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structure of a bovine CLC (show CLCF1 Antibodies) channel (CLC-K (show CLCNKB Antibodies)) using cryo-electron microscopy
results demonstrate that the carboxyl terminus of hClC-Kb is not part of the binding site for barttin, but functionally modifies the interplay with barttin.
These results demonstrate that mutations in a cluster of hydrophobic residues within transmembrane domain 1 affect barttin-CLC-K (show CLCNKB Antibodies) interaction and impair gating modification by the accessory subunit
R8W and G47R, two naturally occurring barttin mutations identified in patients with Bartter syndrome type IV, reduce barttin palmitoylation and CLC-K (show CLCNKB Antibodies)/barttin channel activity.
BSND, was first modeled, and then, the identified mutation was further analyzed by using different bioinformatics tools.
Case Report: G47R mutation decreases barttin expression, resulting CIC-K (show CLCNKB Antibodies) location being changed from the basement membrane to the cytoplasm in the tubule and might have varying effects on renal function associated with factors other than this gene.
The mislocalization of CLC-K2 (show CLCNKB Antibodies) was identified as the molecular pathogenesis of Bartter syndrome by mutant barttins.
ClC-Ka (show CLCNKB Antibodies)/barttin channels are regulated by SGK1 (show SGK1 Antibodies) and SGK3 (show SGK3 Antibodies), which may thus participate in the regulation of transport in kidney and inner ear.
A missense, point mutation on gene BSND exon 1, affects the function of the CLC-K (show CLCNKB Antibodies)/barttin chloride channel (show CLCA1 Antibodies) and caused Bartter syndrome with sensorineural deafness in two families from Spain.
Barttin mutations is associated with antenatal Bartter syndrome with sensorineural deafness
Barttin modulates trafficking and function of ClC-K1 (show CLCNKA Antibodies) and ClC-Kb (show CLCNKB Antibodies) channels
induction of SGK1 (show SGK1 Antibodies), CLC-K1 (show CLCNKA Antibodies) and barttin by high osmolarity and change in intracellular volume in distal renal tubular cells in vivo and in vitro
Bsnd(-/-) mice thus demonstrate a novel function of Cl(-) channels in generating the endocochlear potential and reveal the mechanism leading to deafness in human Bartter syndrome IV.
This gene encodes an essential beta subunit for CLC chloride channels. These heteromeric channels localize to basolateral membranes of renal tubules and of potassium-secreting epithelia of the inner ear. Mutations in this gene have been associated with Bartter syndrome with sensorineural deafness.
Bartter syndrome, infantile, with sensorineural deafness (Barttin)
, deafness, autosomal recessive 73