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PKD1L3 encodes a member of the polycystin protein family. Additionally we are shipping PKD1L3 Antibodies (17) and PKD1L3 Proteins (8) and many more products for this protein.
These results demonstrate that Asp(523) in PKD2L1 is a key determinant of Ca(2+) permeation into the PKD1L3/PKD2L1 complex and that PKD2L1 contributes to forming the pore of the PKD1L3/PKD2L1 channel.
results suggest that the interaction between PKD1L3 and PKD2L1 through their transmembrane domains is essential for proper trafficking of the channels to the cell surface in taste cells of circumvallate and foliate papillae and in cultured cells
the PKD2L1-PKD1L3 complex is involved in acid sensing in vivo
genes are mapped to chromosomes and gene structures are characterized; protein structure is predicted and contains strong ion channel signature motifs that suggest their possible function as components of cation channel (show TRPV1 ELISA Kits) pores
Pkd1l3 and Pkd2l1 are co-expressed in a select subset of taste receptor cells and therefore may, like other PKD (show PRKD1 ELISA Kits) channels, function as a heteromer
These results suggest that PKD1L3 and PKD2L1 heteromers may function as sour taste receptors.
The off-response property of PKD1L3-PKD2L1 channels might explain the physiological phenomena occurring during sour taste sensation.
PKD1L3-PKD2L1 channel activation by acetic acid was pH-dependent and occurred when the ambient pH was <3.1.
our study identified C1 as the first PKD2L1 domain essential for both PKD2L1 trimerization and channel function, and suggest that PKD2L1 and PKD2L1/PKD1L3 channels share the PKD2L1 trimerization process.
functions as a channel-forming subunit in an acid-sensing heteromeric complex formed by PKD1L3 and TRPP3
Among the three gustatory regions innervated by peripheral gustatory neurons in the geniculate ganglion, transgenic Pkd1l3 is expressed in the foliate papillae, not in the fungiform papillae or palate.
This gene encodes a member of the polycystin protein family. The encoded protein contains 11 transmembrane domains, a latrophilin/CL-1-like GPCR proteolytic site (GPS) domain, and a polycystin-1, lipoxygenase, alpha-toxin (PLAT) domain. This protein may function as a component of cation channel pores.
PC1-like 3 protein
, polycystic kidney disease protein 1-like 3