clc 2 antibody  (Alomone Labs)


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    Structured Review

    Alomone Labs clc 2 antibody
    Inhibition of inward-rectifier Cl − currents by <t>ClC-2</t> antibody
    Clc 2 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/clc 2 antibody/product/Alomone Labs
    Average 90 stars, based on 1 article reviews
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    clc 2 antibody - by Bioz Stars, 2022-06
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    Images

    1) Product Images from "Inward-rectifier chloride currents in Reissner's membrane epithelial cells"

    Article Title: Inward-rectifier chloride currents in Reissner's membrane epithelial cells

    Journal: Biochemical and biophysical research communications

    doi: 10.1016/j.bbrc.2010.03.048

    Inhibition of inward-rectifier Cl − currents by ClC-2 antibody
    Figure Legend Snippet: Inhibition of inward-rectifier Cl − currents by ClC-2 antibody

    Techniques Used: Inhibition

    2) Product Images from "Clcn2 encodes the hyperpolarization-activated chloride channel in the ducts of mouse salivary glands"

    Article Title: Clcn2 encodes the hyperpolarization-activated chloride channel in the ducts of mouse salivary glands

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    doi: 10.1152/ajpgi.90384.2008

    Functional expression of the ClC-2 channel in submandibular granular duct cells. A : differential interference contrast images of single granular duct and acinar cells freshly isolated from male mouse submandibular glands. Scale bar = 10 μm
    Figure Legend Snippet: Functional expression of the ClC-2 channel in submandibular granular duct cells. A : differential interference contrast images of single granular duct and acinar cells freshly isolated from male mouse submandibular glands. Scale bar = 10 μm

    Techniques Used: Functional Assay, Expressing, Isolation

    ClC-2 distribution in mouse submandibular and parotid glands. A : immunoperoxidase labeling for ClC-2 in the submandibular gland of a Clcn2 +/+ male mouse. AC, acinar cells; GD, granular duct; SD, striated duct; ED, excretory duct. Inset,
    Figure Legend Snippet: ClC-2 distribution in mouse submandibular and parotid glands. A : immunoperoxidase labeling for ClC-2 in the submandibular gland of a Clcn2 +/+ male mouse. AC, acinar cells; GD, granular duct; SD, striated duct; ED, excretory duct. Inset,

    Techniques Used: Labeling

    3) Product Images from "Increase in Hypotonic Stress-Induced Endocytic Activity in Macrophages via ClC-3"

    Article Title: Increase in Hypotonic Stress-Induced Endocytic Activity in Macrophages via ClC-3

    Journal: Molecules and Cells

    doi: 10.14348/molcells.2014.0031

    Expression and localization of ClC-2 and ClC-3 in BMDMs. (A) ClC transcripts detected in BMDMs by RTPCR. Heart tissue was used as positive control. (B) ClC protein expression in BMDMs measured by Western blot. Heart tissue served as positive control. For specific controls, antibodies against ClCs were pre-incubated with corresponding peptide antigens. (C) Localization of ClC-3 in BMDMs shown by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. Nuclei (blue) and ClC-3 (Green) were counterstained with Hoechst 33342 and ClC-3 antibody, respectively. (D, E) ClC-3 expression in BMDMs after hypo-tonic exposure examined by Western blot. Photos taken from a representative experiment. The data represent mean ± SD from three independent experiments. (F) Localization of ClC-3 in BMDMs stimulated with hypotonic solution visualized by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. ClC-3 collected in clusters around the cytomembrane, shown by arrows (n = 3 for each group).
    Figure Legend Snippet: Expression and localization of ClC-2 and ClC-3 in BMDMs. (A) ClC transcripts detected in BMDMs by RTPCR. Heart tissue was used as positive control. (B) ClC protein expression in BMDMs measured by Western blot. Heart tissue served as positive control. For specific controls, antibodies against ClCs were pre-incubated with corresponding peptide antigens. (C) Localization of ClC-3 in BMDMs shown by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. Nuclei (blue) and ClC-3 (Green) were counterstained with Hoechst 33342 and ClC-3 antibody, respectively. (D, E) ClC-3 expression in BMDMs after hypo-tonic exposure examined by Western blot. Photos taken from a representative experiment. The data represent mean ± SD from three independent experiments. (F) Localization of ClC-3 in BMDMs stimulated with hypotonic solution visualized by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. ClC-3 collected in clusters around the cytomembrane, shown by arrows (n = 3 for each group).

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Positive Control, Western Blot, Incubation, Double Immunofluorescence Staining

    4) Product Images from "Increase in Hypotonic Stress-Induced Endocytic Activity in Macrophages via ClC-3"

    Article Title: Increase in Hypotonic Stress-Induced Endocytic Activity in Macrophages via ClC-3

    Journal: Molecules and Cells

    doi: 10.14348/molcells.2014.0031

    Expression and localization of ClC-2 and ClC-3 in BMDMs. (A) ClC transcripts detected in BMDMs by RTPCR. Heart tissue was used as positive control. (B) ClC protein expression in BMDMs measured by Western blot. Heart tissue served as positive control. For specific controls, antibodies against ClCs were pre-incubated with corresponding peptide antigens. (C) Localization of ClC-3 in BMDMs shown by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. Nuclei (blue) and ClC-3 (Green) were counterstained with Hoechst 33342 and ClC-3 antibody, respectively. (D, E) ClC-3 expression in BMDMs after hypo-tonic exposure examined by Western blot. Photos taken from a representative experiment. The data represent mean ± SD from three independent experiments. (F) Localization of ClC-3 in BMDMs stimulated with hypotonic solution visualized by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. ClC-3 collected in clusters around the cytomembrane, shown by arrows (n = 3 for each group).
    Figure Legend Snippet: Expression and localization of ClC-2 and ClC-3 in BMDMs. (A) ClC transcripts detected in BMDMs by RTPCR. Heart tissue was used as positive control. (B) ClC protein expression in BMDMs measured by Western blot. Heart tissue served as positive control. For specific controls, antibodies against ClCs were pre-incubated with corresponding peptide antigens. (C) Localization of ClC-3 in BMDMs shown by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. Nuclei (blue) and ClC-3 (Green) were counterstained with Hoechst 33342 and ClC-3 antibody, respectively. (D, E) ClC-3 expression in BMDMs after hypo-tonic exposure examined by Western blot. Photos taken from a representative experiment. The data represent mean ± SD from three independent experiments. (F) Localization of ClC-3 in BMDMs stimulated with hypotonic solution visualized by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. ClC-3 collected in clusters around the cytomembrane, shown by arrows (n = 3 for each group).

    Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Positive Control, Western Blot, Incubation, Double Immunofluorescence Staining

    5) Product Images from "Functional Role of CLC-2 Chloride Inward Rectifier Channels in Cardiac Sinoatrial Nodal Pacemaker Cells"

    Article Title: Functional Role of CLC-2 Chloride Inward Rectifier Channels in Cardiac Sinoatrial Nodal Pacemaker Cells

    Journal: Journal of molecular and cellular cardiology

    doi: 10.1016/j.yjmcc.2009.04.008

    Effects of Anti- ClC-2 Ab on I Cl,ir in SAN cells
    Figure Legend Snippet: Effects of Anti- ClC-2 Ab on I Cl,ir in SAN cells

    Techniques Used:

    Molecular expression of ClC-2 in SAN cells. A
    Figure Legend Snippet: Molecular expression of ClC-2 in SAN cells. A

    Techniques Used: Expressing

    Effects of Anti- ClC-2 Ab on pacemaker action potential in SAN cells
    Figure Legend Snippet: Effects of Anti- ClC-2 Ab on pacemaker action potential in SAN cells

    Techniques Used:

    Effects of anti- ClC-2 antibody on I Cl,ir and action potential in guinea-pig SAN cells
    Figure Legend Snippet: Effects of anti- ClC-2 antibody on I Cl,ir and action potential in guinea-pig SAN cells

    Techniques Used:

    6) Product Images from "Epithelial Biology and Secretion: Knockout of ClC-2 reveals critical functions of adherens junctions in colonic homeostasis and tumorigenicity"

    Article Title: Epithelial Biology and Secretion: Knockout of ClC-2 reveals critical functions of adherens junctions in colonic homeostasis and tumorigenicity

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    doi: 10.1152/ajpgi.00087.2018

    Chloride channel protein-2 (ClC-2) knockout (KO) mice have shown disrupted adherens junctions (AJs) with nuclear localization of β-catenin in colon compared with wild-type (WT) mice. Sections of colonic tissue of ClC-2 WT and KO mice were immunolabeled for E-cadherin and β-catenin (red), and the nucleus (blue). A : ClC-2 KO colonic crypts showed dramatic disruptions of E-cadherin in upper crypts and elevated cytosolic and nuclear distribution of β-catenin. B : proximity ligation assay (PLA) showing the interaction (red dots) between E-cadherin and β-catenin in ClC-2 KO mouse colonic crypts was significantly reduced compared with ClC-2 WT. C : nuclear β-catenin was measured using ImageJ and showed significant elevations in ClC-2 KO colon ( n = 6). D : mRNA from the colonic tissues of WT and KO mice were studied for expression of T cell factor-1/lymphoid-enhancing factor-1 (TCF/LEF1) target genes by real-time PCR. The TCF/LEF1 target genes ( Axin2 , Cd44 , and Clcn2 ) were significantly increased in KO colonic tissues compared with WT. Data are presented as means ± SE ( n = 5–6). * P
    Figure Legend Snippet: Chloride channel protein-2 (ClC-2) knockout (KO) mice have shown disrupted adherens junctions (AJs) with nuclear localization of β-catenin in colon compared with wild-type (WT) mice. Sections of colonic tissue of ClC-2 WT and KO mice were immunolabeled for E-cadherin and β-catenin (red), and the nucleus (blue). A : ClC-2 KO colonic crypts showed dramatic disruptions of E-cadherin in upper crypts and elevated cytosolic and nuclear distribution of β-catenin. B : proximity ligation assay (PLA) showing the interaction (red dots) between E-cadherin and β-catenin in ClC-2 KO mouse colonic crypts was significantly reduced compared with ClC-2 WT. C : nuclear β-catenin was measured using ImageJ and showed significant elevations in ClC-2 KO colon ( n = 6). D : mRNA from the colonic tissues of WT and KO mice were studied for expression of T cell factor-1/lymphoid-enhancing factor-1 (TCF/LEF1) target genes by real-time PCR. The TCF/LEF1 target genes ( Axin2 , Cd44 , and Clcn2 ) were significantly increased in KO colonic tissues compared with WT. Data are presented as means ± SE ( n = 5–6). * P

    Techniques Used: Knock-Out, Mouse Assay, Immunolabeling, Proximity Ligation Assay, Expressing, Real-time Polymerase Chain Reaction

    Chloride channel protein-2 (ClC-2) has a critical function in regulation of colonic homeostasis and tumorigenicity via regulation of the stability of adherens junctions (AJs). In normal colonic mucosa, ClC-2 is associated with stability of AJ proteins to maintain colonic homeostasis. In the absence of ClC-2, colonic epithelial cells have disrupted AJ proteins E-cadherin, with internalization of β-catenin to the cytosol and subsequently the nucleus. Increased nuclear β-catenin results in alteration of colonic homeostasis and increased tumorigenicity associated with increased transcription of T cell factor-1/lymphoid-enhancing factor-1 (TCF/LEF1) target genes.
    Figure Legend Snippet: Chloride channel protein-2 (ClC-2) has a critical function in regulation of colonic homeostasis and tumorigenicity via regulation of the stability of adherens junctions (AJs). In normal colonic mucosa, ClC-2 is associated with stability of AJ proteins to maintain colonic homeostasis. In the absence of ClC-2, colonic epithelial cells have disrupted AJ proteins E-cadherin, with internalization of β-catenin to the cytosol and subsequently the nucleus. Increased nuclear β-catenin results in alteration of colonic homeostasis and increased tumorigenicity associated with increased transcription of T cell factor-1/lymphoid-enhancing factor-1 (TCF/LEF1) target genes.

    Techniques Used:

    Tight junction (TJ) proteins did not show alterations between chloride channel protein-2 (ClC-2) wild-type (WT) and knockout (KO) colon. Sections of colonic tissue of ClC-2 WT and KO mice were immunolabeled for zonula occludens-1 (ZO-1), occludin, and claudin-1 (red), and the nucleus (blue). Images were taken with an Olympus IX83 Inverted Motorized Microscope and were analyzed with cellSens software. Total RNA was extracted from colonic tissues, and real-time PCR was performed with the QuantStudio 6 Flex Real-Time PCR System. ClC-2 KO mice did not show alteration of TJ protein distribution or expression ( n = 6).
    Figure Legend Snippet: Tight junction (TJ) proteins did not show alterations between chloride channel protein-2 (ClC-2) wild-type (WT) and knockout (KO) colon. Sections of colonic tissue of ClC-2 WT and KO mice were immunolabeled for zonula occludens-1 (ZO-1), occludin, and claudin-1 (red), and the nucleus (blue). Images were taken with an Olympus IX83 Inverted Motorized Microscope and were analyzed with cellSens software. Total RNA was extracted from colonic tissues, and real-time PCR was performed with the QuantStudio 6 Flex Real-Time PCR System. ClC-2 KO mice did not show alteration of TJ protein distribution or expression ( n = 6).

