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coomassie brilliant blue g 250  (Valiant Co Ltd)

 
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    Structured Review

    Valiant Co Ltd coomassie brilliant blue g 250
    Coomassie Brilliant Blue G 250, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 96/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/0219034305/Coomassie+Brilliant+Blue+G-250/10__1134_slash_s000629792312012x-45-43-50
    Average 96 stars, based on 51 article reviews
    coomassie brilliant blue g 250 - by Bioz Stars, 2026-09
    96/100 stars

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    Related Articles

    Bradford Assay:

    Article Title: Prediction of Nanoparticle Photoreactivity in Mixtures of Surface Foulants Requires Kinetic (Non-equilibrium) Adsorption Considerations.
    Article Snippet: The adsorption of foulants on photocatalytic nanoparticles can suppress their reactivity in water treatment applications by scavenging reactive species at the photocatalyst surface, screening light, or competing for surface sites.. These inhibitory effects are commonly modeled using the Langmuir− Hinshelwood model, assuming that adsorbed layer compositions follow Langmuirian (equilibrium) competitive adsorption.. However, this assumption has not been evaluated in complex mixtures of foulants.

    Electrophoresis:

    Article Title: The Effect of Pomegranate Peel Extract on the Oxidative and Inflammatory Status in the Spleens of Rats with Metabolic Syndrome.
    Article Snippet: Electrophoresis was performed in Mini-Protean II (BioRad, Hercules, CA, USA). .. After electrophoresis, the gels were washed three times with 2,5 % Triton X-100 to remove SDS and then incubated with an enzyme assay buffer (0.05 M Tris-HCl, pH 7.5 containing 5 mM CaCl2, 0.2 M NaCl, 0.05% NaN3) at 37◦C for 18 h. After incubation, the gels were stained with 0.3% CBB R-250 (MP Biomedicals, Illkirch-Graffenstaden, France) mixed with 0.2% CBB G-250 (MP Biomedicals, Illkirch-Graffenstaden, France) and then destained until white bands were visible on a blue background. .. To measure MMP activity, zymograms were scanned with a densitometer (BioRad G5-800, Hercules, CA, USA) and analyzed using Quantity One software v. 4.6.9 (BioRad, Hercules, CA, USA).

    Article Title: Reduced Protein Import via TIM23 SORT Drives Disease Pathology in TIMM50-Associated Mitochondrial Disease.
    Article Snippet: .. Following clarification by centrifugation, supernatants were combined with blue native loading dye (0.5% [wt/vol] Coomassie blue G-250 (MP Biomedicals), 50 mM a-amino n-caproic acid, 10 mM Bis-Tris pH 7.0) and loaded onto 4–16% acrylamide gradient gels as previously described.48 Electrophoresis was carried out at 4 �C overnight with anode buffer (50 mM Bis-Tris pH 7.0) and cathode buffer (50 mM tricine, 15 mM Bis-Tris, 0.02% [wt/vol] Coomassie blue G250). ..

    Incubation:

    Article Title: The Effect of Pomegranate Peel Extract on the Oxidative and Inflammatory Status in the Spleens of Rats with Metabolic Syndrome.
    Article Snippet: Electrophoresis was performed in Mini-Protean II (BioRad, Hercules, CA, USA). .. After electrophoresis, the gels were washed three times with 2,5 % Triton X-100 to remove SDS and then incubated with an enzyme assay buffer (0.05 M Tris-HCl, pH 7.5 containing 5 mM CaCl2, 0.2 M NaCl, 0.05% NaN3) at 37◦C for 18 h. After incubation, the gels were stained with 0.3% CBB R-250 (MP Biomedicals, Illkirch-Graffenstaden, France) mixed with 0.2% CBB G-250 (MP Biomedicals, Illkirch-Graffenstaden, France) and then destained until white bands were visible on a blue background. .. To measure MMP activity, zymograms were scanned with a densitometer (BioRad G5-800, Hercules, CA, USA) and analyzed using Quantity One software v. 4.6.9 (BioRad, Hercules, CA, USA).

