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Promega atp glo kinase kit
Atp Glo Kinase Kit, supplied by Promega, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/atp glo kinase kit/product/Promega
Average 85 stars, based on 1 article reviews
Price from $9.99 to $1999.99
atp glo kinase kit - by Bioz Stars, 2020-04
85/100 stars

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BIA-KA:

Article Title: Ceramide 1-phosphate stimulates glucose uptake in macrophages
Article Snippet: Nitrocellulose membranes, protein markers, and BCA assay reagents were purchased from Bio-Rad. .. The ATP-Glo Kinase Kit™ was from Promega.

Synthesized:

Article Title: Ceramide 1-phosphate stimulates glucose uptake in macrophages
Article Snippet: BHNB-C1P was synthesized as described previously [ ]. .. The ATP-Glo Kinase Kit™ was from Promega.

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  • 95
    Promega adp glo kinase assay kit
    PTN-induced CDK5 activation depends on RPTPβ/ζ but not α ν β3 integrin. ( a ) CDK5 activity was measured using the <t>ADP-Glo</t> Kinase Assay, in CDK5 immunoprecipitates from HUVEC following RPTPβ/ζ knockdown through siRNA (50 nM). Results are expressed as mean ± SE (n = 3) of the percent change in CDK5 activity in PTN-stimulated vs the untreated siNeg cells (set as default 100%). ( b ) HUVEC lysates following RPTPβ/ζ knockdown, through siRNA, were immunoprecipitated with a p35 antibody and the immunoprecipitates were analysed by Western blot for the presence of CDK5 and p35. CDK5 and p35 protein amounts were quantified and the ratio of p35 to CDK5 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change of CDK5/p35 ratio in PTN-stimulated vs. the untreated siNeg cells (set as default 100%). siNeg, cells transfected with a negative control siRNA; siRPTPβ/ζ, cells transfected with siRNA for RPTPβ/ζ. ( c ) HUVEC cells were treated in the presence or absence of peptide B3 (1 μg/ml), known to block PTN-α ν β 3 interaction. Whole cell lysates were immunoprecipitated for p35 and the immunoprecipitates were analysed by Western blot for the presence of CDK5 and p35. CDK5 and p35 protein amounts were quantified and the ratio of p35 to CDK5 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change of CDK5/p35 ratio in stimulated vs. the untreated cells (set as default 100%). ( d ) HUVEC were incubated with PTN (100 ng/ml) in the absence or presence of roscovitine (10 μΜ). Phosphorylation of β 3 Tyr773 was estimated in total cell lysates by Western blot as described in Materials and Methods. Phospho-β 3 Tyr773 (pβ 3 ) and total β 3 (tβ 3 ) amounts were quantified and the ratio pβ 3 /tβ 3 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change in phospho-β 3 Tyr773 relative amounts in PTN-stimulated vs. the untreated cells (set as default 100%). F values of the ANOVA tests are 38.7 for ( a ), 7.8 for ( b ), 18.2 for ( c ) and 11.9 for ( d ).
    Adp Glo Kinase Assay Kit, supplied by Promega, used in various techniques. Bioz Stars score: 95/100, based on 116 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adp glo kinase assay kit/product/Promega
    Average 95 stars, based on 116 article reviews
    Price from $9.99 to $1999.99
    adp glo kinase assay kit - by Bioz Stars, 2020-04
    95/100 stars
      Buy from Supplier

    94
    Promega kinase glo luminescent kinase assay kit
    The kinase activities of GST fusion proteins were measured in vitro . A. Phosphorylation activities of GST fusion proteins containing full-length Stk (using plasmid pQG77), Stk 1–263 (pQG78) or Stk 40–263 (pQG79) were measured with a <t>Kinase-Glo™</t> luminescent kinase assay in vitro at <t>32°C</t> for 4 h. B. Phosphorylation activities of GST fusion proteins containing full-length Stk (using plasmid pQG77) were measured with a Kinase-Glo™ luminescent kinase assay with or without staurosporine in vitro at 32°C for 4 h. GST was used as a negative control. RLU, relative luminescent unit. Data are derived from three independent experiments, **, P
    Kinase Glo Luminescent Kinase Assay Kit, supplied by Promega, used in various techniques. Bioz Stars score: 94/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/kinase glo luminescent kinase assay kit/product/Promega
    Average 94 stars, based on 23 article reviews
    Price from $9.99 to $1999.99
    kinase glo luminescent kinase assay kit - by Bioz Stars, 2020-04
    94/100 stars
      Buy from Supplier

