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  • 93
    Thermo Fisher anti plb
    N -acetylglucosamine-decorated nanoparticles modulate O -linked GlcNAcylation of cardiac proteins. Rat myocytes were incubated with vehicle, empty PK, or PK-GlcNAc for 2 h and proteins were harvested and lysates immunoprecipitated with anti-SERCA2a (A) , <t>anti-RyR2</t> (C) or <t>anti-PLB</t> (E) antibodies and blotted for both O -GlcNAc (top panels) and immunoprecipitated target protein (bottom panels). Densitometry was used to quantify the western blot data and the results are shown in a summary bar graphs for n = 3 experiments for SERCA2a (B) the RyR2 (D) and PLB (F) . *p
    Anti Plb, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti plb
    Impaired diastolic function due to decreased <t>PLB</t> <t>Thr-17</t> phosphorylation: original Ca 2+ -transients at 1 Hz (A) illustrate slower diastolic Ca 2+ -elimination in KO myocytes. Mean data for Ca 2+ -decay (τ, B) and twitch relaxation (rt 50%, C) underline
    Anti Plb, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher plb
    SIN-1 increases the interaction of <t>PLB</t> with PP2a A.) Representative western blot (IB) specific for PP2a C and PLB total following co-immunoprecipitation (Co-IP) with PLB in cardiac homogenates. Co-IP control #1: crosslinked control gel + homogenate; Co-IP control #2: homogenate (no antibody-coupled <t>AminoLink</t> Plus gel). NOTE: The results from two separate Co-IP experiments from different samples are shown for each experimental condition (CONT, SIN-1, etc.). B.) Pooled densitometry data (mean±S.E.M.) for PP2a band intensity normalized to PLB total with control (normal Tyrode), SIN-1 (200 μmol/L), and SIN-1+urate (500 μmol/L). Data displayed as arbitrary units (A.U.). *p
    Plb, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 179 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher b antibodies plb mouse igg
    Alterations of sarcoplasmic reticulum Ca 2+ -ATPase (Serca) 2a and its regulator <t>phospholamban</t> <t>(PLN)</t> during AF. Total PLN ( a ) and PLN phosphorylated by CaMKII (Thr17; b ) or PKA (Ser16; c ) was downregulated in AF animals. d Phosphorylation levels relative to total PLN. e Serca2a protein analysis revealed a trend towards reduced protein expression associated with AF. Mean ± SEM optical density data normalized to GAPDH obtained from n = 5 Western blots per group are displayed. * P
    B Antibodies Plb Mouse Igg, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Cell Signaling Technology Inc phosphorylated pln p pln
    Alterations of sarcoplasmic reticulum Ca 2+ -ATPase (Serca) 2a and its regulator <t>phospholamban</t> <t>(PLN)</t> during AF. Total PLN ( a ) and PLN phosphorylated by CaMKII (Thr17; b ) or PKA (Ser16; c ) was downregulated in AF animals. d Phosphorylation levels relative to total PLN. e Serca2a protein analysis revealed a trend towards reduced protein expression associated with AF. Mean ± SEM optical density data normalized to GAPDH obtained from n = 5 Western blots per group are displayed. * P
    Phosphorylated Pln P Pln, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore pln pka
    Alterations of sarcoplasmic reticulum Ca 2+ -ATPase (Serca) 2a and its regulator <t>phospholamban</t> <t>(PLN)</t> during AF. Total PLN ( a ) and PLN phosphorylated by CaMKII (Thr17; b ) or PKA (Ser16; c ) was downregulated in AF animals. d Phosphorylation levels relative to total PLN. e Serca2a protein analysis revealed a trend towards reduced protein expression associated with AF. Mean ± SEM optical density data normalized to GAPDH obtained from n = 5 Western blots per group are displayed. * P
    Pln Pka, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pln  (Abcam)
    91
    Abcam pln
    The diastolic intracellular Ca 2+ concentration measured using Fura-2 AM fluorescence in isolated cardiomyocytes. A) An example trace of Ca 2+ transients using the Fura-2 fluorescent dye. The cell was stimulated at the frequencies indicated. B) Diastolic [Ca 2+ ] i at different frequencies in isolated cardiomyocytes. C) Diastolic [Ca 2+ ] i with the 0.2 Hz diastolic [Ca 2+ ] i subtracted. D) The relative phosphorylated phospholamban <t>(P-PLN</t> Ser16) to phospholamban (PLN) protein expression ratio. Data are presented as mean±SEM (n = 29–32 cardiomyocytes from 4 hearts (B–C) and 6 hearts (D)). Data were analyzed using two-way ANOVA with the Bonferroni post-hoc test (B–C) and Student's t-test (D). *** = P
    Pln, supplied by Abcam, used in various techniques. Bioz Stars score: 91/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Upstate Biotechnology Inc phospho pln
    The diastolic intracellular Ca 2+ concentration measured using Fura-2 AM fluorescence in isolated cardiomyocytes. A) An example trace of Ca 2+ transients using the Fura-2 fluorescent dye. The cell was stimulated at the frequencies indicated. B) Diastolic [Ca 2+ ] i at different frequencies in isolated cardiomyocytes. C) Diastolic [Ca 2+ ] i with the 0.2 Hz diastolic [Ca 2+ ] i subtracted. D) The relative phosphorylated phospholamban <t>(P-PLN</t> Ser16) to phospholamban (PLN) protein expression ratio. Data are presented as mean±SEM (n = 29–32 cardiomyocytes from 4 hearts (B–C) and 6 hearts (D)). Data were analyzed using two-way ANOVA with the Bonferroni post-hoc test (B–C) and Student's t-test (D). *** = P