    Enzymatic Assay:

    Article Title: The Effect of Pomegranate Peel Extract on the Oxidative and Inflammatory Status in the Spleens of Rats with Metabolic Syndrome.
    Article Snippet: Electrophoresis was performed in Mini-Protean II (BioRad, Hercules, CA, USA). .. After electrophoresis, the gels were washed three times with 2,5 % Triton X-100 to remove SDS and then incubated with an enzyme assay buffer (0.05 M Tris-HCl, pH 7.5 containing 5 mM CaCl2, 0.2 M NaCl, 0.05% NaN3) at 37◦C for 18 h. After incubation, the gels were stained with 0.3% CBB R-250 (MP Biomedicals, Illkirch-Graffenstaden, France) mixed with 0.2% CBB G-250 (MP Biomedicals, Illkirch-Graffenstaden, France) and then destained until white bands were visible on a blue background. .. To measure MMP activity, zymograms were scanned with a densitometer (BioRad G5-800, Hercules, CA, USA) and analyzed using Quantity One software v. 4.6.9 (BioRad, Hercules, CA, USA).

    Staining:

    Article Title: The Effect of Pomegranate Peel Extract on the Oxidative and Inflammatory Status in the Spleens of Rats with Metabolic Syndrome.
    Article Snippet: Electrophoresis was performed in Mini-Protean II (BioRad, Hercules, CA, USA). .. After electrophoresis, the gels were washed three times with 2,5 % Triton X-100 to remove SDS and then incubated with an enzyme assay buffer (0.05 M Tris-HCl, pH 7.5 containing 5 mM CaCl2, 0.2 M NaCl, 0.05% NaN3) at 37◦C for 18 h. After incubation, the gels were stained with 0.3% CBB R-250 (MP Biomedicals, Illkirch-Graffenstaden, France) mixed with 0.2% CBB G-250 (MP Biomedicals, Illkirch-Graffenstaden, France) and then destained until white bands were visible on a blue background. .. To measure MMP activity, zymograms were scanned with a densitometer (BioRad G5-800, Hercules, CA, USA) and analyzed using Quantity One software v. 4.6.9 (BioRad, Hercules, CA, USA).

    Article Title: Escherichia coli proteins uL29 and ACP stabilize the Tn7-encoded TnsD and its DNA binding
    Article Snippet: .. Gels were stained with Coomassie Brilliant Blue (G-250, MP Biomedicals) for 20 minutes and destained overnight before imaging using a GelDoc Go imager system (BioRad). ..

    Article Title: Escherichia coli proteins uL29 and ACP stabilize the Tn7-encoded TnsD and its DNA binding
    Article Snippet: .. Gels were stained with Coomassie Brilliant Blue (G-250, MP Biomedicals) for 20 min and destained overnight before imaging using a GelDoc Go imager system (BioRad). ..

    Imaging:

    Article Title: Escherichia coli proteins uL29 and ACP stabilize the Tn7-encoded TnsD and its DNA binding
    Article Snippet: .. Gels were stained with Coomassie Brilliant Blue (G-250, MP Biomedicals) for 20 minutes and destained overnight before imaging using a GelDoc Go imager system (BioRad). ..

    Article Title: Escherichia coli proteins uL29 and ACP stabilize the Tn7-encoded TnsD and its DNA binding
    Article Snippet: .. Gels were stained with Coomassie Brilliant Blue (G-250, MP Biomedicals) for 20 min and destained overnight before imaging using a GelDoc Go imager system (BioRad). ..

    Clarification Assay:

    Article Title: Reduced Protein Import via TIM23 SORT Drives Disease Pathology in TIMM50-Associated Mitochondrial Disease.
    Article Snippet: .. Following clarification by centrifugation, supernatants were combined with blue native loading dye (0.5% [wt/vol] Coomassie blue G-250 (MP Biomedicals), 50 mM a-amino n-caproic acid, 10 mM Bis-Tris pH 7.0) and loaded onto 4–16% acrylamide gradient gels as previously described.48 Electrophoresis was carried out at 4 �C overnight with anode buffer (50 mM Bis-Tris pH 7.0) and cathode buffer (50 mM tricine, 15 mM Bis-Tris, 0.02% [wt/vol] Coomassie blue G250). ..

