hexanoic acid-2 Search Results


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  • 99
    Thermo Fisher sulfo sanpah
    CaM binding to the RyR2 in cardiac homogenates. ( A ) (Top) Representative immunoblots of the RyR2-bound <t>CaM-SANPAH</t> (a <t>photoreactive</t> cross-linker). The WT and KI cardiac homogenates were first diluted in binding buffer (150 mM KCl, 10 μM CaCl 2 , and 20 mM MES at pH 6.8) and then reacted with various concentrations of CaM-SANPAH (32–1024 nM) in the presence or absence of cAMP (1 μM) and okadaic acid (1 μM). CaM binding to the RyR2 was determined by immunoblotting with anti-CaM antibody to detect the RyR2-bound CaM. (Bottom) Summarized data of CaM binding to the RyR2 as a function of the concentration of CaM-SANPAH. CaM binding was expressed as the ratio to the maximum binding of CaM (at 1024 nM). Data are presented mean ± SEM of 3 hearts. ( B ) Effect of cAMP (1 μM) and suramin (10 μM) on CaM binding to the RyR2. The concentration of CaM-SANPAH was fixed at 128 nM. Data are presented as mean ± SEM of 3 hearts. * P
    Sulfo Sanpah, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 610 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore stannous 2 ethyl hexanoate
    CaM binding to the RyR2 in cardiac homogenates. ( A ) (Top) Representative immunoblots of the RyR2-bound <t>CaM-SANPAH</t> (a <t>photoreactive</t> cross-linker). The WT and KI cardiac homogenates were first diluted in binding buffer (150 mM KCl, 10 μM CaCl 2 , and 20 mM MES at pH 6.8) and then reacted with various concentrations of CaM-SANPAH (32–1024 nM) in the presence or absence of cAMP (1 μM) and okadaic acid (1 μM). CaM binding to the RyR2 was determined by immunoblotting with anti-CaM antibody to detect the RyR2-bound CaM. (Bottom) Summarized data of CaM binding to the RyR2 as a function of the concentration of CaM-SANPAH. CaM binding was expressed as the ratio to the maximum binding of CaM (at 1024 nM). Data are presented mean ± SEM of 3 hearts. ( B ) Effect of cAMP (1 μM) and suramin (10 μM) on CaM binding to the RyR2. The concentration of CaM-SANPAH was fixed at 128 nM. Data are presented as mean ± SEM of 3 hearts. * P
    Stannous 2 Ethyl Hexanoate, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Thermo Fisher sulfo lc spdp
    CaM binding to the RyR2 in cardiac homogenates. ( A ) (Top) Representative immunoblots of the RyR2-bound <t>CaM-SANPAH</t> (a <t>photoreactive</t> cross-linker). The WT and KI cardiac homogenates were first diluted in binding buffer (150 mM KCl, 10 μM CaCl 2 , and 20 mM MES at pH 6.8) and then reacted with various concentrations of CaM-SANPAH (32–1024 nM) in the presence or absence of cAMP (1 μM) and okadaic acid (1 μM). CaM binding to the RyR2 was determined by immunoblotting with anti-CaM antibody to detect the RyR2-bound CaM. (Bottom) Summarized data of CaM binding to the RyR2 as a function of the concentration of CaM-SANPAH. CaM binding was expressed as the ratio to the maximum binding of CaM (at 1024 nM). Data are presented mean ± SEM of 3 hearts. ( B ) Effect of cAMP (1 μM) and suramin (10 μM) on CaM binding to the RyR2. The concentration of CaM-SANPAH was fixed at 128 nM. Data are presented as mean ± SEM of 3 hearts. * P
    Sulfo Lc Spdp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 89 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher n 6 biotinamido hexyl 3 2 pyridyldithio propionamide biotin hpdp
    CaM binding to the RyR2 in cardiac homogenates. ( A ) (Top) Representative immunoblots of the RyR2-bound <t>CaM-SANPAH</t> (a <t>photoreactive</t> cross-linker). The WT and KI cardiac homogenates were first diluted in binding buffer (150 mM KCl, 10 μM CaCl 2 , and 20 mM MES at pH 6.8) and then reacted with various concentrations of CaM-SANPAH (32–1024 nM) in the presence or absence of cAMP (1 μM) and okadaic acid (1 μM). CaM binding to the RyR2 was determined by immunoblotting with anti-CaM antibody to detect the RyR2-bound CaM. (Bottom) Summarized data of CaM binding to the RyR2 as a function of the concentration of CaM-SANPAH. CaM binding was expressed as the ratio to the maximum binding of CaM (at 1024 nM). Data are presented mean ± SEM of 3 hearts. ( B ) Effect of cAMP (1 μM) and suramin (10 μM) on CaM binding to the RyR2. The concentration of CaM-SANPAH was fixed at 128 nM. Data are presented as mean ± SEM of 3 hearts. * P
