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The protein encoded by CLCNKB is a member of the family of voltage-gated chloride channels. Additionally we are shipping CLCNKB Antibodies (55) and many more products for this protein.
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Loss of ClC-K2 compromises TAL (show TALDO1 Proteins) function and abolishes salt reabsorption in the distal convoluted tubule. Our data suggest that ClC-K2 is crucial for renal salt reabsorption and concentrating ability. ClC-K2-deficient mice in most aspects mimic patients with Bartter's syndrome type 3.
Through the combined effects of pHi and pHo on ClC-K2, might be a key regulator of NaCl absorption.
IGF-1 (show IGF1 Proteins), by stimulating ClC-K2 channels, promotes net Na(+) and Cl(-) reabsorption, thus reducing driving force for potassium secretion by the cortical collecting duct.
Taking advantage of the largest number of functional results of CLCNKB mutations, we reveal the functionally important domains and severe mutational spots of the hClC-Kb channel and establish the genotype-phenotype association in classic Bartter's Syndrome.
Five patients had 1 (show SLC35A2 Proteins) or more mutations in CLCNKB, of whom 3 had homozygous mutations and 2 had single heterozygous mutations and only in CLCNKB had hypocalciuria.
Single loci of tag Single Nucleotide Polymorphisms of CLCNKA_B are not enough to increase the Essential Hypertension susceptibility, the combination of CLCNKA (show CLCNKA Proteins) SNP, salt, marine products, meat, edible oil consumption is associated with elevated risk
results demonstrate that the carboxyl terminus of hClC-Kb is not part of the binding site for barttin (show BSND Proteins), but functionally modifies the interplay with barttin (show BSND Proteins).
These results demonstrate that mutations in a cluster of hydrophobic residues within transmembrane domain 1 affect barttin (show BSND Proteins)-CLC-K interaction and impair gating modification by the accessory subunit
we report here for the first time that ClC-Kb disease-causing mutations located around the selectivity filter can result in both reduced surface expression and hyperactivity in heterologous expression systems
Case Report: 2 mutations in the CLCNKB gene, leading to a molecular diagnosis of Bartter syndrome type III in case of sudden infant death.
R8W and G47R, two naturally occurring barttin (show BSND Proteins) mutations identified in patients with Bartter syndrome type IV, reduce barttin (show BSND Proteins) palmitoylation and CLC-K/barttin (show BSND Proteins) channel activity.
HEK293 cells the potentiating effect of niflumic acid (NFA) on CLC-Ka/barttin (show BSND Proteins) and CLC-Kb/barttin (show BSND Proteins) channels seems to be absent while the blocking efficacy of niflumic acid and benzofuran derivatives observed in oocytes is preserved
study investigated the functional consequences of seven mutations; four mutants carried no current whereas others displayed a 30-60 percent reduction in conductance as compared with wild-type ClC-Kb
The open probability and mean open time of ClC-2 (show CLCN2 Proteins) was voltage dependent, decreasing dramatically as the patches were depolarized. ClC-2 (show CLCN2 Proteins) is uniquely suitable to promote anion secretion with little anion reabsorption.
The protein encoded by this gene is a member of the family of voltage-gated chloride channels. Chloride channels have several functions, including the regulation of cell volume, membrane potential stabilization, signal transduction and transepithelial transport. This gene is expressed predominantly in the kidney and may be important for renal salt reabsorption. Mutations in this gene are associated with autosomal recessive Bartter syndrome type 3 (BS3). Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
chloride channel Kb
, chloride channel Ka
, chloride channel K1-like; putative basolateral cTAL chloride channel ClC-Ka
, chloride channel protein ClC-Kb
, putative basolateral mTAL chloride channel ClC-Ka
, chloride channel K2
, chloride channel, kidney, B
, chloride channel protein ClC-Kb-like
, chloride channel, voltage-sensitive Kb