    Article Title: Reduced Protein Import via TIM23 SORT Drives Disease Pathology in TIMM50-Associated Mitochondrial Disease
    Article Snippet: .. Following clarification by centrifugation, supernatants were combined with blue native loading dye (0.5% [wt/vol] Coomassie blue G-250 (MP Biomedicals), 50 mM α-amino n-caproic acid, 10 mM Bis-Tris pH 7.0) and loaded onto 4–16% acrylamide gradient gels as previously described. ..

    Centrifugation:

    Article Title: Reduced Protein Import via TIM23 SORT Drives Disease Pathology in TIMM50-Associated Mitochondrial Disease.
    Article Snippet: .. Following clarification by centrifugation, supernatants were combined with blue native loading dye (0.5% [wt/vol] Coomassie blue G-250 (MP Biomedicals), 50 mM a-amino n-caproic acid, 10 mM Bis-Tris pH 7.0) and loaded onto 4–16% acrylamide gradient gels as previously described.48 Electrophoresis was carried out at 4 �C overnight with anode buffer (50 mM Bis-Tris pH 7.0) and cathode buffer (50 mM tricine, 15 mM Bis-Tris, 0.02% [wt/vol] Coomassie blue G250). ..

    Article Title: Reduced Protein Import via TIM23 SORT Drives Disease Pathology in TIMM50-Associated Mitochondrial Disease
    Article Snippet: .. Following clarification by centrifugation, supernatants were combined with blue native loading dye (0.5% [wt/vol] Coomassie blue G-250 (MP Biomedicals), 50 mM α-amino n-caproic acid, 10 mM Bis-Tris pH 7.0) and loaded onto 4–16% acrylamide gradient gels as previously described. ..



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    The C-terminal region of TnsD mediates DNA-binding specificity. ( a ) Domain architecture of TnsD from the prototypical Tn7 element. ( b ) <t>Coomassie-stained</t> SDS-polyacrylamide gels showing the solubilized TnsD fraction from the cell lysate, the purification steps on Ni-affinity beads (unbound fraction, washes with 30 mM imidazole, elution with 300 mM imidazole), and subsequent purification over a heparin column. ( c ) Representative electrophoretic mobility shift assays (EMSAs) with increasing concentrations of protein showing DNA binding specificity of TnsD (top) or TnsD NTD (bottom) towards the region + 23 to + 58 of attTn7 (10 nM, lanes 1–5) or a control dsDNA (10 nM, lanes 6–10). ( d ) DNA-binding quantification at a protein concentration of 40 nM. Error bars indicate standard deviation ( n = 3).
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    Image Search Results


    The C-terminal region of TnsD mediates DNA-binding specificity. ( a ) Domain architecture of TnsD from the prototypical Tn7 element. ( b ) Coomassie-stained SDS-polyacrylamide gels showing the solubilized TnsD fraction from the cell lysate, the purification steps on Ni-affinity beads (unbound fraction, washes with 30 mM imidazole, elution with 300 mM imidazole), and subsequent purification over a heparin column. ( c ) Representative electrophoretic mobility shift assays (EMSAs) with increasing concentrations of protein showing DNA binding specificity of TnsD (top) or TnsD NTD (bottom) towards the region + 23 to + 58 of attTn7 (10 nM, lanes 1–5) or a control dsDNA (10 nM, lanes 6–10). ( d ) DNA-binding quantification at a protein concentration of 40 nM. Error bars indicate standard deviation ( n = 3).

    Journal: Mobile DNA

    Article Title: Escherichia coli proteins uL29 and ACP stabilize the Tn7-encoded TnsD and its DNA binding

    doi: 10.1186/s13100-025-00369-6

    Figure Lengend Snippet: The C-terminal region of TnsD mediates DNA-binding specificity. ( a ) Domain architecture of TnsD from the prototypical Tn7 element. ( b ) Coomassie-stained SDS-polyacrylamide gels showing the solubilized TnsD fraction from the cell lysate, the purification steps on Ni-affinity beads (unbound fraction, washes with 30 mM imidazole, elution with 300 mM imidazole), and subsequent purification over a heparin column. ( c ) Representative electrophoretic mobility shift assays (EMSAs) with increasing concentrations of protein showing DNA binding specificity of TnsD (top) or TnsD NTD (bottom) towards the region + 23 to + 58 of attTn7 (10 nM, lanes 1–5) or a control dsDNA (10 nM, lanes 6–10). ( d ) DNA-binding quantification at a protein concentration of 40 nM. Error bars indicate standard deviation ( n = 3).