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    PTN-induced CDK5 activation depends on RPTPβ/ζ but not α ν β3 integrin. ( a ) CDK5 activity was measured using the ADP-Glo Kinase Assay, in CDK5 immunoprecipitates from HUVEC following RPTPβ/ζ knockdown through siRNA (50 nM). Results are expressed as mean ± SE (n = 3) of the percent change in CDK5 activity in PTN-stimulated vs the untreated siNeg cells (set as default 100%). ( b ) HUVEC lysates following RPTPβ/ζ knockdown, through siRNA, were immunoprecipitated with a p35 antibody and the immunoprecipitates were analysed by Western blot for the presence of CDK5 and p35. CDK5 and p35 protein amounts were quantified and the ratio of p35 to CDK5 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change of CDK5/p35 ratio in PTN-stimulated vs. the untreated siNeg cells (set as default 100%). siNeg, cells transfected with a negative control siRNA; siRPTPβ/ζ, cells transfected with siRNA for RPTPβ/ζ. ( c ) HUVEC cells were treated in the presence or absence of peptide B3 (1 μg/ml), known to block PTN-α ν β 3 interaction. Whole cell lysates were immunoprecipitated for p35 and the immunoprecipitates were analysed by Western blot for the presence of CDK5 and p35. CDK5 and p35 protein amounts were quantified and the ratio of p35 to CDK5 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change of CDK5/p35 ratio in stimulated vs. the untreated cells (set as default 100%). ( d ) HUVEC were incubated with PTN (100 ng/ml) in the absence or presence of roscovitine (10 μΜ). Phosphorylation of β 3 Tyr773 was estimated in total cell lysates by Western blot as described in Materials and Methods. Phospho-β 3 Tyr773 (pβ 3 ) and total β 3 (tβ 3 ) amounts were quantified and the ratio pβ 3 /tβ 3 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change in phospho-β 3 Tyr773 relative amounts in PTN-stimulated vs. the untreated cells (set as default 100%). F values of the ANOVA tests are 38.7 for ( a ), 7.8 for ( b ), 18.2 for ( c ) and 11.9 for ( d ).

    Journal: Scientific Reports

    Article Title: Cyclin-dependent kinase 5 mediates pleiotrophin-induced endothelial cell migration

    doi: 10.1038/s41598-018-24326-x

    Figure Lengend Snippet: PTN-induced CDK5 activation depends on RPTPβ/ζ but not α ν β3 integrin. ( a ) CDK5 activity was measured using the ADP-Glo Kinase Assay, in CDK5 immunoprecipitates from HUVEC following RPTPβ/ζ knockdown through siRNA (50 nM). Results are expressed as mean ± SE (n = 3) of the percent change in CDK5 activity in PTN-stimulated vs the untreated siNeg cells (set as default 100%). ( b ) HUVEC lysates following RPTPβ/ζ knockdown, through siRNA, were immunoprecipitated with a p35 antibody and the immunoprecipitates were analysed by Western blot for the presence of CDK5 and p35. CDK5 and p35 protein amounts were quantified and the ratio of p35 to CDK5 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change of CDK5/p35 ratio in PTN-stimulated vs. the untreated siNeg cells (set as default 100%). siNeg, cells transfected with a negative control siRNA; siRPTPβ/ζ, cells transfected with siRNA for RPTPβ/ζ. ( c ) HUVEC cells were treated in the presence or absence of peptide B3 (1 μg/ml), known to block PTN-α ν β 3 interaction. Whole cell lysates were immunoprecipitated for p35 and the immunoprecipitates were analysed by Western blot for the presence of CDK5 and p35. CDK5 and p35 protein amounts were quantified and the ratio of p35 to CDK5 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change of CDK5/p35 ratio in stimulated vs. the untreated cells (set as default 100%). ( d ) HUVEC were incubated with PTN (100 ng/ml) in the absence or presence of roscovitine (10 μΜ). Phosphorylation of β 3 Tyr773 was estimated in total cell lysates by Western blot as described in Materials and Methods. Phospho-β 3 Tyr773 (pβ 3 ) and total β 3 (tβ 3 ) amounts were quantified and the ratio pβ 3 /tβ 3 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change in phospho-β 3 Tyr773 relative amounts in PTN-stimulated vs. the untreated cells (set as default 100%). F values of the ANOVA tests are 38.7 for ( a ), 7.8 for ( b ), 18.2 for ( c ) and 11.9 for ( d ).