    Techniques Used: Knock-Out, Mouse Assay, Immunolabeling, Microscopy, Software, Real-time Polymerase Chain Reaction, Expressing

    Colonoids from chloride channel protein-2 (ClC-2) knockout (KO) mice had altered adherens junctions (AJ) protein distribution. Colonoids from ClC-2 wild-type (WT) and KO mice were immunolabeled for E-cadherin (red), β-catenin (green), carbonic anhydrase II (CAII, green), chromogranin A (CgA, red), Muc2 (red), and the nucleus (blue). ClC-2 KO mice had evidence of disruption of E-cadherin, elevated cytosolic and nuclear distribution of β-catenin, reduced carbonic anhydrase II (CAII), and increased Muc2.
    Figure Legend Snippet: Colonoids from chloride channel protein-2 (ClC-2) knockout (KO) mice had altered adherens junctions (AJ) protein distribution. Colonoids from ClC-2 wild-type (WT) and KO mice were immunolabeled for E-cadherin (red), β-catenin (green), carbonic anhydrase II (CAII, green), chromogranin A (CgA, red), Muc2 (red), and the nucleus (blue). ClC-2 KO mice had evidence of disruption of E-cadherin, elevated cytosolic and nuclear distribution of β-catenin, reduced carbonic anhydrase II (CAII), and increased Muc2.

    Techniques Used: Knock-Out, Mouse Assay, Immunolabeling

    Chloride channel protein-2 (ClC-2) loss in intestinal crypts altered formation of colonoids. Colonoid cultures from colonic crypts of ClC-2 wild-type (WT) and knockout (KO) mice harvested to form spheroids and colonoids ( n = 3). Representative photos were taken ( A ), and quantification of spheroids ( B ) and crypts buds ( C ) was analyzed at day 6 in culture. A and B : at day 6 postculture initiation, we observed a mixed phenotype of more spheroids from ClC-2 KO colonic crypts compared with crypt-like structures in ClC-2 WT. C : the no. of buds from ClC-2 KO colonoids was significantly reduced compared with WT colonoids. D : the efficiency of colonoids from ClC-2 KO crypts (growth percentage) was not different compared with WT. E : the surface area of the colonoids was measured and showed no significant difference between two groups. Data are presented as means ± SE ( n = 3). * P
    Figure Legend Snippet: Chloride channel protein-2 (ClC-2) loss in intestinal crypts altered formation of colonoids. Colonoid cultures from colonic crypts of ClC-2 wild-type (WT) and knockout (KO) mice harvested to form spheroids and colonoids ( n = 3). Representative photos were taken ( A ), and quantification of spheroids ( B ) and crypts buds ( C ) was analyzed at day 6 in culture. A and B : at day 6 postculture initiation, we observed a mixed phenotype of more spheroids from ClC-2 KO colonic crypts compared with crypt-like structures in ClC-2 WT. C : the no. of buds from ClC-2 KO colonoids was significantly reduced compared with WT colonoids. D : the efficiency of colonoids from ClC-2 KO crypts (growth percentage) was not different compared with WT. E : the surface area of the colonoids was measured and showed no significant difference between two groups. Data are presented as means ± SE ( n = 3). * P

    Techniques Used: Knock-Out, Mouse Assay

    Gene expression profile of chloride channel protein-2 (ClC-2, clcn2 ) in colorectal cancer. Gene expression data using microarray and RNA-Seq retrieved from the National Institutes of Health Cancer Genome Atlas (TCGA) project. The expression of ClC-2 was significantly reduced compared with normal colorectal tissues.
    Figure Legend Snippet: Gene expression profile of chloride channel protein-2 (ClC-2, clcn2 ) in colorectal cancer. Gene expression data using microarray and RNA-Seq retrieved from the National Institutes of Health Cancer Genome Atlas (TCGA) project. The expression of ClC-2 was significantly reduced compared with normal colorectal tissues.

    Techniques Used: Expressing, Microarray, RNA Sequencing Assay

    Absence of chloride channel protein-2 (ClC-2) promoted the development of colitis-associated tumors. A : protocol used for the development of colitis-associated colorectal cancer (CAC) based on the coadministration of azoxymethane (AOM, 10 mg/kg ip at day 0 ) and dextran sulfate sodium (DSS, 2% in 3 cycles of 5 days each at weeks 2 , 5 , and 8 ). B : absence of ClC-2 significantly elevated tumor growth and size ( n = 8–9 for each group). ClC-2 knockout (KO) mice showed a significant elevation in the total number and size of colon tumors compared with wild-type (WT) mice. C : tumors were analyzed for dysplasia grade [low-grade dysplasia (LGD) and high-grade dysplasia (HGD)] and quantified based on percent of tumors demonstrating each grade. ClC-2 KO mice showed significantly increased HGD compared with WT mice, using a Fisher’s exact test. D and E : the proportion of proliferating cells in nontumor and tumor regions, quantified using bromodeoxyuridine (BrdU) staining, was significantly increased in the KO CAC mice compared with WT CAC mice. Data are presented as means ± SE. * P
    Figure Legend Snippet: Absence of chloride channel protein-2 (ClC-2) promoted the development of colitis-associated tumors. A : protocol used for the development of colitis-associated colorectal cancer (CAC) based on the coadministration of azoxymethane (AOM, 10 mg/kg ip at day 0 ) and dextran sulfate sodium (DSS, 2% in 3 cycles of 5 days each at weeks 2 , 5 , and 8 ). B : absence of ClC-2 significantly elevated tumor growth and size ( n = 8–9 for each group). ClC-2 knockout (KO) mice showed a significant elevation in the total number and size of colon tumors compared with wild-type (WT) mice. C : tumors were analyzed for dysplasia grade [low-grade dysplasia (LGD) and high-grade dysplasia (HGD)] and quantified based on percent of tumors demonstrating each grade. ClC-2 KO mice showed significantly increased HGD compared with WT mice, using a Fisher’s exact test. D and E : the proportion of proliferating cells in nontumor and tumor regions, quantified using bromodeoxyuridine (BrdU) staining, was significantly increased in the KO CAC mice compared with WT CAC mice. Data are presented as means ± SE. * P