    Article Snippet: Gels were stained with Coomassie Brilliant Blue (G-250, MP Biomedicals) for 20 min and destained overnight before imaging using a GelDoc Go imager system (BioRad).

    Techniques: Binding Assay, Staining, Purification, Electrophoretic Mobility Shift Assay, Control, Protein Concentration, Standard Deviation

    ACP and uL29 bind to the TnsD: attTn7 complex. ( a ) Coomassie-stained SDS-polyacrylamide gel showing purified uL29, holo- and apo-ACP. ( b ) EMSA showing how the binding of TnsD (20 nM) to the region + 23 to + 58 of attTn7 (10nM) is affected by the presence of apo ACP (lane 3), holo ACP (lane 4), uL29 (lane 5) or both host factors combined (lanes 6–7). ( c ) EMSA of TnsD (40 nM, lane 3) bound to attTn7 (10 nM) with increasing concentrations of equimolar mixtures of uL29:apo-ACP (20–320 nM, lanes 4–8). ( d ) EMSA showing how the binding of TnsD NTD (20 nM) to the region + 23 to + 58 of attTn7 (10nM) is not affected by the presence of host factors as in (b)

    Journal: Mobile DNA

    Article Title: Escherichia coli proteins uL29 and ACP stabilize the Tn7-encoded TnsD and its DNA binding

    doi: 10.1186/s13100-025-00369-6

    Figure Lengend Snippet: ACP and uL29 bind to the TnsD: attTn7 complex. ( a ) Coomassie-stained SDS-polyacrylamide gel showing purified uL29, holo- and apo-ACP. ( b ) EMSA showing how the binding of TnsD (20 nM) to the region + 23 to + 58 of attTn7 (10nM) is affected by the presence of apo ACP (lane 3), holo ACP (lane 4), uL29 (lane 5) or both host factors combined (lanes 6–7). ( c ) EMSA of TnsD (40 nM, lane 3) bound to attTn7 (10 nM) with increasing concentrations of equimolar mixtures of uL29:apo-ACP (20–320 nM, lanes 4–8). ( d ) EMSA showing how the binding of TnsD NTD (20 nM) to the region + 23 to + 58 of attTn7 (10nM) is not affected by the presence of host factors as in (b)

    Article Snippet: Gels were stained with Coomassie Brilliant Blue (G-250, MP Biomedicals) for 20 min and destained overnight before imaging using a GelDoc Go imager system (BioRad).

    Techniques: Staining, Purification, Binding Assay

    uL29 and ACP interact with the C-terminal domain of TnsD. ( a ) Coomassie-stained native polyacrylamide gel of uL29 (lane 1), apo-ACP (lane 2), holo-ACP (lane 3), and TnsD (lane 4) on their own or mixed (lanes 5–8) to monitor complex formation. ( b ) Coomassie-stained SDS-polyacrylamide gel showing the amount of soluble TnsD before (diluted), during (intermediate) and after (concentrated) concentration with a 30 kDa MWCO concentrator on its own (lanes 2-4) or when supplemented with excess apo-ACP and uL29 (lanes 5-7). Both host factors are enriched in the concentrated fraction but uL29 is only visible when the gel is silver-stained (inset). Molecular weight markers are indicated in kDa. ( c ) AlphaFold2 prediction showing that the interaction between TnsD, uL29 and ACP occurs through the extreme C-terminal region of TnsD (see also Figure S3). ( d ) Detail of the TnsD: uL29:ACP interaction showing that it is primarily mediated by electrostatic interactions. On the left panel, the C-terminal region of TnsD (residues 389–508) is shown as an electrostatic surface (red indicates negatively charge and blue positively charged) with ACP (purple) and uL29 (pink) shown as cartoon representations. Reciprocally, on the right panel ACP and uL29 are shown as electrostatic surfaces, with TnsD shown as a cartoon (light blue)