    Article Snippet: Alternatively, a non-radioactive CDK5 activity assay was developed by using the ADP-Glo™ Kinase Assay kit (Promega Corporation) and 100 μg of total cell or tissue lysates immunoprecipitated with an antibody for CDK5.

    Techniques: Activation Assay, Activity Assay, Kinase Assay, Immunoprecipitation, Western Blot, Transfection, Negative Control, Blocking Assay, Incubation

    PTN-induced CDK5 activation depends on PI3K but not c-Src or ERK1/2. ( a ) CDK5 activity was measured in CDK5 immunoprecipitates from HUVEC previously treated with the following pharmacological inhibitors: SU6656 (10 μΜ), wortmannin (wortmn, 100 nM) or U0126 (20 nM). CDK5 activity was evaluated by using the ADP-Glo Kinase Assay. Results are expressed as mean ± SE (n = 3) of the percent change in CDK5 activity in PTN-stimulated vs the untreated cells (set as default 100%). ( b ) HUVEC were incubated with PTN (100 ng/ml) in the absence or presence of roscovitine (10 μΜ). Phosphorylation of ERK1/2 was estimated in total cell lysates by Western blot as described in Materials and Methods. Phospho-ERK1/2 (pERK1/2) and total ERK1/2 (tERK1/2) amounts were quantified and the ratio pERK1/2/tERK1/2 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change in phospho-ERK1/2 relative amounts in PTN-stimulated vs. the untreated cells (set as default 100%). F values of the ANOVA tests are 15.8 for ( a ) and 7.8 for ( b ).

    Journal: Scientific Reports

    Article Title: Cyclin-dependent kinase 5 mediates pleiotrophin-induced endothelial cell migration

    doi: 10.1038/s41598-018-24326-x

    Figure Lengend Snippet: PTN-induced CDK5 activation depends on PI3K but not c-Src or ERK1/2. ( a ) CDK5 activity was measured in CDK5 immunoprecipitates from HUVEC previously treated with the following pharmacological inhibitors: SU6656 (10 μΜ), wortmannin (wortmn, 100 nM) or U0126 (20 nM). CDK5 activity was evaluated by using the ADP-Glo Kinase Assay. Results are expressed as mean ± SE (n = 3) of the percent change in CDK5 activity in PTN-stimulated vs the untreated cells (set as default 100%). ( b ) HUVEC were incubated with PTN (100 ng/ml) in the absence or presence of roscovitine (10 μΜ). Phosphorylation of ERK1/2 was estimated in total cell lysates by Western blot as described in Materials and Methods. Phospho-ERK1/2 (pERK1/2) and total ERK1/2 (tERK1/2) amounts were quantified and the ratio pERK1/2/tERK1/2 was calculated in each lane. Results are expressed as mean ± SE (n = 3) of the percent change in phospho-ERK1/2 relative amounts in PTN-stimulated vs. the untreated cells (set as default 100%). F values of the ANOVA tests are 15.8 for ( a ) and 7.8 for ( b ).

    Article Snippet: Alternatively, a non-radioactive CDK5 activity assay was developed by using the ADP-Glo™ Kinase Assay kit (Promega Corporation) and 100 μg of total cell or tissue lysates immunoprecipitated with an antibody for CDK5.

    Techniques: Activation Assay, Activity Assay, Kinase Assay, Incubation, Western Blot

    Biochemical and pharmacological characterization of PI3KD/V-IN-01 A. Chemical structure of PI3KD/V-IN-01. B. ADP-Glo™ Biochemical IC50 determination of PI3KD/V-IN-01 against a panel of PI3K-related kinases. C. Determination of the inhibitory effect of PI3KD/V-IN-01 against class I PI3Ks in the cellular context. Specifically, PI3Kα in NIH-3T3 cells with PDGF-BB stimulation; PI3Kβ in NIH-3T3 cells with LPA stimulation; PI3Kγ in RAW264.7 cells with C5a stimulation; PI3Kδ in Raji cells with anti-IgM stimulation. D. Selectivity profile of PI3KD/V-IN-01 in the DiscoveRx's KinomeScan™ platform. E. Effect of PI3KD/V-IN-01 on autophagy in HeLa cells using co-culture of EBSS and HCQ (25 μM) and investigating LC3BII expression. F. Immuno-fluorescent imaging analysis of the effect of PI3K inhibitors on LC3BII expression in HeLa cells and of LAMP1 expression in HeLa cells treated with PI3K inhibitors.