    Techniques Used: Knock-Out, Mouse Assay, BrdU Staining

    Role of chloride channel protein-2 (ClC-2) in ultrastructural morphology of intercellular junctions in colon. A : to evaluate the role of ClC-2 in ultrastructural morphology of intercellular junctions, images were taken using a JEOL JEM-1200EX transmission electron microscope (TEM) and Gatan ES1000 camera system of intestines from ClC-2 wild-type (WT) and knockout (KO) mice. In small intestine ( top ), there is no dramatic morphological change between two groups compared with colon. In WT colon, tight junctions (TJs) and adherens junctions (AJs) appeared to be more electron dense and were more closely apposed compared with ClC-2 KO colon, in which TJs and AJs were less well defined and lateral epithelial membranes were tortuously folded (black arrows) ( n = 2). B : mucosa from small intestine (SI) and colon were studied for expression of ClC-2 by Western blotting. Densitometry analysis was performed to quantify expression using β-actin as a loading control. Data are presented as means ± SE ( n = 4). ** P
    Figure Legend Snippet: Role of chloride channel protein-2 (ClC-2) in ultrastructural morphology of intercellular junctions in colon. A : to evaluate the role of ClC-2 in ultrastructural morphology of intercellular junctions, images were taken using a JEOL JEM-1200EX transmission electron microscope (TEM) and Gatan ES1000 camera system of intestines from ClC-2 wild-type (WT) and knockout (KO) mice. In small intestine ( top ), there is no dramatic morphological change between two groups compared with colon. In WT colon, tight junctions (TJs) and adherens junctions (AJs) appeared to be more electron dense and were more closely apposed compared with ClC-2 KO colon, in which TJs and AJs were less well defined and lateral epithelial membranes were tortuously folded (black arrows) ( n = 2). B : mucosa from small intestine (SI) and colon were studied for expression of ClC-2 by Western blotting. Densitometry analysis was performed to quantify expression using β-actin as a loading control. Data are presented as means ± SE ( n = 4). ** P

    Techniques Used: Transmission Assay, Microscopy, Transmission Electron Microscopy, Knock-Out, Mouse Assay, Expressing, Western Blot

    Chloride channel protein-2 (ClC-2) knockout (KO) mice have altered colonic crypt differentiation. A : ClC-2 wild-type (WT) and KO mice were given bromodeoxyuridine (BrdU, ip) 24 h before being killed and analyzed ( n = 6). The ratio of BrdU-positive cells in colonic crypts was significantly increased in ClC-2 KO mice compared with WT mice. B : immunohistochemistry (IHC) for carbonic anhydrase II (CAII) as a maker of mature colonic enterocytes. The brackets indicate the region of most highly expressed CAII in the crypts, with ClC-2 KO mice having less differentiated colonic enterocytes than WT mice. C : crypt depth in hematoxylin and eosin (H E)-stained colonic cross sections, showing no significant difference between WT and ClC-2 KO mice. D : the no. of goblet cells per crypt was quantified using Alcian blue staining and showed no significant differences between two groups. E : the ratio of enterochromaffin cells per crypt was quantified using chromogranin A (CgA) staining and showed no significant difference between two groups. Data are presented as means ± SE ( n = 6). *** P
    Figure Legend Snippet: Chloride channel protein-2 (ClC-2) knockout (KO) mice have altered colonic crypt differentiation. A : ClC-2 wild-type (WT) and KO mice were given bromodeoxyuridine (BrdU, ip) 24 h before being killed and analyzed ( n = 6). The ratio of BrdU-positive cells in colonic crypts was significantly increased in ClC-2 KO mice compared with WT mice. B : immunohistochemistry (IHC) for carbonic anhydrase II (CAII) as a maker of mature colonic enterocytes. The brackets indicate the region of most highly expressed CAII in the crypts, with ClC-2 KO mice having less differentiated colonic enterocytes than WT mice. C : crypt depth in hematoxylin and eosin (H E)-stained colonic cross sections, showing no significant difference between WT and ClC-2 KO mice. D : the no. of goblet cells per crypt was quantified using Alcian blue staining and showed no significant differences between two groups. E : the ratio of enterochromaffin cells per crypt was quantified using chromogranin A (CgA) staining and showed no significant difference between two groups. Data are presented as means ± SE ( n = 6). *** P

    Techniques Used: Knock-Out, Mouse Assay, Immunohistochemistry, Staining

    7) Product Images from "Parallel intermediate conductance K+ and Cl− channel activity mediates electroneutral K+ exit across basolateral membranes in rat distal colon"

    Article Title: Parallel intermediate conductance K+ and Cl− channel activity mediates electroneutral K+ exit across basolateral membranes in rat distal colon

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    doi: 10.1152/ajpgi.00011.2020

    Localization of CLC2- and Na + -K + -ATPase α-subunit (NaKα)-like proteins in rat distal colon. A and A’ : CLC2-like proteins (green) localized predominantly in surface cells (arrows), while minimally expressed in crypt regions (asterisks). B and B’ : NaKα-like proteins (red) localized to both surface (arrows) and crypt (asterisks) cells. C and C’ : nuclei (blue) stained with Hoechst 33342. D : composite of A , B , and C . D’ : composite of A’ , B’ , and C’ . Higher magnification of the boxed region from D and D’ presented in E and E’ , respectively. E : CLC2 and NaKα colocalized (orange) in both lateral (arrows) and basement (arrowheads) membranes of surface cells. E’ : in crypt cells, NaKα (arrow) and CLC2 (arrowhead) localized in the basolateral membranes of crypts. Identical results obtained in different specimens obtained from three different experiments with three different male and female (not shown) rat distal colons.
    Figure Legend Snippet: Localization of CLC2- and Na + -K + -ATPase α-subunit (NaKα)-like proteins in rat distal colon. A and A’ : CLC2-like proteins (green) localized predominantly in surface cells (arrows), while minimally expressed in crypt regions (asterisks). B and B’ : NaKα-like proteins (red) localized to both surface (arrows) and crypt (asterisks) cells. C and C’ : nuclei (blue) stained with Hoechst 33342. D : composite of A , B , and C . D’ : composite of A’ , B’ , and C’ . Higher magnification of the boxed region from D and D’ presented in E and E’ , respectively. E : CLC2 and NaKα colocalized (orange) in both lateral (arrows) and basement (arrowheads) membranes of surface cells. E’ : in crypt cells, NaKα (arrow) and CLC2 (arrowhead) localized in the basolateral membranes of crypts. Identical results obtained in different specimens obtained from three different experiments with three different male and female (not shown) rat distal colons.