    Phospho Pln, supplied by Upstate Biotechnology Inc, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Badrilla total pln
    <t>CaMKIIδ-dependent</t> (p-Thr 17 <t>-PLN)</t> and PKA-dependent phosphorylation (p-Ser 16 -PLN) of PLN in human failing hearts. (A) Expression of p-Thr 17 -PLN; (B) Expression of p-Ser 16 -PLN; (C) Expression of total PLN; (D) Ratio of p-Thr 17 -PLN to total PLN; (E)
    Total Pln, supplied by Badrilla, used in various techniques. Bioz Stars score: 92/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Cell Signaling Technology Inc phospho plb
    The expression of <t>p-PP1a,</t> <t>p-PLB</t> and SERCA2a. The effects of luteolin and SP600125 on the expression of total PP1a and phospho-PP1a (A, B), total PLB and phospho-PLB (C, D), SERCA (E, F). The results were expressed as the mean ± SEM, n = 3. * P
    Phospho Plb, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Abcam unphosphorylated plb
    The expression of <t>p-PP1a,</t> <t>p-PLB</t> and SERCA2a. The effects of luteolin and SP600125 on the expression of total PP1a and phospho-PP1a (A, B), total PLB and phospho-PLB (C, D), SERCA (E, F). The results were expressed as the mean ± SEM, n = 3. * P
    Unphosphorylated Plb, supplied by Abcam, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore plb
    The expression of <t>p-PP1a,</t> <t>p-PLB</t> and SERCA2a. The effects of luteolin and SP600125 on the expression of total PP1a and phospho-PP1a (A, B), total PLB and phospho-PLB (C, D), SERCA (E, F). The results were expressed as the mean ± SEM, n = 3. * P
    Plb, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Badrilla ps16 pln
    The expression of <t>p-PP1a,</t> <t>p-PLB</t> and SERCA2a. The effects of luteolin and SP600125 on the expression of total PP1a and phospho-PP1a (A, B), total PLB and phospho-PLB (C, D), SERCA (E, F). The results were expressed as the mean ± SEM, n = 3. * P
    Ps16 Pln, supplied by Badrilla, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Cell Signaling Technology Inc phopholamban plb
    The expression of <t>p-PP1a,</t> <t>p-PLB</t> and SERCA2a. The effects of luteolin and SP600125 on the expression of total PP1a and phospho-PP1a (A, B), total PLB and phospho-PLB (C, D), SERCA (E, F). The results were expressed as the mean ± SEM, n = 3. * P
    Phopholamban Plb, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Promega plb buffer
    The expression of <t>p-PP1a,</t> <t>p-PLB</t> and SERCA2a. The effects of luteolin and SP600125 on the expression of total PP1a and phospho-PP1a (A, B), total PLB and phospho-PLB (C, D), SERCA (E, F). The results were expressed as the mean ± SEM, n = 3. * P
    Plb Buffer, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 269 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Badrilla p plb
    KN93 administration reversed CaMKII activation and the disturbed Ca 2+ handling proteins in HFD-induced heart. A, Western blot analysis of phosphorylated CaMKII (p-CaMKII) at T287 site and the total protein CaMKII level in the heart tissue. B, Western blot analysis of phosphorylated <t>RyR2</t> (p-RyR2) at S2807 and S2814 site, and the total protein level of RyR2 in the heart tissue. C, Western blot analysis of phosphorylated phospholamban <t>(p-PLB)</t> at T17 site and the total protein level of SERCA2 and PLB in the heart tissues. n = 5. * P
    P Plb, supplied by Badrilla, used in various techniques. Bioz Stars score: 91/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Promega plb reagent
    KN93 administration reversed CaMKII activation and the disturbed Ca 2+ handling proteins in HFD-induced heart. A, Western blot analysis of phosphorylated CaMKII (p-CaMKII) at T287 site and the total protein CaMKII level in the heart tissue. B, Western blot analysis of phosphorylated <t>RyR2</t> (p-RyR2) at S2807 and S2814 site, and the total protein level of RyR2 in the heart tissue. C, Western blot analysis of phosphorylated phospholamban <t>(p-PLB)</t> at T17 site and the total protein level of SERCA2 and PLB in the heart tissues. n = 5. * P
    Plb Reagent, supplied by Promega, used in various techniques. Bioz Stars score: 85/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Badrilla phosopho plb
    KN93 administration reversed CaMKII activation and the disturbed Ca 2+ handling proteins in HFD-induced heart. A, Western blot analysis of phosphorylated CaMKII (p-CaMKII) at T287 site and the total protein CaMKII level in the heart tissue. B, Western blot analysis of phosphorylated <t>RyR2</t> (p-RyR2) at S2807 and S2814 site, and the total protein level of RyR2 in the heart tissue. C, Western blot analysis of phosphorylated phospholamban <t>(p-PLB)</t> at T17 site and the total protein level of SERCA2 and PLB in the heart tissues. n = 5. * P
    Phosopho Plb, supplied by Badrilla, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    N -acetylglucosamine-decorated nanoparticles modulate O -linked GlcNAcylation of cardiac proteins. Rat myocytes were incubated with vehicle, empty PK, or PK-GlcNAc for 2 h and proteins were harvested and lysates immunoprecipitated with anti-SERCA2a (A) , anti-RyR2 (C) or anti-PLB (E) antibodies and blotted for both O -GlcNAc (top panels) and immunoprecipitated target protein (bottom panels). Densitometry was used to quantify the western blot data and the results are shown in a summary bar graphs for n = 3 experiments for SERCA2a (B) the RyR2 (D) and PLB (F) . *p

