rabbit anti herg antibody  (Alomone Labs)


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    Alomone Labs rabbit anti herg antibody
    Rabbit Anti Herg Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti herg antibody/product/Alomone Labs
    Average 94 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    rabbit anti herg antibody - by Bioz Stars, 2022-09
    94/100 stars

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    Alomone Labs rabbit anti c terminal herg antibody
    Rescue of trafficking deficient LQT2 mutants. (A) Representative western blot analysis of cell lysate from stable HEK293 cells expressing WT and traffic deficient LQT2 mutations in the <t>HERG</t> 1a subunit grown at 37°C and 27°C. (B) Representative western blot analysis of cell lysates from stable HEK293 cells expressing WT and traffic deficient LQT2 mutations in the HERG 1a subunit grown in the presence (+) or absence (−) of 10 µM E4031 for 36 hours. Western blots were probed with <t>anti-C</t> terminal HERG antibody and were repeated twice (n = 2).
    Rabbit Anti C Terminal Herg Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti c terminal herg antibody/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti c terminal herg antibody - by Bioz Stars, 2022-09
    94/100 stars
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    Rescue of trafficking deficient LQT2 mutants. (A) Representative western blot analysis of cell lysate from stable HEK293 cells expressing WT and traffic deficient LQT2 mutations in the HERG 1a subunit grown at 37°C and 27°C. (B) Representative western blot analysis of cell lysates from stable HEK293 cells expressing WT and traffic deficient LQT2 mutations in the HERG 1a subunit grown in the presence (+) or absence (−) of 10 µM E4031 for 36 hours. Western blots were probed with anti-C terminal HERG antibody and were repeated twice (n = 2).

    Journal: PLoS ONE

    Article Title: Changes in Channel Trafficking and Protein Stability Caused by LQT2 Mutations in the PAS Domain of the HERG Channel

    doi: 10.1371/journal.pone.0032654

    Figure Lengend Snippet: Rescue of trafficking deficient LQT2 mutants. (A) Representative western blot analysis of cell lysate from stable HEK293 cells expressing WT and traffic deficient LQT2 mutations in the HERG 1a subunit grown at 37°C and 27°C. (B) Representative western blot analysis of cell lysates from stable HEK293 cells expressing WT and traffic deficient LQT2 mutations in the HERG 1a subunit grown in the presence (+) or absence (−) of 10 µM E4031 for 36 hours. Western blots were probed with anti-C terminal HERG antibody and were repeated twice (n = 2).

    Article Snippet: Proteins were transferred by semi-dry blotting to a nitrocellulose membrane and incubated overnight at 4°C with a rabbit anti-C terminal HERG antibody (Alomone Labs) and detected by ECL.

    Techniques: Western Blot, Expressing

    Trafficking effects of LQT2 mutations in hetero-tetrameric HERG channels. (A) Western blot analysis of cell lysates from transiently transfected HEK293 cells co-expressing WT HERG 1a cmyc tagged subunit alone, WT HERG 1b untagged alone, HERG 1a cmyc with HERG 1b or LQT2 mutant HERG 1a cmyc with HERG 1b. Mature forms of HERG 1a cmyc and HERG 1b are indicated by 155 kDa and 95 kDa labels, respectively. Immature forms of HERG 1a cmyc and HERG 1b are indicated by 135 kDa and 85 kDa labels, respectively. Equal amounts of cell lysate were loaded in all lanes as assessed using BCA protein assay quantification Western blots were probed with anti-C terminal HERG antibody and were repeated twice (n = 2). (B) Western blot analysis of immunoprecipitations using anti-cmyc antibody from transiently transfected HEK293 cells co-expressing WT HERG 1a cmyc tagged subunit alone, WT HERG 1b untagged alone , HERG 1a cmyc with HERG 1b or LQT2 mutant HERG 1a cmyc with HERG 1b. Western blots were probed with anti-C terminal HERG antibody and were repeated twice (n = 2).

    Journal: PLoS ONE

    Article Title: Changes in Channel Trafficking and Protein Stability Caused by LQT2 Mutations in the PAS Domain of the HERG Channel

    doi: 10.1371/journal.pone.0032654

    Figure Lengend Snippet: Trafficking effects of LQT2 mutations in hetero-tetrameric HERG channels. (A) Western blot analysis of cell lysates from transiently transfected HEK293 cells co-expressing WT HERG 1a cmyc tagged subunit alone, WT HERG 1b untagged alone, HERG 1a cmyc with HERG 1b or LQT2 mutant HERG 1a cmyc with HERG 1b. Mature forms of HERG 1a cmyc and HERG 1b are indicated by 155 kDa and 95 kDa labels, respectively. Immature forms of HERG 1a cmyc and HERG 1b are indicated by 135 kDa and 85 kDa labels, respectively. Equal amounts of cell lysate were loaded in all lanes as assessed using BCA protein assay quantification Western blots were probed with anti-C terminal HERG antibody and were repeated twice (n = 2). (B) Western blot analysis of immunoprecipitations using anti-cmyc antibody from transiently transfected HEK293 cells co-expressing WT HERG 1a cmyc tagged subunit alone, WT HERG 1b untagged alone , HERG 1a cmyc with HERG 1b or LQT2 mutant HERG 1a cmyc with HERG 1b. Western blots were probed with anti-C terminal HERG antibody and were repeated twice (n = 2).