    Techniques Used: Staining

    8) Product Images from "Genetic Ablation of the ClC-2 Cl- Channel Disrupts Mouse Gastric Parietal Cell Acid Secretion"

    Article Title: Genetic Ablation of the ClC-2 Cl- Channel Disrupts Mouse Gastric Parietal Cell Acid Secretion

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0138174

    Immunolocalization and expression of H/K ATPase-β subunit in WT and ClC-2 -/- mouse gastric mucosa. Gastric mucosal sections from WT and ClC-2 -/- mice were stained for H/K ATPase β subunit by immunohistochemistry (A) and immunofluorescence (C). H/K ATPase β subunit positive cells were orange/brown in (A) and green in (C). Bar in (A) = 25 μm; bar in (B) = 10 μm, representative figures from n = 10–20 regions examined. (B) Quantitation of H/K ATPase-containing cells/gland of WT and ClC-2 -/- gastric mucosa, n = 6. # P
    Figure Legend Snippet: Immunolocalization and expression of H/K ATPase-β subunit in WT and ClC-2 -/- mouse gastric mucosa. Gastric mucosal sections from WT and ClC-2 -/- mice were stained for H/K ATPase β subunit by immunohistochemistry (A) and immunofluorescence (C). H/K ATPase β subunit positive cells were orange/brown in (A) and green in (C). Bar in (A) = 25 μm; bar in (B) = 10 μm, representative figures from n = 10–20 regions examined. (B) Quantitation of H/K ATPase-containing cells/gland of WT and ClC-2 -/- gastric mucosa, n = 6. # P

    Techniques Used: Expressing, Mouse Assay, Staining, Immunohistochemistry, Immunofluorescence, Quantitation Assay

    Immunolocalization and expression of ClC-2 in parietal cells of WT and ClC-2 -/- mouse gastric mucosa. (A) WT gastric mucosa was stained for both H/K ATPase (green) and ClC-2 (red). Nuclei are stained blue, bar = 25 μm. Lower panels show the area delineated by the white boxes magnified 2.5X, bar = 10 μm. (B) H/K ATPase (green) and ClC-2 (red) stained ClC-2 -/- gastric mucosa. Nuclei are stained blue, bar = 25 μm. (C) Western blot of ClC-2 in WT and ClC-2 -/- mouse gastric mucosa, with β-actin as loading control. Molecular weight markers are indicated. (D) Immunogold electron microscopy of ClC-2 in WT and ClC-2 -/- mouse gastric parietal cells. Gold labelling is seen as large black dots (black arrowheads). TV, tubulovesicles, bar = 100nm. Inset shows lower magnification of the parietal cell showing M, mitochondria, TV and N, nucleus for orientation, bar = 1 μm. Representative figures of n = 10–20 regions examined.
    Figure Legend Snippet: Immunolocalization and expression of ClC-2 in parietal cells of WT and ClC-2 -/- mouse gastric mucosa. (A) WT gastric mucosa was stained for both H/K ATPase (green) and ClC-2 (red). Nuclei are stained blue, bar = 25 μm. Lower panels show the area delineated by the white boxes magnified 2.5X, bar = 10 μm. (B) H/K ATPase (green) and ClC-2 (red) stained ClC-2 -/- gastric mucosa. Nuclei are stained blue, bar = 25 μm. (C) Western blot of ClC-2 in WT and ClC-2 -/- mouse gastric mucosa, with β-actin as loading control. Molecular weight markers are indicated. (D) Immunogold electron microscopy of ClC-2 in WT and ClC-2 -/- mouse gastric parietal cells. Gold labelling is seen as large black dots (black arrowheads). TV, tubulovesicles, bar = 100nm. Inset shows lower magnification of the parietal cell showing M, mitochondria, TV and N, nucleus for orientation, bar = 1 μm. Representative figures of n = 10–20 regions examined.

    Techniques Used: Expressing, Staining, Western Blot, Molecular Weight, Electron Microscopy

    Histological characterization of the gastric mucosa of WT and ClC-2 -/- mice. A. Haematoxylin and eosin staining of the gastric mucosa of WT and ClC-2 -/- mice is shown. Flat pink cells with purple nuclei are parietal cells; dark purple cells are zymogen cells (arrowheads). Brackets indicate the gastric gland layer and * indicates places of glandular dilation. Bar = 50 μm. B. Height of the gastric gland region was measured in WT and ClC-2 -/- mice. Results are plotted as mean ± SE (n = 6). * P
    Figure Legend Snippet: Histological characterization of the gastric mucosa of WT and ClC-2 -/- mice. A. Haematoxylin and eosin staining of the gastric mucosa of WT and ClC-2 -/- mice is shown. Flat pink cells with purple nuclei are parietal cells; dark purple cells are zymogen cells (arrowheads). Brackets indicate the gastric gland layer and * indicates places of glandular dilation. Bar = 50 μm. B. Height of the gastric gland region was measured in WT and ClC-2 -/- mice. Results are plotted as mean ± SE (n = 6). * P

    Techniques Used: Mouse Assay, Staining

    (A) Effect of histamine on the pH of gastric contents and (B) (C) effect of histamine/carbachol on acid (B) and pepsinogen (C) secretion in WT and ClC-2 -/- mouse gastric mucosa. (A) The pH of gastric contents was measured in WT (white column) and ClC-2 -/- (black column) mice after 15 min of histamine stimulation. Data are plotted as mean ± SE (n = 3). * P
    Figure Legend Snippet: (A) Effect of histamine on the pH of gastric contents and (B) (C) effect of histamine/carbachol on acid (B) and pepsinogen (C) secretion in WT and ClC-2 -/- mouse gastric mucosa. (A) The pH of gastric contents was measured in WT (white column) and ClC-2 -/- (black column) mice after 15 min of histamine stimulation. Data are plotted as mean ± SE (n = 3). * P

    Techniques Used: Mouse Assay

    Ultrastructure of parietal cells in WT and ClC-2 -/- mouse gastric mucosa. Nucleus (N), mitochondria (M) and tubulovesicles (TV) are indicated. Electron dense bodies in the ClC-2 -/- panel are presumed to be fragments of mitochondria. Representation of n = 4 with at least 10 parietal cells examined from 3 different areas of each sample. Bar = 1 μm.
    Figure Legend Snippet: Ultrastructure of parietal cells in WT and ClC-2 -/- mouse gastric mucosa. Nucleus (N), mitochondria (M) and tubulovesicles (TV) are indicated. Electron dense bodies in the ClC-2 -/- panel are presumed to be fragments of mitochondria. Representation of n = 4 with at least 10 parietal cells examined from 3 different areas of each sample. Bar = 1 μm.