    Journal: Nanomedicine

    Article Title: Bioactive nanoparticles improve calcium handling in failing cardiac myocytes

    doi: 10.2217/nnm.15.126

    Figure Lengend Snippet: N -acetylglucosamine-decorated nanoparticles modulate O -linked GlcNAcylation of cardiac proteins. Rat myocytes were incubated with vehicle, empty PK, or PK-GlcNAc for 2 h and proteins were harvested and lysates immunoprecipitated with anti-SERCA2a (A) , anti-RyR2 (C) or anti-PLB (E) antibodies and blotted for both O -GlcNAc (top panels) and immunoprecipitated target protein (bottom panels). Densitometry was used to quantify the western blot data and the results are shown in a summary bar graphs for n = 3 experiments for SERCA2a (B) the RyR2 (D) and PLB (F) . *p

    Article Snippet: The protein concentration of the lysate was determined with the BCA Protein Assay (Thermo Fisher Scientific, Waltham, MA, USA), 10 μg of the immunoprecipitating antibody anti-SERCA2a (Santa Cruz Biotechnology, Dallas, TX, USA), anti-RyR2 (34C, Life Technologies, Grand Island, NY, USA) or anti-PLB (Life Technologies, Grand Island, NY, USA) were added to 500 µg of cell lysate and incubated overnight at 4°C with agitation.

    Techniques: Incubation, Immunoprecipitation, Western Blot

    Impaired diastolic function due to decreased PLB Thr-17 phosphorylation: original Ca 2+ -transients at 1 Hz (A) illustrate slower diastolic Ca 2+ -elimination in KO myocytes. Mean data for Ca 2+ -decay (τ, B) and twitch relaxation (rt 50%, C) underline

    Journal: Journal of molecular and cellular cardiology

    Article Title: While systolic cardiomyocyte function is preserved, diastolic myocyte function and recovery from acidosis are impaired in CaMKII?-KO mice

    doi: 10.1016/j.yjmcc.2013.02.014

    Figure Lengend Snippet: Impaired diastolic function due to decreased PLB Thr-17 phosphorylation: original Ca 2+ -transients at 1 Hz (A) illustrate slower diastolic Ca 2+ -elimination in KO myocytes. Mean data for Ca 2+ -decay (τ, B) and twitch relaxation (rt 50%, C) underline

    Article Snippet: Denaturated tissue homogenates were subjected to Western blotting (4–15% gradient and 10% SDS-polyacrylamide gels) using anti-phopho-CaMKII (1:1,000, Thermo Fisher Scientific), anti-RyR2 (1:10000, Sigma-Aldrich), anti-phospho-RyR2-2809 (1:5,000, Badrilla), anti-phospho-RyR2-2815 (1:5,000, Badrilla), anti-SERCA2a (1:20,000, Affinity Bioreagents), anti-PLB (1:10,000, Millipore), anti-phospho-Ser-16 (1:10,000, Badrilla), anti-phospho-Thr-17 (1:10,000, Badrilla), anti-NCX (1:5000, Swant), anti-I-1 (1:2000, Novus Biologicals), anti-CSQ (1:20000, Affinity Bioreagents), and anti-GAPDH (1:20,000, Biotrend) antibodies.

    Techniques:

    SIN-1 increases the interaction of PLB with PP2a A.) Representative western blot (IB) specific for PP2a C and PLB total following co-immunoprecipitation (Co-IP) with PLB in cardiac homogenates. Co-IP control #1: crosslinked control gel + homogenate; Co-IP control #2: homogenate (no antibody-coupled AminoLink Plus gel). NOTE: The results from two separate Co-IP experiments from different samples are shown for each experimental condition (CONT, SIN-1, etc.). B.) Pooled densitometry data (mean±S.E.M.) for PP2a band intensity normalized to PLB total with control (normal Tyrode), SIN-1 (200 μmol/L), and SIN-1+urate (500 μmol/L). Data displayed as arbitrary units (A.U.). *p

    Journal: Nitric oxide : biology and chemistry / official journal of the Nitric Oxide Society

    Article Title: Peroxynitrite Increases Protein Phosphatase Activity and Promotes the Interaction of Phospholamban with Protein Phosphatase 2a in the Myocardium

    doi: 10.1016/j.niox.2009.01.003

    Figure Lengend Snippet: SIN-1 increases the interaction of PLB with PP2a A.) Representative western blot (IB) specific for PP2a C and PLB total following co-immunoprecipitation (Co-IP) with PLB in cardiac homogenates. Co-IP control #1: crosslinked control gel + homogenate; Co-IP control #2: homogenate (no antibody-coupled AminoLink Plus gel). NOTE: The results from two separate Co-IP experiments from different samples are shown for each experimental condition (CONT, SIN-1, etc.). B.) Pooled densitometry data (mean±S.E.M.) for PP2a band intensity normalized to PLB total with control (normal Tyrode), SIN-1 (200 μmol/L), and SIN-1+urate (500 μmol/L). Data displayed as arbitrary units (A.U.). *p

    Article Snippet: The provided AminoLink Plus gel was coupled to a custom antibody to PLB (Zymed, San Francisco, CA) for 4 hours at 22°C.

    Techniques: Western Blot, Immunoprecipitation, Co-Immunoprecipitation Assay

    Two-color flow cytometric analyses of expression of L11 antigen by LN T cells (Thy 1 + ) and weak expression by Thy 1 − cells (predominantly B cells). MLN and PLN lymphocytes were immunostained with isotype-matched control mAb ( A ) or L11 ( B ), PE-mouse anti–rat IgG and finally FITC-conjugated anti–Thy-1. Cells were analyzed using a FACScan ® and CellQuest \xa9 software; x- and y-axis are log 10 fluorescence.

