sour taste receptors.
palmitoylation at Cys (zeige DNAJC5 Proteine)-38 and phosphorylation at Thr (zeige TRH Proteine)-39 independently regulated TRPP3 channel function
our study identified C1 as the first PKD2L1 domain essential for both PKD2L1 trimerization and channel function, and suggest that PKD2L1 and PKD2L1/PKD1L3 (zeige PKD1L3 Proteine) channels share the PKD2L1 trimerization process.
Trimerization may be important for both homo- and possibly heteromeric assemblies of PKD2L1.
This study demonistrated that human PKD2L play the role of food preference behavior.
Pkd2L1 is a novel target channel whose function is regulated by the versatile scaffolding protein RACK1 (zeige GNB2L1 Proteine).
Despite the moderate sequence identity between C-terminal regulatory domains (CRDs) of PKD2 (zeige PKD2 Proteine) and PKD2L1, they both form trimers, implying that trimeric organization of CRDs may be true of all polycystin channels.
The calcium-binding EF-hand in polycystin-L is not a domain for channel activation and ensuing inactivation.
Taken together, alpha-actinin (zeige ACTN1 Proteine) not only attaches TRPP3 to the cytoskeleton but also up-regulates TRPP3 channel function.
This gene encodes a member of the polycystin protein family. The encoded protein contains multiple transmembrane domains, and cytoplasmic N- and C-termini. The protein may be an integral membrane protein involved in cell-cell/matrix interactions. This protein functions as a calcium-regulated nonselective cation channel. Two transcript variants encoding different isoforms have been found for this gene.
polycystic kidney disease 2-like 1
, polycystic kidney disease 2-like 1 protein-like
, polycystic kidney disease 2-like 1 protein
, polycystin-2 homolog
, transient receptor potential cation channel, subfamily P, member 3