    Techniques Used:

    9) Product Images from "Expression of Voltage-Gated Chloride Channels in Human Glioma Cells"

    Article Title: Expression of Voltage-Gated Chloride Channels in Human Glioma Cells

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.23-13-05572.2003

    Human biopsy samples stain positive for ClC-2, ClC-3, and ClC-5. Consecutive cryostat sections of frozen patient samples of a glioblastoma tumor ( A ) and a pilocytic astrocytoma tumor ( B ) were immunohistochemically stained with antibodies to ClC-2 (a1, b1), ClC-3 (a2, b2), and ClC-5 (a3, b3) and detected with a DAB reaction (a brown reaction product). The slices were counterstained with methyl green to detect cell nuclei. The control stainings (a4, b4) were performed under identical conditions omitting only the primary antibodies.
    Figure Legend Snippet: Human biopsy samples stain positive for ClC-2, ClC-3, and ClC-5. Consecutive cryostat sections of frozen patient samples of a glioblastoma tumor ( A ) and a pilocytic astrocytoma tumor ( B ) were immunohistochemically stained with antibodies to ClC-2 (a1, b1), ClC-3 (a2, b2), and ClC-5 (a3, b3) and detected with a DAB reaction (a brown reaction product). The slices were counterstained with methyl green to detect cell nuclei. The control stainings (a4, b4) were performed under identical conditions omitting only the primary antibodies.

    Techniques Used: Staining

    ClC-3 antisense oligonucleotides inhibit whole-cell outward Cl – currents in D54 glioma cells. A , Whole-cell outward currents from a representative control (nonsense- or ClC-2 antisense-treated cell) and ClC-3 antisense-treated cell before and after Na-gluconate bath solution and the subtracted gluconate-sensitive current. Currents elicited by voltage step protocol are shown in the inset. B , Antisense treatment significantly reduced whole-cell outward Cl – currents at peak voltages: +80, 40%; +100 mV, 48%; +120 mV, 50%. Interestingly, the current that remained appeared to be the leak current that was not sensitive to gluconate ( n =number of cells examined). C , Western blot analysis demonstrates the specificity of the ClC-3 antisense oligonucleotides (lane 1, nonsense-treated cells; lane 2, ClC-2 antisense-treated cells; lane 3, ClC-3 antisense-treated cells; lane 4, ClC-3 antisense-treated cells with a threefold higher concentration of DNA). Of note, for electrophysiology experiments ClC-3 was used at a three- to fourfold higher concentration than ClC-2 (see Materials and Methods).
    Figure Legend Snippet: ClC-3 antisense oligonucleotides inhibit whole-cell outward Cl – currents in D54 glioma cells. A , Whole-cell outward currents from a representative control (nonsense- or ClC-2 antisense-treated cell) and ClC-3 antisense-treated cell before and after Na-gluconate bath solution and the subtracted gluconate-sensitive current. Currents elicited by voltage step protocol are shown in the inset. B , Antisense treatment significantly reduced whole-cell outward Cl – currents at peak voltages: +80, 40%; +100 mV, 48%; +120 mV, 50%. Interestingly, the current that remained appeared to be the leak current that was not sensitive to gluconate ( n =number of cells examined). C , Western blot analysis demonstrates the specificity of the ClC-3 antisense oligonucleotides (lane 1, nonsense-treated cells; lane 2, ClC-2 antisense-treated cells; lane 3, ClC-3 antisense-treated cells; lane 4, ClC-3 antisense-treated cells with a threefold higher concentration of DNA). Of note, for electrophysiology experiments ClC-3 was used at a three- to fourfold higher concentration than ClC-2 (see Materials and Methods).

    Techniques Used: Western Blot, Concentration Assay

    Western blot analysis demonstrating expression of ClC-2, ClC-3, and ClC-5 in the human glioma cell lines U251, D54, U138, U118, STTG1, and U87. A , Top, Alpha Diagnostics ClC-2 antibody recognizes a doublet at ∼90 kDa and several bands at a higher molecular weight, possibly multimers of ClC-2. A , Middle, Alpha Diagnostics ClC-3 antibody recognizes a prominent band at ∼85 kDa and a much lighter band ∼15 kDa higher. A , Bottom, Alpha Diagnostics ClC-5 antibody recognizes a prominent band at ∼90 kd and a lighter band at a slightly higher molecular weight. B demonstrates similar results with Alomone's ClC-2 and ClC-3 antibodies and Jentsch ClC-5 antibody. All blots either were probed with actin (Sigma) as a loading control with the designated antibody or they were stripped and reprobed.
    Figure Legend Snippet: Western blot analysis demonstrating expression of ClC-2, ClC-3, and ClC-5 in the human glioma cell lines U251, D54, U138, U118, STTG1, and U87. A , Top, Alpha Diagnostics ClC-2 antibody recognizes a doublet at ∼90 kDa and several bands at a higher molecular weight, possibly multimers of ClC-2. A , Middle, Alpha Diagnostics ClC-3 antibody recognizes a prominent band at ∼85 kDa and a much lighter band ∼15 kDa higher. A , Bottom, Alpha Diagnostics ClC-5 antibody recognizes a prominent band at ∼90 kd and a lighter band at a slightly higher molecular weight. B demonstrates similar results with Alomone's ClC-2 and ClC-3 antibodies and Jentsch ClC-5 antibody. All blots either were probed with actin (Sigma) as a loading control with the designated antibody or they were stripped and reprobed.

    Techniques Used: Western Blot, Expressing, Molecular Weight

    Immunogold EM with 6 nm gold particles localizes ClC-2, ClC-3, and ClC-5 to the plasma membrane of glioma cells. A – C show localization of a portion of ClC-2, ClC-3, and ClC-5 with the plasma membrane of human glioma cells (Alomone ClC-2 and ClC-3 and Jentsch ClC-5).
    Figure Legend Snippet: Immunogold EM with 6 nm gold particles localizes ClC-2, ClC-3, and ClC-5 to the plasma membrane of glioma cells. A – C show localization of a portion of ClC-2, ClC-3, and ClC-5 with the plasma membrane of human glioma cells (Alomone ClC-2 and ClC-3 and Jentsch ClC-5).

