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luminescence reagent steadyglo  (Promega)

 
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    Promega luminescence reagent steadyglo
    Luminescence Reagent Steadyglo, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/luminescence+reagent+steadyglo/steadyglo+luminescence+reagent/pmc11409196-223-15-18
    Average 90 stars, based on 1 article reviews
    luminescence reagent steadyglo - by Bioz Stars, 2026-09
    90/100 stars

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    Incubation:

    Article Title: O‐ GlcNAc modification of HSP27 alters its protein interactions and promotes refolding of proteins through the BAG3 / HSP70 co‐chaperone
    Article Snippet: .. The refolding reactions were incubated in a white, 96‐well plate for 1 h at 37°C, SteadyGlo luminescence reagent (Promega) was added to each well, and luminescence was measured on a SpectraMax M5 plate reader. ..



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    luminescence reagent steadyglo  (Promega)
    90
    Promega luminescence reagent steadyglo
    Luminescence Reagent Steadyglo, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/luminescence+reagent+steadyglo/steadyglo+luminescence+reagent/pmc11409196-223-15-18
    Average 90 stars, based on 1 article reviews
    luminescence reagent steadyglo - by Bioz Stars, 2026-09
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    steadyglo luminescence reagent  (Promega)
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    Promega steadyglo luminescence reagent
    Mutations in the EEVD motif reduce collaboration between Hsp72 and DnaJB4. A , ATP hydrolysis assay comparing the turnover rate of Hsp72 WT and mutants in the presence of DnaJB4, as measured by malachite green assay. The left graph shows mean intrinsic ATPase rate ±SD (n = 3) of the various Hsp72 mutants. The right graph shows mean ATPase rate ±SD (n = 3) of the various Hsp72 mutants in the presence of increasing concentrations of DnaJB4. Curves were fit according to Michaelis–Menten kinetics at steady state. Statistics were performed using unpaired Student’s t test (∗ p < 0.05, ns, not significant). B , luciferase refolding assay comparing WT and mutant Hsp72 in the presence of DnaJB4. Refolding was measured by <t>SteadyGlo</t> luciferase reagent (see the ). The graph shows mean percent luciferase refolded relative to nondenatured luciferase control ±SD (n = 3). C , luciferase refolding assay comparing WT and I637A mutant Hsp72 in the presence of DnaJB4 or DnaJA2. The graph shows mean percent luciferase refolded relative to nondenatured luciferase control ±SD (n = 3).
    Steadyglo Luminescence Reagent, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/luminescence+reagent+steadyglo/steadyglo+luminescence+reagent/pmc08913300-314-5-8
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    steadyglo luminescence reagent - by Bioz Stars, 2026-09
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    the steadyglo luminescence reagent  (Promega)
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    Promega the steadyglo luminescence reagent
    Mutations in the EEVD motif reduce collaboration between Hsp72 and DnaJB4. A , ATP hydrolysis assay comparing the turnover rate of Hsp72 WT and mutants in the presence of DnaJB4, as measured by malachite green assay. The left graph shows mean intrinsic ATPase rate ±SD (n = 3) of the various Hsp72 mutants. The right graph shows mean ATPase rate ±SD (n = 3) of the various Hsp72 mutants in the presence of increasing concentrations of DnaJB4. Curves were fit according to Michaelis–Menten kinetics at steady state. Statistics were performed using unpaired Student’s t test (∗ p < 0.05, ns, not significant). B , luciferase refolding assay comparing WT and mutant Hsp72 in the presence of DnaJB4. Refolding was measured by <t>SteadyGlo</t> luciferase reagent (see the ). The graph shows mean percent luciferase refolded relative to nondenatured luciferase control ±SD (n = 3). C , luciferase refolding assay comparing WT and I637A mutant Hsp72 in the presence of DnaJB4 or DnaJA2. The graph shows mean percent luciferase refolded relative to nondenatured luciferase control ±SD (n = 3).
    The Steadyglo Luminescence Reagent, supplied by Promega, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/luminescence+reagent+steadyglo/steadyglo+luminescence+reagent/us11059826-4571-17-20
    Average 90 stars, based on 1 article reviews
    the steadyglo luminescence reagent - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Mutations in the EEVD motif reduce collaboration between Hsp72 and DnaJB4. A , ATP hydrolysis assay comparing the turnover rate of Hsp72 WT and mutants in the presence of DnaJB4, as measured by malachite green assay. The left graph shows mean intrinsic ATPase rate ±SD (n = 3) of the various Hsp72 mutants. The right graph shows mean ATPase rate ±SD (n = 3) of the various Hsp72 mutants in the presence of increasing concentrations of DnaJB4. Curves were fit according to Michaelis–Menten kinetics at steady state. Statistics were performed using unpaired Student’s t test (∗ p < 0.05, ns, not significant). B , luciferase refolding assay comparing WT and mutant Hsp72 in the presence of DnaJB4. Refolding was measured by SteadyGlo luciferase reagent (see the ). The graph shows mean percent luciferase refolded relative to nondenatured luciferase control ±SD (n = 3). C , luciferase refolding assay comparing WT and I637A mutant Hsp72 in the presence of DnaJB4 or DnaJA2. The graph shows mean percent luciferase refolded relative to nondenatured luciferase control ±SD (n = 3).

    Journal: The Journal of Biological Chemistry

    Article Title: Two distinct classes of cochaperones compete for the EEVD motif in heat shock protein 70 to tune its chaperone activities

    doi: 10.1016/j.jbc.2022.101697

    Figure Lengend Snippet: Mutations in the EEVD motif reduce collaboration between Hsp72 and DnaJB4. A , ATP hydrolysis assay comparing the turnover rate of Hsp72 WT and mutants in the presence of DnaJB4, as measured by malachite green assay. The left graph shows mean intrinsic ATPase rate ±SD (n = 3) of the various Hsp72 mutants. The right graph shows mean ATPase rate ±SD (n = 3) of the various Hsp72 mutants in the presence of increasing concentrations of DnaJB4. Curves were fit according to Michaelis–Menten kinetics at steady state. Statistics were performed using unpaired Student’s t test (∗ p < 0.05, ns, not significant). B , luciferase refolding assay comparing WT and mutant Hsp72 in the presence of DnaJB4. Refolding was measured by SteadyGlo luciferase reagent (see the ). The graph shows mean percent luciferase refolded relative to nondenatured luciferase control ±SD (n = 3). C , luciferase refolding assay comparing WT and I637A mutant Hsp72 in the presence of DnaJB4 or DnaJA2. The graph shows mean percent luciferase refolded relative to nondenatured luciferase control ±SD (n = 3).

    Article Snippet: Luminescence was measured using the SteadyGlo luminescence reagent (Promega), and percent refolded luciferase was calculated using a standard curve of 100 to 0 nM native luciferase.

    Techniques: Hydrolysis Assay, Malachite Green Assay, Luciferase, Mutagenesis, Control