    Journal: The Journal of Experimental Medicine

    Article Title: Anti-CD43 Inhibition of T Cell Homing

    doi:

    Figure Lengend Snippet: Two-color flow cytometric analyses of expression of L11 antigen by LN T cells (Thy 1 + ) and weak expression by Thy 1 − cells (predominantly B cells). MLN and PLN lymphocytes were immunostained with isotype-matched control mAb ( A ) or L11 ( B ), PE-mouse anti–rat IgG and finally FITC-conjugated anti–Thy-1. Cells were analyzed using a FACScan ® and CellQuest \xa9 software; x- and y-axis are log 10 fluorescence.

    Article Snippet: Lymphocytes from BALB/c MLN, PLN, and spleens were labeled with 10 mM Cell-Tracker Orange (Molecular Probes Inc., Eugene, OR) according to the manufacturer's instructions or with TRITC, washed, and treated with L11 or isotype-matched negative control mAb (1 μg/106 cells) for 20 min.

    Techniques: Flow Cytometry, Expressing, Software, Fluorescence

    mAb L11 inhibits T cell binding to HEV in vivo. ( A ) L11 pretreatment inhibits T ( closed bars ) but not B ( open bars ) cell localization to PLN, MLN, PP, and spleen 1 h after intravenous injection. TRITClabeled lymphocytes were treated with L11 or isotype-matched negative control mAb for 20 min, washed, and 5 × 10 7 cells injected via the tail vein. After 1 h, peripheral blood was collected by heart puncture and lymphocyte suspensions prepared from lymphoid organs were stained with FITC-conjugated anti–Thy-1, spiked with internal standard fluorescent beads for enumeration, and analyzed by two-color flow cytometry. ( B ) Homing of L11-pretreated T cells returns to that of control cells over 48 h. Redistribution studies were performed as described for A using cells labeled with 10 mM Cell-Tracker Orange.

    Journal: The Journal of Experimental Medicine

    Article Title: Anti-CD43 Inhibition of T Cell Homing

    doi:

    Figure Lengend Snippet: mAb L11 inhibits T cell binding to HEV in vivo. ( A ) L11 pretreatment inhibits T ( closed bars ) but not B ( open bars ) cell localization to PLN, MLN, PP, and spleen 1 h after intravenous injection. TRITClabeled lymphocytes were treated with L11 or isotype-matched negative control mAb for 20 min, washed, and 5 × 10 7 cells injected via the tail vein. After 1 h, peripheral blood was collected by heart puncture and lymphocyte suspensions prepared from lymphoid organs were stained with FITC-conjugated anti–Thy-1, spiked with internal standard fluorescent beads for enumeration, and analyzed by two-color flow cytometry. ( B ) Homing of L11-pretreated T cells returns to that of control cells over 48 h. Redistribution studies were performed as described for A using cells labeled with 10 mM Cell-Tracker Orange.

    Article Snippet: Lymphocytes from BALB/c MLN, PLN, and spleens were labeled with 10 mM Cell-Tracker Orange (Molecular Probes Inc., Eugene, OR) according to the manufacturer's instructions or with TRITC, washed, and treated with L11 or isotype-matched negative control mAb (1 μg/106 cells) for 20 min.

    Techniques: Binding Assay, In Vivo, Injection, Negative Control, Staining, Flow Cytometry, Cytometry, Labeling

    mAb L11 inhibits T cell binding to HEV in vitro. ( A ) L11 blocks binding of total LN lymphocytes to PLN HEV in modified Stamper-Woodruff frozen section assays performed using isolated BALB/c PLN and MLN lymphocytes mixed 1:1 with TRITC-labeled rat MLN cells (internal standard cells not recognized by L11). Cells were preincubated with isotype-matched control mAb or with L11, added to freshly cut PLN frozen sections, and incubated for 30 min with constant rotation (76 rpm) at 4°C. The number of mouse and rat lymphocytes bound to > 30 HEV on each of quadruplicate sections was determined by fluorescence microscopy. The ratio of the number of L11-treated cells bound/rat internal standard to the number of control antibody treated cells bound/rat internal standard was calculated and sample cell binding expressed as percent of control cell binding. ( B ) Blocking of T versus B cells was assessed as described for total lymphocytes using T cells isolated by negative selection ( > 97% Thy 1 + ). B cells were identified in mixed populations by prestaining cell suspensions with FITC-conjugated antiB220.

    Journal: The Journal of Experimental Medicine

    Article Title: Anti-CD43 Inhibition of T Cell Homing

    doi:

    Figure Lengend Snippet: mAb L11 inhibits T cell binding to HEV in vitro. ( A ) L11 blocks binding of total LN lymphocytes to PLN HEV in modified Stamper-Woodruff frozen section assays performed using isolated BALB/c PLN and MLN lymphocytes mixed 1:1 with TRITC-labeled rat MLN cells (internal standard cells not recognized by L11). Cells were preincubated with isotype-matched control mAb or with L11, added to freshly cut PLN frozen sections, and incubated for 30 min with constant rotation (76 rpm) at 4°C. The number of mouse and rat lymphocytes bound to > 30 HEV on each of quadruplicate sections was determined by fluorescence microscopy. The ratio of the number of L11-treated cells bound/rat internal standard to the number of control antibody treated cells bound/rat internal standard was calculated and sample cell binding expressed as percent of control cell binding. ( B ) Blocking of T versus B cells was assessed as described for total lymphocytes using T cells isolated by negative selection ( > 97% Thy 1 + ). B cells were identified in mixed populations by prestaining cell suspensions with FITC-conjugated antiB220.

    Article Snippet: Lymphocytes from BALB/c MLN, PLN, and spleens were labeled with 10 mM Cell-Tracker Orange (Molecular Probes Inc., Eugene, OR) according to the manufacturer's instructions or with TRITC, washed, and treated with L11 or isotype-matched negative control mAb (1 μg/106 cells) for 20 min.