    Article Snippet: Proteins were transferred by semi-dry blotting to a nitrocellulose membrane and incubated overnight at 4°C with a rabbit anti-C terminal HERG antibody (Alomone Labs) and detected by ECL.

    Techniques: Western Blot, Transfection, Expressing, Mutagenesis, BIA-KA

    Trafficking phenotype of LQT2 mutant in channels formed by HERG 1a subunit. (A) Western blot of membrane protein extracts from stable HEK293 cell lines expressing full-length WT or LQT2 mutant forms of HERG 1a channel subunit. Mature fully-glycosylated HERG 1a subunit (indicated by 155 kDa label) and immature HERG 1a subunit (indicated by 135 kDa label) are indicated. (B) Western blots of membrane protein extracts from stable HEK293 cell lines expressing full-length WT or LQT2 mutant forms of HERG 1a channel subunit before (−) and after treatment (+) with N-glycosidase F. Western blots were probed with anti-C terminal HERG antibody and were repeated twice (n = 2).

    Journal: PLoS ONE

    Article Title: Changes in Channel Trafficking and Protein Stability Caused by LQT2 Mutations in the PAS Domain of the HERG Channel

    doi: 10.1371/journal.pone.0032654

    Figure Lengend Snippet: Trafficking phenotype of LQT2 mutant in channels formed by HERG 1a subunit. (A) Western blot of membrane protein extracts from stable HEK293 cell lines expressing full-length WT or LQT2 mutant forms of HERG 1a channel subunit. Mature fully-glycosylated HERG 1a subunit (indicated by 155 kDa label) and immature HERG 1a subunit (indicated by 135 kDa label) are indicated. (B) Western blots of membrane protein extracts from stable HEK293 cell lines expressing full-length WT or LQT2 mutant forms of HERG 1a channel subunit before (−) and after treatment (+) with N-glycosidase F. Western blots were probed with anti-C terminal HERG antibody and were repeated twice (n = 2).

    Article Snippet: Proteins were transferred by semi-dry blotting to a nitrocellulose membrane and incubated overnight at 4°C with a rabbit anti-C terminal HERG antibody (Alomone Labs) and detected by ECL.

    Techniques: Mutagenesis, Western Blot, Expressing

    Hypoxia blocks interaction of Hsp90 but not hsp70 with the cg form of hERG which is restored in the presence of ROS inhibitors A B: HEK/hERG cells were pulse labeled with 35 S-methionine for 6 hrs under normoxia or hypoxia in absence (A) or presence of MnTMPyP (B). Cross-linked radiolabeled hERG/chaperone complexes were immunoprecipitated with anti-hERG (lane 1 2), anti-Hsp90 (lane 3 4) and anti-Hsp70 (lane 5 6) antibodies and analyzed by 6% SDS-PAGE gels. The cg form of hERG co-immunoprecipitated with Hsp90 is shown in the box. C . Analysis of hERG binding to Hsp90 in cells treated with anti-oxidant N-acetyl cysteine (NAC; 500µm) (lane 1), during hypoxia and with xanthine/xanthine oxidase X/XO (400µM/5units/ml), a superoxide generating system, with or without NAC (lanes 2 3), during normoxia.

    Journal: Biochemical and biophysical research communications

    Article Title: Hypoxia inhibits maturation and trafficking of HERG K+ channel protein: Role of Hsp90 and ROS

    doi: 10.1016/j.bbrc.2009.07.149

    Figure Lengend Snippet: Hypoxia blocks interaction of Hsp90 but not hsp70 with the cg form of hERG which is restored in the presence of ROS inhibitors A B: HEK/hERG cells were pulse labeled with 35 S-methionine for 6 hrs under normoxia or hypoxia in absence (A) or presence of MnTMPyP (B). Cross-linked radiolabeled hERG/chaperone complexes were immunoprecipitated with anti-hERG (lane 1 2), anti-Hsp90 (lane 3 4) and anti-Hsp70 (lane 5 6) antibodies and analyzed by 6% SDS-PAGE gels. The cg form of hERG co-immunoprecipitated with Hsp90 is shown in the box. C . Analysis of hERG binding to Hsp90 in cells treated with anti-oxidant N-acetyl cysteine (NAC; 500µm) (lane 1), during hypoxia and with xanthine/xanthine oxidase X/XO (400µM/5units/ml), a superoxide generating system, with or without NAC (lanes 2 3), during normoxia.