    Journal: Oncotarget

    Article Title: Simultaneous inhibition of Vps34 kinase would enhance PI3Kδ inhibitor cytotoxicity in the B-cell malignancies

    doi: 10.18632/oncotarget.10650

    Figure Lengend Snippet: Biochemical and pharmacological characterization of PI3KD/V-IN-01 A. Chemical structure of PI3KD/V-IN-01. B. ADP-Glo™ Biochemical IC50 determination of PI3KD/V-IN-01 against a panel of PI3K-related kinases. C. Determination of the inhibitory effect of PI3KD/V-IN-01 against class I PI3Ks in the cellular context. Specifically, PI3Kα in NIH-3T3 cells with PDGF-BB stimulation; PI3Kβ in NIH-3T3 cells with LPA stimulation; PI3Kγ in RAW264.7 cells with C5a stimulation; PI3Kδ in Raji cells with anti-IgM stimulation. D. Selectivity profile of PI3KD/V-IN-01 in the DiscoveRx's KinomeScan™ platform. E. Effect of PI3KD/V-IN-01 on autophagy in HeLa cells using co-culture of EBSS and HCQ (25 μM) and investigating LC3BII expression. F. Immuno-fluorescent imaging analysis of the effect of PI3K inhibitors on LC3BII expression in HeLa cells and of LAMP1 expression in HeLa cells treated with PI3K inhibitors.

    Article Snippet: The ADP-Glo™ kinase assay kit was from Promega Corporation.

    Techniques: Co-Culture Assay, Expressing, Imaging

    Evaluation of ADP-Glo™ kinase assay linearity and implementation of the assay for parasite lysate . Panel A . ATP to ADP conversion curves were prepared at the indicated “ATP + ADP” concentration in 20 μl of 1× reaction buffer. Kinase assay was performed as described in methods section. There is a linear relationship observed between the luminescent signal and amount of ADP present in the reaction mix. Panel B . ADP-Glo™ Kinase Assay was utilized to detect functional activity of kinases in the parasite lysate. Reactions were setup by taking varying amounts of the lysate in a total volume of 20 μl per reaction, as described in methods section. Kinase reactions were initiated by adding 1 μM ATP and allowed to take place at 30 °C for 1 h, followed by ADP-Glo™ kinase assay. The luminescence signal thus produced increases with the amount of lysate in a kinase reaction. Luminescence values represent the mean of two replicates. Abbreviation: RLU, Relative Lights Unit.

    Journal: MethodsX

    Article Title: Screening of chemical library against whole cell kinome activity via non-radioactive, high throughput kinase assay

    doi: 10.1016/j.mex.2018.12.003

    Figure Lengend Snippet: Evaluation of ADP-Glo™ kinase assay linearity and implementation of the assay for parasite lysate . Panel A . ATP to ADP conversion curves were prepared at the indicated “ATP + ADP” concentration in 20 μl of 1× reaction buffer. Kinase assay was performed as described in methods section. There is a linear relationship observed between the luminescent signal and amount of ADP present in the reaction mix. Panel B . ADP-Glo™ Kinase Assay was utilized to detect functional activity of kinases in the parasite lysate. Reactions were setup by taking varying amounts of the lysate in a total volume of 20 μl per reaction, as described in methods section. Kinase reactions were initiated by adding 1 μM ATP and allowed to take place at 30 °C for 1 h, followed by ADP-Glo™ kinase assay. The luminescence signal thus produced increases with the amount of lysate in a kinase reaction. Luminescence values represent the mean of two replicates. Abbreviation: RLU, Relative Lights Unit.

    Article Snippet: The composition for measuring functional activity of the parasite kinome involves ATP regeneration-based luciferase reaction system resulting from nascent ADP phosphorylation by utilizing ADP-Glo™ kinase assay kit (Promega Corporation, catalog no. V9101).

