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  • 88
    Jena Bioscience magnesium acetate
    Magnesium Acetate, supplied by Jena Bioscience, 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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    99
    Millipore mgac
    Mgac, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 54 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Promega mgac
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Mgac, supplied by Promega, used in various techniques. Bioz Stars score: 94/100, based on 201 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Applichem mgac
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Mgac, supplied by Applichem, used in various techniques. Bioz Stars score: 90/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck KGaA magnesium acetate
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Magnesium Acetate, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 92/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Fisher Scientific magnesium acetate
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Magnesium Acetate, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 92/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    TwistDx magnesium acetate
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Magnesium Acetate, supplied by TwistDx, used in various techniques. Bioz Stars score: 92/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Carl Roth GmbH magnesium acetate
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Magnesium Acetate, supplied by Carl Roth GmbH, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 4 article reviews
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    99
    Millipore m magnesium acetate
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    M Magnesium Acetate, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 56 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    FUJIFILM magnesium acetate
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Magnesium Acetate, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 92/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Eppendorf AG magnesium acetate
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Magnesium Acetate, supplied by Eppendorf AG, used in various techniques. Bioz Stars score: 92/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Thermo Fisher magnesium acetate buffer
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Magnesium Acetate Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher magnesium acetate heptahydrate
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Magnesium Acetate Heptahydrate, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Millipore magnesium acetate tetrahydrate
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    Magnesium Acetate Tetrahydrate, supplied by Millipore, used in various techniques. Bioz Stars score: 89/100, based on 97 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck & Co m magnesium acetate tetrahydrate
    <t>Dephosphorylation</t> of PC1 by PP1α. To determine whether PP1α can dephosphorylate <t>PKA-phosphorylated</t> PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.
    M Magnesium Acetate Tetrahydrate, supplied by Merck & Co, used in various techniques. Bioz Stars score: 92/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Dephosphorylation of PC1 by PP1α. To determine whether PP1α can dephosphorylate PKA-phosphorylated PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.

    Journal: PLoS ONE

    Article Title: Protein Phosphatase-1? Interacts with and Dephosphorylates Polycystin-1

    doi: 10.1371/journal.pone.0036798

    Figure Lengend Snippet: Dephosphorylation of PC1 by PP1α. To determine whether PP1α can dephosphorylate PKA-phosphorylated PC1, a GST-PC1 C-tail fusion protein (GST-HT 193 ) was purified from bacteria, bound to GSH-agarose beads, and phosphorylated by PKA with [γ- 32 P]ATP. Unincorporated 32 P was removed by washing the fusion protein with an excess of cold ATP in PP1α or PP2B reaction buffer. The radiolabeled protein was then incubated in the presence or absence of purified, recombinant PP1α or PP2B (calcineurin) for 0–2 h. Aliquots of the reaction were removed and tested for phosphatase activity against the generic substrate p-nitrophenyl phosphate (pNPP) or frozen on dry ice in 1× SDS-PAGE sample buffer to terminate the phosphatase reaction. Terminated reactions were resolved by SDS-PAGE, and phosphorylated fusion protein was detected first by autoradiography (AR) followed by immunoblotting.

    Article Snippet: Protein Phosphorylation and Dephosphorylation Purified fusion proteins were adsorbed to GSH-Sepharose beads pre-washed in PKA buffer (40 mM Tris-HCl pH 7.4, 20 mM magnesium acetate) and phosphorylated with ∼190 units/ml purified, recombinant catalytic subunit of cAMP-dependent protein kinase (Promega) in PKA buffer with 0.2 mM ATP and 50 µCi/ml [γ-32 P]ATP, 3,000 Ci/mmol (PerkinElmer).

    Techniques: De-Phosphorylation Assay, Purification, Incubation, Recombinant, Activity Assay, SDS Page, Autoradiography

    Dephosphorylation of human PC1 by PP1α. To determine whether PP1α can also dephosphorylate PKA-phosphorylated human PC1 (hPC1), GST-hPC1 C-tail fusion proteins (GST-hHT 193 and GST-hHT 193 S4168A) were purified, phosphorylated, and detected as described in Figure 4 . GST-hHT 193 S4168A was used in this analysis to be certain that phosphorylation and dephosphorylation was occurring on a residue other than S4168, which is equivalent to the site of PKA phosphorylation on mouse PC1 (S4159).

    Journal: PLoS ONE

    Article Title: Protein Phosphatase-1? Interacts with and Dephosphorylates Polycystin-1

    doi: 10.1371/journal.pone.0036798

    Figure Lengend Snippet: Dephosphorylation of human PC1 by PP1α. To determine whether PP1α can also dephosphorylate PKA-phosphorylated human PC1 (hPC1), GST-hPC1 C-tail fusion proteins (GST-hHT 193 and GST-hHT 193 S4168A) were purified, phosphorylated, and detected as described in Figure 4 . GST-hHT 193 S4168A was used in this analysis to be certain that phosphorylation and dephosphorylation was occurring on a residue other than S4168, which is equivalent to the site of PKA phosphorylation on mouse PC1 (S4159).

    Article Snippet: Protein Phosphorylation and Dephosphorylation Purified fusion proteins were adsorbed to GSH-Sepharose beads pre-washed in PKA buffer (40 mM Tris-HCl pH 7.4, 20 mM magnesium acetate) and phosphorylated with ∼190 units/ml purified, recombinant catalytic subunit of cAMP-dependent protein kinase (Promega) in PKA buffer with 0.2 mM ATP and 50 µCi/ml [γ-32 P]ATP, 3,000 Ci/mmol (PerkinElmer).

    Techniques: De-Phosphorylation Assay, Purification