    Article Snippet: As shown in , after a 6hr pulse, hERG antibody immunoprecipitated both cg and fg forms of hERG under normoxic conditions whereas only cg form was observed during hypoxia (lane 1 vs lane2) confirming our pulse chase data that hypoxia inhibits maturation.

    Techniques: Labeling, Immunoprecipitation, SDS Page, Binding Assay

    Bag1 regulates hERG expression. A , diagram of Bag1M transfection constructs used in this study. The UBL and BAG domain boundaries are marked with residue numbers, and the position of the R237A mutation disrupting Hsp70 interaction is shown with a star. B , HeLa cells stably expressing hERG were transfected with siRNA against Bag1 (targeting all isoforms) or non-silencing control. CG and FG hERG were detected as 135- and 155-kDa bands, respectively, by immunoblot ( IB ) and quantified relative to the amount of each in control cells. Averages and standard deviations are shown to the right of data points. Knockdown of Bag1 was confirmed by immunoblot; the bands corresponding to endogenous Bag1L, Bag1M, and Bag1S are marked. C , experiment in B was performed with MG132 treatment, and hERG was quantified relative to MG132-treated non-silencing controls. D , HEK293 cells were transfected with hERG and the indicated Bag1 construct or vector control. CG and FG hERG were detected and quantified as above. Bands corresponding to Bag1M, Bag1S, and C-Bag1 are marked. Lower panel , the experiment was performed with MG132 treatment and quantitation relative to MG132 treated vector control reported below the blot. E , HEK293 cells were transfected with human transferrin receptor ( TfR ) and Bag1 or vector control. The receptor was detected by immunoblot, and total amounts were quantified. F , HEK293 cells were transfected with hERG, GFP, and either Bag1 or vector control. Separately, HEK293 cells were transfected with hERG, siGLO, and either siRNA against Bag1 or non-silencing control. Transfected cells were identified by fluorescence microscopy. Voltage response curves from patch clamp measurements are shown. Data points and lines representing the averages are shown. *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Bag1 Co-chaperone Promotes TRC8 E3 Ligase-dependent Degradation of Misfolded Human Ether a Go-Go-related Gene (hERG) Potassium Channels *

    doi: 10.1074/jbc.M116.752618

    Figure Lengend Snippet: Bag1 regulates hERG expression. A , diagram of Bag1M transfection constructs used in this study. The UBL and BAG domain boundaries are marked with residue numbers, and the position of the R237A mutation disrupting Hsp70 interaction is shown with a star. B , HeLa cells stably expressing hERG were transfected with siRNA against Bag1 (targeting all isoforms) or non-silencing control. CG and FG hERG were detected as 135- and 155-kDa bands, respectively, by immunoblot ( IB ) and quantified relative to the amount of each in control cells. Averages and standard deviations are shown to the right of data points. Knockdown of Bag1 was confirmed by immunoblot; the bands corresponding to endogenous Bag1L, Bag1M, and Bag1S are marked. C , experiment in B was performed with MG132 treatment, and hERG was quantified relative to MG132-treated non-silencing controls. D , HEK293 cells were transfected with hERG and the indicated Bag1 construct or vector control. CG and FG hERG were detected and quantified as above. Bands corresponding to Bag1M, Bag1S, and C-Bag1 are marked. Lower panel , the experiment was performed with MG132 treatment and quantitation relative to MG132 treated vector control reported below the blot. E , HEK293 cells were transfected with human transferrin receptor ( TfR ) and Bag1 or vector control. The receptor was detected by immunoblot, and total amounts were quantified. F , HEK293 cells were transfected with hERG, GFP, and either Bag1 or vector control. Separately, HEK293 cells were transfected with hERG, siGLO, and either siRNA against Bag1 or non-silencing control. Transfected cells were identified by fluorescence microscopy. Voltage response curves from patch clamp measurements are shown. Data points and lines representing the averages are shown. *, p

    Article Snippet: The following commercially available antibodies were used: Bag1 (Santa Cruz Biotechnology); CHIP (Abcam); goat anti-rabbit IgG-conjugated HRP (Jackson ImmunoResearch); goat anti-mouse IgG-conjugated HRP (Sigma); gp78 (Abcam); hemagglutinin (HA.11) (Covance); hERG (Alomone Labs); HRD1 (Abcam); Hsc70 (StressMarq); Hsp70 (StressMarq); Hsc/Hsp70 (StressGen); RMA1 (Abcam);TRC8 (Abcam); tubulin (Sigma); Ube2j1 (Abcam); Ube2g2 (Abcam); and ubiquitin (P4D1, Santa Cruz Biotechnology).

    Techniques: Expressing, Transfection, Construct, Mutagenesis, Stable Transfection, Plasmid Preparation, Quantitation Assay, Fluorescence, Microscopy, Patch Clamp