    Techniques Used:

    RT-PCR of ClC-1 through ClC-7 in D54 glioma cells. Lane 1 is a 100 bp marker (Invitrogen). Lanes denoted with + are RT-PCR reactions with primers for the designated ClC channel. Lanes denoted with – are identical reactions with water substituted for reverse transcriptase. Using D54-MG total RNA as a template, only the muscle-specific ClC-1 primers did not yield a product. ClC-2 through ClC-7 mRNA was present in D54-MG cells as judged by amplification of the expected size PCR products using gene-specific primers.
    Figure Legend Snippet: RT-PCR of ClC-1 through ClC-7 in D54 glioma cells. Lane 1 is a 100 bp marker (Invitrogen). Lanes denoted with + are RT-PCR reactions with primers for the designated ClC channel. Lanes denoted with – are identical reactions with water substituted for reverse transcriptase. Using D54-MG total RNA as a template, only the muscle-specific ClC-1 primers did not yield a product. ClC-2 through ClC-7 mRNA was present in D54-MG cells as judged by amplification of the expected size PCR products using gene-specific primers.

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Marker, Amplification, Polymerase Chain Reaction

    10) Product Images from "Genetic Ablation of the ClC-2 Cl- Channel Disrupts Mouse Gastric Parietal Cell Acid Secretion"

    Article Title: Genetic Ablation of the ClC-2 Cl- Channel Disrupts Mouse Gastric Parietal Cell Acid Secretion

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0138174

    Immunolocalization and expression of H/K ATPase-β subunit in WT and ClC-2 -/- mouse gastric mucosa. Gastric mucosal sections from WT and ClC-2 -/- mice were stained for H/K ATPase β subunit by immunohistochemistry (A) and immunofluorescence (C). H/K ATPase β subunit positive cells were orange/brown in (A) and green in (C). Bar in (A) = 25 μm; bar in (B) = 10 μm, representative figures from n = 10–20 regions examined. (B) Quantitation of H/K ATPase-containing cells/gland of WT and ClC-2 -/- gastric mucosa, n = 6. # P
    Figure Legend Snippet: Immunolocalization and expression of H/K ATPase-β subunit in WT and ClC-2 -/- mouse gastric mucosa. Gastric mucosal sections from WT and ClC-2 -/- mice were stained for H/K ATPase β subunit by immunohistochemistry (A) and immunofluorescence (C). H/K ATPase β subunit positive cells were orange/brown in (A) and green in (C). Bar in (A) = 25 μm; bar in (B) = 10 μm, representative figures from n = 10–20 regions examined. (B) Quantitation of H/K ATPase-containing cells/gland of WT and ClC-2 -/- gastric mucosa, n = 6. # P

    Techniques Used: Expressing, Mouse Assay, Staining, Immunohistochemistry, Immunofluorescence, Quantitation Assay

    Immunolocalization and expression of ClC-2 in parietal cells of WT and ClC-2 -/- mouse gastric mucosa. (A) WT gastric mucosa was stained for both H/K ATPase (green) and ClC-2 (red). Nuclei are stained blue, bar = 25 μm. Lower panels show the area delineated by the white boxes magnified 2.5X, bar = 10 μm. (B) H/K ATPase (green) and ClC-2 (red) stained ClC-2 -/- gastric mucosa. Nuclei are stained blue, bar = 25 μm. (C) Western blot of ClC-2 in WT and ClC-2 -/- mouse gastric mucosa, with β-actin as loading control. Molecular weight markers are indicated. (D) Immunogold electron microscopy of ClC-2 in WT and ClC-2 -/- mouse gastric parietal cells. Gold labelling is seen as large black dots (black arrowheads). TV, tubulovesicles, bar = 100nm. Inset shows lower magnification of the parietal cell showing M, mitochondria, TV and N, nucleus for orientation, bar = 1 μm. Representative figures of n = 10–20 regions examined.
    Figure Legend Snippet: Immunolocalization and expression of ClC-2 in parietal cells of WT and ClC-2 -/- mouse gastric mucosa. (A) WT gastric mucosa was stained for both H/K ATPase (green) and ClC-2 (red). Nuclei are stained blue, bar = 25 μm. Lower panels show the area delineated by the white boxes magnified 2.5X, bar = 10 μm. (B) H/K ATPase (green) and ClC-2 (red) stained ClC-2 -/- gastric mucosa. Nuclei are stained blue, bar = 25 μm. (C) Western blot of ClC-2 in WT and ClC-2 -/- mouse gastric mucosa, with β-actin as loading control. Molecular weight markers are indicated. (D) Immunogold electron microscopy of ClC-2 in WT and ClC-2 -/- mouse gastric parietal cells. Gold labelling is seen as large black dots (black arrowheads). TV, tubulovesicles, bar = 100nm. Inset shows lower magnification of the parietal cell showing M, mitochondria, TV and N, nucleus for orientation, bar = 1 μm. Representative figures of n = 10–20 regions examined.

    Techniques Used: Expressing, Staining, Western Blot, Molecular Weight, Electron Microscopy

    Histological characterization of the gastric mucosa of WT and ClC-2 -/- mice. A. Haematoxylin and eosin staining of the gastric mucosa of WT and ClC-2 -/- mice is shown. Flat pink cells with purple nuclei are parietal cells; dark purple cells are zymogen cells (arrowheads). Brackets indicate the gastric gland layer and * indicates places of glandular dilation. Bar = 50 μm. B. Height of the gastric gland region was measured in WT and ClC-2 -/- mice. Results are plotted as mean ± SE (n = 6). * P
    Figure Legend Snippet: Histological characterization of the gastric mucosa of WT and ClC-2 -/- mice. A. Haematoxylin and eosin staining of the gastric mucosa of WT and ClC-2 -/- mice is shown. Flat pink cells with purple nuclei are parietal cells; dark purple cells are zymogen cells (arrowheads). Brackets indicate the gastric gland layer and * indicates places of glandular dilation. Bar = 50 μm. B. Height of the gastric gland region was measured in WT and ClC-2 -/- mice. Results are plotted as mean ± SE (n = 6). * P