    Techniques: Kinase Assay, Concentration Assay, Functional Assay, Activity Assay, Produced

    Applications of ADP-Glo™ kinase assay with parasite lysate . Panel A . To Elucidate proportion of calcium-dependent protein kinases in the parasite kinome, kinase reaction was performed using 10 ng of parasite lysate in the presence and absence of 2.5 mM Ca 2+ , as described in methods section. ˜30% of kinome activity has been reported to impart largely because of calcium-dependent protein kinases. Panel B . To check if the assay can be applied for HTS, thio-oxo-imidazolidinone derivative, MCR03 was tested for any effect on the activity of kinases. For this, 10 ng of parasite lysate was allowed to pre-incubate in the reaction buffer with 100 μM of the test compound in the presence and absence of calcium. Once the reactions were complete, the ADP-Glo™ Kinase Assay was performed as described in methods section. MCR 03 significantly exhibited differential inhibition in the presence and absence of calcium. Percent activity represent the mean of two replicates.

    Journal: MethodsX

    Article Title: Screening of chemical library against whole cell kinome activity via non-radioactive, high throughput kinase assay

    doi: 10.1016/j.mex.2018.12.003

    Figure Lengend Snippet: Applications of ADP-Glo™ kinase assay with parasite lysate . Panel A . To Elucidate proportion of calcium-dependent protein kinases in the parasite kinome, kinase reaction was performed using 10 ng of parasite lysate in the presence and absence of 2.5 mM Ca 2+ , as described in methods section. ˜30% of kinome activity has been reported to impart largely because of calcium-dependent protein kinases. Panel B . To check if the assay can be applied for HTS, thio-oxo-imidazolidinone derivative, MCR03 was tested for any effect on the activity of kinases. For this, 10 ng of parasite lysate was allowed to pre-incubate in the reaction buffer with 100 μM of the test compound in the presence and absence of calcium. Once the reactions were complete, the ADP-Glo™ Kinase Assay was performed as described in methods section. MCR 03 significantly exhibited differential inhibition in the presence and absence of calcium. Percent activity represent the mean of two replicates.

    Article Snippet: The composition for measuring functional activity of the parasite kinome involves ATP regeneration-based luciferase reaction system resulting from nascent ADP phosphorylation by utilizing ADP-Glo™ kinase assay kit (Promega Corporation, catalog no. V9101).

    Techniques: Kinase Assay, Activity Assay, Inhibition

    The kinase activities of GST fusion proteins were measured in vitro . A. Phosphorylation activities of GST fusion proteins containing full-length Stk (using plasmid pQG77), Stk 1–263 (pQG78) or Stk 40–263 (pQG79) were measured with a Kinase-Glo™ luminescent kinase assay in vitro at 32°C for 4 h. B. Phosphorylation activities of GST fusion proteins containing full-length Stk (using plasmid pQG77) were measured with a Kinase-Glo™ luminescent kinase assay with or without staurosporine in vitro at 32°C for 4 h. GST was used as a negative control. RLU, relative luminescent unit. Data are derived from three independent experiments, **, P

    Journal: PLoS ONE

    Article Title: The Eukaryotic-Type Serine/Threonine Protein Kinase Stk Is Required for Biofilm Formation and Virulence in Staphylococcus epidermidis

    doi: 10.1371/journal.pone.0025380

    Figure Lengend Snippet: The kinase activities of GST fusion proteins were measured in vitro . A. Phosphorylation activities of GST fusion proteins containing full-length Stk (using plasmid pQG77), Stk 1–263 (pQG78) or Stk 40–263 (pQG79) were measured with a Kinase-Glo™ luminescent kinase assay in vitro at 32°C for 4 h. B. Phosphorylation activities of GST fusion proteins containing full-length Stk (using plasmid pQG77) were measured with a Kinase-Glo™ luminescent kinase assay with or without staurosporine in vitro at 32°C for 4 h. GST was used as a negative control. RLU, relative luminescent unit. Data are derived from three independent experiments, **, P

    Article Snippet: In vitro kinase assay For the in vitro kinase assay, 2 µg of WT Stk, Stk1–263 or Stk40–263 and 1 µg histone 1 (H1) were incubated separately in 50 µl kinase buffer (50 mM Tris-HCl [pH 7.5], 100 µM dithiothreitol [DTT], 1 mM MnCl2 , 100 µM ATP) for 4 h at 32°C Kinase activity was assayed using a Kinase-Glo™ Luminescent Kinase Assay kit (Promega) and the luminescent signal reflecting the ATP level in the reaction system was measured in a Victor 3 plate reader.

    Techniques: In Vitro, Plasmid Preparation, Kinase Assay, Negative Control, Derivative Assay