    N 6 Biotinamido Hexyl 3 2 Pyridyldithio Propionamide Biotin Hpdp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher succinimidyl 6
    CaM binding to the RyR2 in cardiac homogenates. ( A ) (Top) Representative immunoblots of the RyR2-bound <t>CaM-SANPAH</t> (a <t>photoreactive</t> cross-linker). The WT and KI cardiac homogenates were first diluted in binding buffer (150 mM KCl, 10 μM CaCl 2 , and 20 mM MES at pH 6.8) and then reacted with various concentrations of CaM-SANPAH (32–1024 nM) in the presence or absence of cAMP (1 μM) and okadaic acid (1 μM). CaM binding to the RyR2 was determined by immunoblotting with anti-CaM antibody to detect the RyR2-bound CaM. (Bottom) Summarized data of CaM binding to the RyR2 as a function of the concentration of CaM-SANPAH. CaM binding was expressed as the ratio to the maximum binding of CaM (at 1024 nM). Data are presented mean ± SEM of 3 hearts. ( B ) Effect of cAMP (1 μM) and suramin (10 μM) on CaM binding to the RyR2. The concentration of CaM-SANPAH was fixed at 128 nM. Data are presented as mean ± SEM of 3 hearts. * P
    Succinimidyl 6, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 182 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher n 7 nitrobenz 2 oxa 1 3 diazol 4 yl amino hexanoic acid c6 nbd
    CaM binding to the RyR2 in cardiac homogenates. ( A ) (Top) Representative immunoblots of the RyR2-bound <t>CaM-SANPAH</t> (a <t>photoreactive</t> cross-linker). The WT and KI cardiac homogenates were first diluted in binding buffer (150 mM KCl, 10 μM CaCl 2 , and 20 mM MES at pH 6.8) and then reacted with various concentrations of CaM-SANPAH (32–1024 nM) in the presence or absence of cAMP (1 μM) and okadaic acid (1 μM). CaM binding to the RyR2 was determined by immunoblotting with anti-CaM antibody to detect the RyR2-bound CaM. (Bottom) Summarized data of CaM binding to the RyR2 as a function of the concentration of CaM-SANPAH. CaM binding was expressed as the ratio to the maximum binding of CaM (at 1024 nM). Data are presented mean ± SEM of 3 hearts. ( B ) Effect of cAMP (1 μM) and suramin (10 μM) on CaM binding to the RyR2. The concentration of CaM-SANPAH was fixed at 128 nM. Data are presented as mean ± SEM of 3 hearts. * P
    N 7 Nitrobenz 2 Oxa 1 3 Diazol 4 Yl Amino Hexanoic Acid C6 Nbd, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Thermo Fisher lc spdp
    Biotin transfer workflow for identification of the ligand-binding partner. ( a) Ligand labelling: Ligands of interest are labelled in a two-step reaction through addition of a commercial amine-to-sulfhydryl crosslinker <t>(LC-SPDP</t> or <t>PEG4</t> version) followed by addition of ASB. Both a control ligand and a ligand-of-interest are prepared in parallel. ( b ) Biotin-transfer to cell surface receptor on periodate-treated live cells: The labelled ligand in incubated with cells to encourage ligand-directed cell surface binding prior to addition of a catalyst to promote oxime bond formation and crosslinking. Cells are then solubilized under reducing conditions resulting in the transfer of the biotin from the ligand to its crosslinked binding partner. ( c ) Isolation of biotinylated proteins and identification of enriched peptides by comparative mass spectrometry: Biotinylated proteins are immobilized on a streptavidin resin and digested with trypsin. The intensity of peptides resulting from parallel experiments with the control ligand and the ligand-of-interest are then compared using standard mass spectrometry-based proteomic workflows.
    Lc Spdp, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 98 stars, based on 21 article reviews
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    N/A
    Methyl 2 bromohexanoate undergoes addition reaction with methyl 10 undecenoate to yield lactone and dimethyl 2 butyltridecandioate
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    N/A
    Phorbol 12 13 Dihexanoate is a potent and hydrophobic PKC activator and a potent tumor promoter
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    Image Search Results