    Techniques: Binding Assay, In Vitro, Modification, Isolation, Labeling, Incubation, Fluorescence, Microscopy, Blocking Assay, Selection

    Alterations of sarcoplasmic reticulum Ca 2+ -ATPase (Serca) 2a and its regulator phospholamban (PLN) during AF. Total PLN ( a ) and PLN phosphorylated by CaMKII (Thr17; b ) or PKA (Ser16; c ) was downregulated in AF animals. d Phosphorylation levels relative to total PLN. e Serca2a protein analysis revealed a trend towards reduced protein expression associated with AF. Mean ± SEM optical density data normalized to GAPDH obtained from n = 5 Western blots per group are displayed. * P

    Journal: PLoS ONE

    Article Title: Atrial Fibrillation Complicated by Heart Failure Induces Distinct Remodeling of Calcium Cycling Proteins

    doi: 10.1371/journal.pone.0116395

    Figure Lengend Snippet: Alterations of sarcoplasmic reticulum Ca 2+ -ATPase (Serca) 2a and its regulator phospholamban (PLN) during AF. Total PLN ( a ) and PLN phosphorylated by CaMKII (Thr17; b ) or PKA (Ser16; c ) was downregulated in AF animals. d Phosphorylation levels relative to total PLN. e Serca2a protein analysis revealed a trend towards reduced protein expression associated with AF. Mean ± SEM optical density data normalized to GAPDH obtained from n = 5 Western blots per group are displayed. * P

    Article Snippet: Equal amounts of protein were separated on 6–20% SDS polyacrylamide gels, transferred to polyvinylidene difluoride membranes, and developed using primary antibodies directed against L-type calcium channel (LTCC) α1c subunit (sc-25686; Santa Cruz Biotechnology, Heidelberg, Germany), LTCC α2 subunit (ab62814; Abcam), Na+ -Ca2+ exchanger (NCX) 1 (ab2869; Abcam), catalytic protein kinase A (PKA) subunits Cα/β (ab26322; Abcam), phosphorylated regulatory PKA subunit RIIα (Ser99) (ab32390; Abcam), phospholamban (PLN) (MA3-922; Thermo Scientific, Dreieich, Germany), phosphorylated PLN (Ser16) (07-052; Upstate (Merck Millipore), Billerica, MA, USA), phosphorylated PLN (Thr17) (sc-17024-R; Santa Cruz Biotechnology, Heidelberg, Germany), Ca2+ -calmodulin-dependent protein kinase II (CaMKII) δ (C1035-04E; Biomol, Hamburg, Germany), autophosphorylated CaMKIIδ (Thr286) (V1111; Promega, Madison, WI, USA), ryanodine receptor type 2 (RyR2) (ab2868; Abcam), phosphorylated RyR2 (Ser2808) (A010-30; Badrilla, Leeds, UK), phosphorylated RyR2 (Ser2814) (A010-31AP; Badrilla), and sarcoplasmic reticulum Ca2+ -ATPase (Serca) 2a (sc-8095; Santa Cruz Biotechnology).

    Techniques: Expressing, Western Blot

    The diastolic intracellular Ca 2+ concentration measured using Fura-2 AM fluorescence in isolated cardiomyocytes. A) An example trace of Ca 2+ transients using the Fura-2 fluorescent dye. The cell was stimulated at the frequencies indicated. B) Diastolic [Ca 2+ ] i at different frequencies in isolated cardiomyocytes. C) Diastolic [Ca 2+ ] i with the 0.2 Hz diastolic [Ca 2+ ] i subtracted. D) The relative phosphorylated phospholamban (P-PLN Ser16) to phospholamban (PLN) protein expression ratio. Data are presented as mean±SEM (n = 29–32 cardiomyocytes from 4 hearts (B–C) and 6 hearts (D)). Data were analyzed using two-way ANOVA with the Bonferroni post-hoc test (B–C) and Student's t-test (D). *** = P

    Journal: PLoS ONE

    Article Title: Hearts from Mice Fed a Non-Obesogenic High-Fat Diet Exhibit Changes in Their Oxidative State, Calcium and Mitochondria in Parallel with Increased Susceptibility to Reperfusion Injury

    doi: 10.1371/journal.pone.0100579

    Figure Lengend Snippet: The diastolic intracellular Ca 2+ concentration measured using Fura-2 AM fluorescence in isolated cardiomyocytes. A) An example trace of Ca 2+ transients using the Fura-2 fluorescent dye. The cell was stimulated at the frequencies indicated. B) Diastolic [Ca 2+ ] i at different frequencies in isolated cardiomyocytes. C) Diastolic [Ca 2+ ] i with the 0.2 Hz diastolic [Ca 2+ ] i subtracted. D) The relative phosphorylated phospholamban (P-PLN Ser16) to phospholamban (PLN) protein expression ratio. Data are presented as mean±SEM (n = 29–32 cardiomyocytes from 4 hearts (B–C) and 6 hearts (D)). Data were analyzed using two-way ANOVA with the Bonferroni post-hoc test (B–C) and Student's t-test (D). *** = P

    Article Snippet: Primary antibodies used included phosphorylated (Ser473) Akt (1∶2000, Cell Signaling), Akt (1∶2000, Cell Signaling), cleaved caspase 3 (CC3) (1∶1000, Cell Signaling), Bcl-2-associated X protein (BAX) (1∶2000, Cell Signaling), B-cell lymphoma-2 (Bcl-2) (1∶2000, Cell Signaling), mitofusin 1 (Mfn-1) (1∶1000, Abcam), Mfn-2 (1∶1000, Abcam), optic atrophy 1 (OPA1) (1∶10,000, Abcam), dynamin related protein 1 (DRP1) (1∶1000, Cell Signaling), phosphate carrier (PiC) (1∶100,000, Sigma- Genosys), voltage-dependent anion channel (VDAC) (1∶4000, Cell Signaling), cyclophilin D (CypD) (1∶2000, Abcam), adenine nucleotide transferase (ANT) (1∶10,000, custom made (see )), hexokinase II (1∶1000, Cell Signaling), phosphorylated (Ser16) phospholamban (P-PLN) (1∶2000, Abcam), PLN (1∶5000, Abcam) and catalase (1∶2000, Abcam).