    Techniques Used: Mouse Assay, Staining

    (A) Effect of histamine on the pH of gastric contents and (B) (C) effect of histamine/carbachol on acid (B) and pepsinogen (C) secretion in WT and ClC-2 -/- mouse gastric mucosa. (A) The pH of gastric contents was measured in WT (white column) and ClC-2 -/- (black column) mice after 15 min of histamine stimulation. Data are plotted as mean ± SE (n = 3). * P
    Figure Legend Snippet: (A) Effect of histamine on the pH of gastric contents and (B) (C) effect of histamine/carbachol on acid (B) and pepsinogen (C) secretion in WT and ClC-2 -/- mouse gastric mucosa. (A) The pH of gastric contents was measured in WT (white column) and ClC-2 -/- (black column) mice after 15 min of histamine stimulation. Data are plotted as mean ± SE (n = 3). * P

    Techniques Used: Mouse Assay

    Ultrastructure of parietal cells in WT and ClC-2 -/- mouse gastric mucosa. Nucleus (N), mitochondria (M) and tubulovesicles (TV) are indicated. Electron dense bodies in the ClC-2 -/- panel are presumed to be fragments of mitochondria. Representation of n = 4 with at least 10 parietal cells examined from 3 different areas of each sample. Bar = 1 μm.
    Figure Legend Snippet: Ultrastructure of parietal cells in WT and ClC-2 -/- mouse gastric mucosa. Nucleus (N), mitochondria (M) and tubulovesicles (TV) are indicated. Electron dense bodies in the ClC-2 -/- panel are presumed to be fragments of mitochondria. Representation of n = 4 with at least 10 parietal cells examined from 3 different areas of each sample. Bar = 1 μm.

    Techniques Used:

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    Alomone Labs clc 2 antibody
    Inhibition of inward-rectifier Cl − currents by <t>ClC-2</t> antibody
    Clc 2 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Inhibition of inward-rectifier Cl − currents by ClC-2 antibody

    Journal: Biochemical and biophysical research communications

    Article Title: Inward-rectifier chloride currents in Reissner's membrane epithelial cells

    doi: 10.1016/j.bbrc.2010.03.048

    Figure Lengend Snippet: Inhibition of inward-rectifier Cl − currents by ClC-2 antibody

    Article Snippet: ClC-2 antibody against an intracellular domain was obtained from Alomone Labs.

    Techniques: Inhibition

    Functional expression of the ClC-2 channel in submandibular granular duct cells. A : differential interference contrast images of single granular duct and acinar cells freshly isolated from male mouse submandibular glands. Scale bar = 10 μm

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Clcn2 encodes the hyperpolarization-activated chloride channel in the ducts of mouse salivary glands

    doi: 10.1152/ajpgi.90384.2008

    Figure Lengend Snippet: Functional expression of the ClC-2 channel in submandibular granular duct cells. A : differential interference contrast images of single granular duct and acinar cells freshly isolated from male mouse submandibular glands. Scale bar = 10 μm

    Article Snippet: This antibody recognizes the COOH-terminus epitope RSRHGLPREGTPSDSDDKC of rat ClC-2 that is identical to mouse ClC-2 (ACL-002, Alomone Labs, Jerusalem, Israel).

    Techniques: Functional Assay, Expressing, Isolation

    ClC-2 distribution in mouse submandibular and parotid glands. A : immunoperoxidase labeling for ClC-2 in the submandibular gland of a Clcn2 +/+ male mouse. AC, acinar cells; GD, granular duct; SD, striated duct; ED, excretory duct. Inset,

    Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

    Article Title: Clcn2 encodes the hyperpolarization-activated chloride channel in the ducts of mouse salivary glands

    doi: 10.1152/ajpgi.90384.2008

    Figure Lengend Snippet: ClC-2 distribution in mouse submandibular and parotid glands. A : immunoperoxidase labeling for ClC-2 in the submandibular gland of a Clcn2 +/+ male mouse. AC, acinar cells; GD, granular duct; SD, striated duct; ED, excretory duct. Inset,

    Article Snippet: This antibody recognizes the COOH-terminus epitope RSRHGLPREGTPSDSDDKC of rat ClC-2 that is identical to mouse ClC-2 (ACL-002, Alomone Labs, Jerusalem, Israel).

    Techniques: Labeling

    Expression and localization of ClC-2 and ClC-3 in BMDMs. (A) ClC transcripts detected in BMDMs by RTPCR. Heart tissue was used as positive control. (B) ClC protein expression in BMDMs measured by Western blot. Heart tissue served as positive control. For specific controls, antibodies against ClCs were pre-incubated with corresponding peptide antigens. (C) Localization of ClC-3 in BMDMs shown by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. Nuclei (blue) and ClC-3 (Green) were counterstained with Hoechst 33342 and ClC-3 antibody, respectively. (D, E) ClC-3 expression in BMDMs after hypo-tonic exposure examined by Western blot. Photos taken from a representative experiment. The data represent mean ± SD from three independent experiments. (F) Localization of ClC-3 in BMDMs stimulated with hypotonic solution visualized by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. ClC-3 collected in clusters around the cytomembrane, shown by arrows (n = 3 for each group).

    Journal: Molecules and Cells

    Article Title: Increase in Hypotonic Stress-Induced Endocytic Activity in Macrophages via ClC-3

    doi: 10.14348/molcells.2014.0031

    Figure Lengend Snippet: Expression and localization of ClC-2 and ClC-3 in BMDMs. (A) ClC transcripts detected in BMDMs by RTPCR. Heart tissue was used as positive control. (B) ClC protein expression in BMDMs measured by Western blot. Heart tissue served as positive control. For specific controls, antibodies against ClCs were pre-incubated with corresponding peptide antigens. (C) Localization of ClC-3 in BMDMs shown by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. Nuclei (blue) and ClC-3 (Green) were counterstained with Hoechst 33342 and ClC-3 antibody, respectively. (D, E) ClC-3 expression in BMDMs after hypo-tonic exposure examined by Western blot. Photos taken from a representative experiment. The data represent mean ± SD from three independent experiments. (F) Localization of ClC-3 in BMDMs stimulated with hypotonic solution visualized by double-staining immunofluorescence (original magnification × 1000). Scale bar = 20 μm. ClC-3 collected in clusters around the cytomembrane, shown by arrows (n = 3 for each group).

    Article Snippet: Rabbit anti-ClC-3 or rabbit anti-ClC-2 Abs were from Alomone Laboratories (Israel).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Positive Control, Western Blot, Incubation, Double Immunofluorescence Staining