    CaM binding to the RyR2 in cardiac homogenates. ( A ) (Top) Representative immunoblots of the RyR2-bound CaM-SANPAH (a photoreactive cross-linker). The WT and KI cardiac homogenates were first diluted in binding buffer (150 mM KCl, 10 μM CaCl 2 , and 20 mM MES at pH 6.8) and then reacted with various concentrations of CaM-SANPAH (32–1024 nM) in the presence or absence of cAMP (1 μM) and okadaic acid (1 μM). CaM binding to the RyR2 was determined by immunoblotting with anti-CaM antibody to detect the RyR2-bound CaM. (Bottom) Summarized data of CaM binding to the RyR2 as a function of the concentration of CaM-SANPAH. CaM binding was expressed as the ratio to the maximum binding of CaM (at 1024 nM). Data are presented mean ± SEM of 3 hearts. ( B ) Effect of cAMP (1 μM) and suramin (10 μM) on CaM binding to the RyR2. The concentration of CaM-SANPAH was fixed at 128 nM. Data are presented as mean ± SEM of 3 hearts. * P

    Journal: JCI Insight

    Article Title: Ryanodine receptor–bound calmodulin is essential to protect against catecholaminergic polymorphic ventricular tachycardia

    doi: 10.1172/jci.insight.126112

    Figure Lengend Snippet: CaM binding to the RyR2 in cardiac homogenates. ( A ) (Top) Representative immunoblots of the RyR2-bound CaM-SANPAH (a photoreactive cross-linker). The WT and KI cardiac homogenates were first diluted in binding buffer (150 mM KCl, 10 μM CaCl 2 , and 20 mM MES at pH 6.8) and then reacted with various concentrations of CaM-SANPAH (32–1024 nM) in the presence or absence of cAMP (1 μM) and okadaic acid (1 μM). CaM binding to the RyR2 was determined by immunoblotting with anti-CaM antibody to detect the RyR2-bound CaM. (Bottom) Summarized data of CaM binding to the RyR2 as a function of the concentration of CaM-SANPAH. CaM binding was expressed as the ratio to the maximum binding of CaM (at 1024 nM). Data are presented mean ± SEM of 3 hearts. ( B ) Effect of cAMP (1 μM) and suramin (10 μM) on CaM binding to the RyR2. The concentration of CaM-SANPAH was fixed at 128 nM. Data are presented as mean ± SEM of 3 hearts. * P

    Article Snippet: The binding of CaM to the RyR2 was evaluated using the photoreactive cross-linker sulfo-SANPAH (Thermo Fisher Scientific) as described previously ( ).

    Techniques: Chick Chorioallantoic Membrane Assay, Binding Assay, Western Blot, Concentration Assay

    Biotin transfer workflow for identification of the ligand-binding partner. ( a) Ligand labelling: Ligands of interest are labelled in a two-step reaction through addition of a commercial amine-to-sulfhydryl crosslinker (LC-SPDP or PEG4 version) followed by addition of ASB. Both a control ligand and a ligand-of-interest are prepared in parallel. ( b ) Biotin-transfer to cell surface receptor on periodate-treated live cells: The labelled ligand in incubated with cells to encourage ligand-directed cell surface binding prior to addition of a catalyst to promote oxime bond formation and crosslinking. Cells are then solubilized under reducing conditions resulting in the transfer of the biotin from the ligand to its crosslinked binding partner. ( c ) Isolation of biotinylated proteins and identification of enriched peptides by comparative mass spectrometry: Biotinylated proteins are immobilized on a streptavidin resin and digested with trypsin. The intensity of peptides resulting from parallel experiments with the control ligand and the ligand-of-interest are then compared using standard mass spectrometry-based proteomic workflows.

    Journal: Scientific Reports

    Article Title: Biotin-transfer from a trifunctional crosslinker for identification of cell surface receptors of soluble protein ligands

    doi: 10.1038/srep46574

    Figure Lengend Snippet: Biotin transfer workflow for identification of the ligand-binding partner. ( a) Ligand labelling: Ligands of interest are labelled in a two-step reaction through addition of a commercial amine-to-sulfhydryl crosslinker (LC-SPDP or PEG4 version) followed by addition of ASB. Both a control ligand and a ligand-of-interest are prepared in parallel. ( b ) Biotin-transfer to cell surface receptor on periodate-treated live cells: The labelled ligand in incubated with cells to encourage ligand-directed cell surface binding prior to addition of a catalyst to promote oxime bond formation and crosslinking. Cells are then solubilized under reducing conditions resulting in the transfer of the biotin from the ligand to its crosslinked binding partner. ( c ) Isolation of biotinylated proteins and identification of enriched peptides by comparative mass spectrometry: Biotinylated proteins are immobilized on a streptavidin resin and digested with trypsin. The intensity of peptides resulting from parallel experiments with the control ligand and the ligand-of-interest are then compared using standard mass spectrometry-based proteomic workflows.

    Article Snippet: For the first step, 20 nmol of a linker, LC-SPDP or PEG4 -SPDP (Thermo Fisher), was incubated with the ligand for 30 minutes at RT.

    Techniques: Ligand Binding Assay, Cell Surface Receptor Assay, Incubation, Binding Assay, Isolation, Mass Spectrometry

    ASB labelling of a monoclonal antibody (anti-transferrin receptor) with either LC-SPDP+ASB or PEG4-SPDP+ASB leads to a visible shift in both the heavy chain and the light chain by SDS-PAGE. Total protein was visualized using Sypro Ruby under reducing conditions.

    Journal: Scientific Reports

    Article Title: Biotin-transfer from a trifunctional crosslinker for identification of cell surface receptors of soluble protein ligands

    doi: 10.1038/srep46574

    Figure Lengend Snippet: ASB labelling of a monoclonal antibody (anti-transferrin receptor) with either LC-SPDP+ASB or PEG4-SPDP+ASB leads to a visible shift in both the heavy chain and the light chain by SDS-PAGE. Total protein was visualized using Sypro Ruby under reducing conditions.

    Article Snippet: For the first step, 20 nmol of a linker, LC-SPDP or PEG4 -SPDP (Thermo Fisher), was incubated with the ligand for 30 minutes at RT.

    Techniques: SDS Page