    Techniques: Concentration Assay, Fluorescence, Isolation, Expressing

    CaMKIIδ-dependent (p-Thr 17 -PLN) and PKA-dependent phosphorylation (p-Ser 16 -PLN) of PLN in human failing hearts. (A) Expression of p-Thr 17 -PLN; (B) Expression of p-Ser 16 -PLN; (C) Expression of total PLN; (D) Ratio of p-Thr 17 -PLN to total PLN; (E)

    Journal: American Journal of Translational Research

    Article Title: Posttranslational modifications of calcium/calmodulin-dependent protein kinase IIδ and its downstream signaling in human failing hearts

    doi:

    Figure Lengend Snippet: CaMKIIδ-dependent (p-Thr 17 -PLN) and PKA-dependent phosphorylation (p-Ser 16 -PLN) of PLN in human failing hearts. (A) Expression of p-Thr 17 -PLN; (B) Expression of p-Ser 16 -PLN; (C) Expression of total PLN; (D) Ratio of p-Thr 17 -PLN to total PLN; (E)

    Article Snippet: Proteins were transferred on PVDF membranes (Immobilon-P, EMD Millipore, USA) and incubated with primary antibodies against p-Thr287 -CaMKII (Cell Signaling, USA), oxMet281/282 -CaMKII (EMD Millipore, USA), total CaMKIIδ (Santa Cruz, USA), p-Thr17 -PLN (Badrilla, UK), p-Ser16 -PLN (Badrilla, UK), total PLN (Badrilla, UK), p-Ser282(284) -cMyBP-C (Enzo, USA), total cMyBP-C (Santa Cruz, USA), total SERCA2a (Badrilla, UK), PP1β (Abcam, USA) and PP2A (Sigma-Aldrich, USA).

    Techniques: Expressing

    The expression of p-PP1a, p-PLB and SERCA2a. The effects of luteolin and SP600125 on the expression of total PP1a and phospho-PP1a (A, B), total PLB and phospho-PLB (C, D), SERCA (E, F). The results were expressed as the mean ± SEM, n = 3. * P

    Journal: PLoS ONE

    Article Title: ERK/PP1a/PLB/SERCA2a and JNK Pathways Are Involved in Luteolin-Mediated Protection of Rat Hearts and Cardiomyocytes following Ischemia/Reperfusion

    doi: 10.1371/journal.pone.0082957

    Figure Lengend Snippet: The expression of p-PP1a, p-PLB and SERCA2a. The effects of luteolin and SP600125 on the expression of total PP1a and phospho-PP1a (A, B), total PLB and phospho-PLB (C, D), SERCA (E, F). The results were expressed as the mean ± SEM, n = 3. * P

    Article Snippet: After blocking with 5% non-fat dry milk in Tris-buffered saline containing 0.1% Tween 20 (TBST), membranes were immunoblotted overnight at 4°C with primary antibodies against the following: Bcl-2 and Bax (1∶500, Santa Cruz, USA); ERK1/2, phospho-ERK1/2, JNK, phospho-JNK, PP1a, phospho-PP1a, PLB, and phospho-PLB (1∶1000; Cell Signaling Technology, MA, USA); SERCA2a (1∶5000; Abcam; England); and β-actin (1∶1000; Zhongshan; Beijing, China).

    Techniques: Expressing

    The possible mechanisms of luteolin exerting its protective effects on myocardium following I/R injury. Pretreatment with luteolin and SP600125 can deregulate the expression of p-JNK, upregulate the expression of p-ERK following I/R, which can result in cells apoptosis were inhibited and contractile function of myocardium was improved. Pretreatment with luteolin can also decrease the expression of SERCA2a via ERK1/2-PP1a-PLB pathway. The effect of luteolin was almost completely abolished by pretreatment PD98059 before it.

    Journal: PLoS ONE

    Article Title: ERK/PP1a/PLB/SERCA2a and JNK Pathways Are Involved in Luteolin-Mediated Protection of Rat Hearts and Cardiomyocytes following Ischemia/Reperfusion

    doi: 10.1371/journal.pone.0082957

    Figure Lengend Snippet: The possible mechanisms of luteolin exerting its protective effects on myocardium following I/R injury. Pretreatment with luteolin and SP600125 can deregulate the expression of p-JNK, upregulate the expression of p-ERK following I/R, which can result in cells apoptosis were inhibited and contractile function of myocardium was improved. Pretreatment with luteolin can also decrease the expression of SERCA2a via ERK1/2-PP1a-PLB pathway. The effect of luteolin was almost completely abolished by pretreatment PD98059 before it.

    Article Snippet: After blocking with 5% non-fat dry milk in Tris-buffered saline containing 0.1% Tween 20 (TBST), membranes were immunoblotted overnight at 4°C with primary antibodies against the following: Bcl-2 and Bax (1∶500, Santa Cruz, USA); ERK1/2, phospho-ERK1/2, JNK, phospho-JNK, PP1a, phospho-PP1a, PLB, and phospho-PLB (1∶1000; Cell Signaling Technology, MA, USA); SERCA2a (1∶5000; Abcam; England); and β-actin (1∶1000; Zhongshan; Beijing, China).