    Journal: Mobile DNA

    Article Title: Escherichia coli proteins uL29 and ACP stabilize the Tn7-encoded TnsD and its DNA binding

    doi: 10.1186/s13100-025-00369-6

    Figure Lengend Snippet: uL29 and ACP interact with the C-terminal domain of TnsD. ( a ) Coomassie-stained native polyacrylamide gel of uL29 (lane 1), apo-ACP (lane 2), holo-ACP (lane 3), and TnsD (lane 4) on their own or mixed (lanes 5–8) to monitor complex formation. ( b ) Coomassie-stained SDS-polyacrylamide gel showing the amount of soluble TnsD before (diluted), during (intermediate) and after (concentrated) concentration with a 30 kDa MWCO concentrator on its own (lanes 2-4) or when supplemented with excess apo-ACP and uL29 (lanes 5-7). Both host factors are enriched in the concentrated fraction but uL29 is only visible when the gel is silver-stained (inset). Molecular weight markers are indicated in kDa. ( c ) AlphaFold2 prediction showing that the interaction between TnsD, uL29 and ACP occurs through the extreme C-terminal region of TnsD (see also Figure S3). ( d ) Detail of the TnsD: uL29:ACP interaction showing that it is primarily mediated by electrostatic interactions. On the left panel, the C-terminal region of TnsD (residues 389–508) is shown as an electrostatic surface (red indicates negatively charge and blue positively charged) with ACP (purple) and uL29 (pink) shown as cartoon representations. Reciprocally, on the right panel ACP and uL29 are shown as electrostatic surfaces, with TnsD shown as a cartoon (light blue)

    Article Snippet: Gels were stained with Coomassie Brilliant Blue (G-250, MP Biomedicals) for 20 min and destained overnight before imaging using a GelDoc Go imager system (BioRad).

    Techniques: Staining, Concentration Assay, Molecular Weight

    Helix a2 in ACP mediates the interaction with uL29 and TnsD. ( a ) Detail view of the AlphaFold model of showing helix a2 from ACP (purple) cradled by Arg397, Arg401 and Arg405 from TnsD (light blue) on one side of the helix, and Arg450, Tyr451 and Lys408 from TnsD, and Lys44 and Arg48 from uL29 (light pink) on the other side. Side chains are shown as color-coded sticks and labeled. ( b ) Coomassie-stained native gel showing the interaction between uL29 and the different ACP variants as indicated. All proteins were used at 25 µM. (c-d) EMSA showing how the binding of TnsD (40 nM) to the region + 23 to + 58 of attTn7 (10 nM) is affected by the presence of apo-ACP D39R/E42A ( c ) or holo- ACP D39R/E42A ( d ). Host factors were added as equimolar uL29:ACP mixtures (20–320 nM)

    Journal: Mobile DNA

    Article Title: Escherichia coli proteins uL29 and ACP stabilize the Tn7-encoded TnsD and its DNA binding

    doi: 10.1186/s13100-025-00369-6

    Figure Lengend Snippet: Helix a2 in ACP mediates the interaction with uL29 and TnsD. ( a ) Detail view of the AlphaFold model of showing helix a2 from ACP (purple) cradled by Arg397, Arg401 and Arg405 from TnsD (light blue) on one side of the helix, and Arg450, Tyr451 and Lys408 from TnsD, and Lys44 and Arg48 from uL29 (light pink) on the other side. Side chains are shown as color-coded sticks and labeled. ( b ) Coomassie-stained native gel showing the interaction between uL29 and the different ACP variants as indicated. All proteins were used at 25 µM. (c-d) EMSA showing how the binding of TnsD (40 nM) to the region + 23 to + 58 of attTn7 (10 nM) is affected by the presence of apo-ACP D39R/E42A ( c ) or holo- ACP D39R/E42A ( d ). Host factors were added as equimolar uL29:ACP mixtures (20–320 nM)

    Article Snippet: Gels were stained with Coomassie Brilliant Blue (G-250, MP Biomedicals) for 20 min and destained overnight before imaging using a GelDoc Go imager system (BioRad).

    Techniques: Labeling, Staining, Binding Assay