    Techniques: Expressing

    KN93 administration reversed CaMKII activation and the disturbed Ca 2+ handling proteins in HFD-induced heart. A, Western blot analysis of phosphorylated CaMKII (p-CaMKII) at T287 site and the total protein CaMKII level in the heart tissue. B, Western blot analysis of phosphorylated RyR2 (p-RyR2) at S2807 and S2814 site, and the total protein level of RyR2 in the heart tissue. C, Western blot analysis of phosphorylated phospholamban (p-PLB) at T17 site and the total protein level of SERCA2 and PLB in the heart tissues. n = 5. * P

    Journal: Journal of Cardiovascular Pharmacology

    Article Title: CaMKII Activation Promotes Cardiac Electrical Remodeling and Increases the Susceptibility to Arrhythmia Induction in High-fat Diet–Fed Mice With Hyperlipidemia Conditions

    doi: 10.1097/FJC.0000000000000512

    Figure Lengend Snippet: KN93 administration reversed CaMKII activation and the disturbed Ca 2+ handling proteins in HFD-induced heart. A, Western blot analysis of phosphorylated CaMKII (p-CaMKII) at T287 site and the total protein CaMKII level in the heart tissue. B, Western blot analysis of phosphorylated RyR2 (p-RyR2) at S2807 and S2814 site, and the total protein level of RyR2 in the heart tissue. C, Western blot analysis of phosphorylated phospholamban (p-PLB) at T17 site and the total protein level of SERCA2 and PLB in the heart tissues. n = 5. * P

    Article Snippet: Primary antibodies used in this study are as follows: CaMKII (santa Cruze Biotech, SC-9035), p-CaMKII (T287, Thermo Fisher Scientific, PA5-37833), RyR2 (Millipore, AB9080), p-RyR2 (S2808, Abcam, ab59225), p-RyR2 (S2814, badrilla, A010-31), PLB (Cell signaling Technology, 8495), p-PLB (Thr17, Badrilla, A010-13), SERCA2 (Abcam, ab150435), Kv4.2 (Sigma, SAB5200070), Kv4.3 (Sigma, SAB5200076), Cav1.2 (Thermo Fisher Scientific, PA5-23015), CX43 (Abcam, ab11370), and β-actin (Boster, BM0627).

    Techniques: Activation Assay, Western Blot

    Protein expression of HCN4, CaMKII, SERCA2a, phospholamban (PLB), PLB-T17, RyR and Nav1.5 in sinoatrial nodes from control rabbits and those with HF (n=6 per group) was analyzed by western blot analysis. α-Sarcomeric actin was used as a loading control. *P

    Journal: Experimental and Therapeutic Medicine

    Article Title: Heart failure modulates electropharmacological characteristics of sinoatrial nodes

    doi: 10.3892/etm.2016.4015

    Figure Lengend Snippet: Protein expression of HCN4, CaMKII, SERCA2a, phospholamban (PLB), PLB-T17, RyR and Nav1.5 in sinoatrial nodes from control rabbits and those with HF (n=6 per group) was analyzed by western blot analysis. α-Sarcomeric actin was used as a loading control. *P

    Article Snippet: Blots were probed with primary antibodies against HCN4 (AB5808; 1:500; Millipore, Billerica, MA, USA), CaMKII (ab54927; 1:500; Abcam, Cambridge, UK), SERCA2a (sc-8095; 1:2,000; Santa Cruz Biotechnology, Inc., Dallas, TX, USA), phospholamban (PLB; MA3-922; 1:2,000; Thermo Fisher Scientific, Inc.), PLB-T17 (A010-13; 1:5,000; Badrilla, Leeds, UK), RyR (MA3-916; 1:1,000; Thermo Fisher Scientific, Inc.), Nav1.5 (AB5493; 1:1,000; Millipore), and one of the following secondary antibodies conjugated to horseradish peroxidase for 1 H at room temperature: Goat anti-Rabbit (AP132P; 1:20,000, Millipore), donkey anti-sheep/goat (AB324P; 1:8,000; Millipore), or goat anti-Mouse (AP124P; 1:8,000; Millipore).

    Techniques: Expressing, Western Blot

    Structural analysis of gliptins-DPP4/8/9 binding. (A) A representative Western blot ( n = 3) showing expression of DPP8 and DPP9 in total protein lysate (50 μg) of HL-1 cardiomyocytes and mouse LV. (B) 3D structural alignment of saxagliptin bound to DPP4 (PDB code: 3bjm) and sitagliptin (PDB code: 1×70) aligned with the 3D structure of DPP8 (PDB code: 6eoo) using pymol. The 3D structure of DPP4 and DPP8 are shown as cartoon representation and colored in orange and gray, respectively. The DPP4-bound forms of saxagliptin and sitagliptin are shown in sticks and colored in magenta and green, respectively. The DPP4 and DPP8 amino-acids present in the gliptin-binding surface of DPP4 are shown in sticks and colored in orange and gray, respectively, if conserved in the structural model or, in red and cyan, if not. (C) 3D structural alignment as described in (B) but using DPP9 (PDB code: 6eoq, colored in yellow) in place of DPP8. Representative Western blots ( n = 6) for (D) pCaMKII (T286), (E) pPLB (T17), and (F) CaMKII and PLB expression in HL-1 cardiomyocytes treated with TC-E 5007 (2 μM) for the indicated time points. GAPDH was used as a loading control. “n” represents the number of experiments.

    Journal: Frontiers in Physiology

    Article Title: Saxagliptin but Not Sitagliptin Inhibits CaMKII and PKC via DPP9 Inhibition in Cardiomyocytes

    doi: 10.3389/fphys.2018.01622

    Figure Lengend Snippet: Structural analysis of gliptins-DPP4/8/9 binding. (A) A representative Western blot ( n = 3) showing expression of DPP8 and DPP9 in total protein lysate (50 μg) of HL-1 cardiomyocytes and mouse LV. (B) 3D structural alignment of saxagliptin bound to DPP4 (PDB code: 3bjm) and sitagliptin (PDB code: 1×70) aligned with the 3D structure of DPP8 (PDB code: 6eoo) using pymol. The 3D structure of DPP4 and DPP8 are shown as cartoon representation and colored in orange and gray, respectively. The DPP4-bound forms of saxagliptin and sitagliptin are shown in sticks and colored in magenta and green, respectively. The DPP4 and DPP8 amino-acids present in the gliptin-binding surface of DPP4 are shown in sticks and colored in orange and gray, respectively, if conserved in the structural model or, in red and cyan, if not. (C) 3D structural alignment as described in (B) but using DPP9 (PDB code: 6eoq, colored in yellow) in place of DPP8. Representative Western blots ( n = 6) for (D) pCaMKII (T286), (E) pPLB (T17), and (F) CaMKII and PLB expression in HL-1 cardiomyocytes treated with TC-E 5007 (2 μM) for the indicated time points. GAPDH was used as a loading control. “n” represents the number of experiments.

    Article Snippet: The following primary antibodies (diluted in 5% [w/v] BSA-TBST) were used: phospho-CaMKII (pCaMKII, T286, 1:1000, Abcam, ab32678), phospho-PLB (pPLB, T17, 1:5000, Badrilla, A010-13), DPP8 (1:500, Santa Cruz, sc-376399), DPP9 (1:500, Santa Cruz, sc-271634), CaMKII (1:500, Santa Cruz, sc-9035), and PLB (1:2000, Thermo Fisher Scientific, MA3-922).

    Techniques: Binding Assay, Western Blot, Expressing

    Saxagliptin but not sitagliptin inhibits the CaMKII-PLB axis. Representative Western blots ( n = 6) for (A–D) pCaMKII (T286), (E–H) pPLB (T17), and (I) CaMKII and PLB expression in HL-1 cardiomyocytes treated with saxagliptin (A,C,E,G) or sitagliptin (B,D,F,H) for the indicated time points ( A , B , E , F,I , 2 μM) and concentrations ( C,D , 5 min; G,H , 30 min). GAPDH was used as a loading control. “n” represents the number of experiments.

    Journal: Frontiers in Physiology

    Article Title: Saxagliptin but Not Sitagliptin Inhibits CaMKII and PKC via DPP9 Inhibition in Cardiomyocytes

    doi: 10.3389/fphys.2018.01622

    Figure Lengend Snippet: Saxagliptin but not sitagliptin inhibits the CaMKII-PLB axis. Representative Western blots ( n = 6) for (A–D) pCaMKII (T286), (E–H) pPLB (T17), and (I) CaMKII and PLB expression in HL-1 cardiomyocytes treated with saxagliptin (A,C,E,G) or sitagliptin (B,D,F,H) for the indicated time points ( A , B , E , F,I , 2 μM) and concentrations ( C,D , 5 min; G,H , 30 min). GAPDH was used as a loading control. “n” represents the number of experiments.

    Article Snippet: The following primary antibodies (diluted in 5% [w/v] BSA-TBST) were used: phospho-CaMKII (pCaMKII, T286, 1:1000, Abcam, ab32678), phospho-PLB (pPLB, T17, 1:5000, Badrilla, A010-13), DPP8 (1:500, Santa Cruz, sc-376399), DPP9 (1:500, Santa Cruz, sc-271634), CaMKII (1:500, Santa Cruz, sc-9035), and PLB (1:2000, Thermo Fisher Scientific, MA3-922).

    Techniques: Western Blot, Expressing

    Saxagliptin inhibits the CaMKII-PLB axis via DPP9 inhibition. (A) mRNA and (B) protein expression of DPP8 and DPP9 in HL-1 cardiomyocytes transfected with si-scr, si-DPP8 or si-DPP9. GAPDH was used as a house keeping gene/protein. A representative Western blot showing (C) pCaMKII (T286), and (D) pPLB (T17) expression in HL-1 cardiomyocytes transfected with si-DPP8 or si-DPP9, and/or treated with saxagliptin or sitagliptin (2 μM each) as indicated for (C) 5 min and (D) 30 min. All values are expressed as mean ± SEM ( n = 6). ∗ p

    Journal: Frontiers in Physiology

    Article Title: Saxagliptin but Not Sitagliptin Inhibits CaMKII and PKC via DPP9 Inhibition in Cardiomyocytes

    doi: 10.3389/fphys.2018.01622

    Figure Lengend Snippet: Saxagliptin inhibits the CaMKII-PLB axis via DPP9 inhibition. (A) mRNA and (B) protein expression of DPP8 and DPP9 in HL-1 cardiomyocytes transfected with si-scr, si-DPP8 or si-DPP9. GAPDH was used as a house keeping gene/protein. A representative Western blot showing (C) pCaMKII (T286), and (D) pPLB (T17) expression in HL-1 cardiomyocytes transfected with si-DPP8 or si-DPP9, and/or treated with saxagliptin or sitagliptin (2 μM each) as indicated for (C) 5 min and (D) 30 min. All values are expressed as mean ± SEM ( n = 6). ∗ p

    Article Snippet: The following primary antibodies (diluted in 5% [w/v] BSA-TBST) were used: phospho-CaMKII (pCaMKII, T286, 1:1000, Abcam, ab32678), phospho-PLB (pPLB, T17, 1:5000, Badrilla, A010-13), DPP8 (1:500, Santa Cruz, sc-376399), DPP9 (1:500, Santa Cruz, sc-271634), CaMKII (1:500, Santa Cruz, sc-9035), and PLB (1:2000, Thermo Fisher Scientific, MA3-922).

    Techniques: Inhibition, Expressing, Transfection, Western Blot