Structured Review

Fisher Scientific coomassie blue
Effect of site-specific phosphorylation on biochemical characteristics of Pfn1. A) Pull-down assays of indicated GST-tagged Pfn1 constructs with HEK-293 cell lysate were run on an SDS-PAGE and immunoblotted with anti-actin and anti-VASP antibodies (GST was used as a negative control). <t>Coomassie</t> stain in parallel confirms comparable amounts of GST-tagged proteins in the pull-down assay. Note that virtually negligible amount of T89D-Pfn1 was found to be immobilized on glutathione-linked agarose beads. B) Bacteria expressing indicated GST-tagged Pfn1 constructs were lysed with either non-denaturing (containing 1% NP-40) or denaturing (containing 1% NP-40, 2% SDS for one buffer and the other with 6M urea in addition) extraction buffers. Bacterial lysates were immunoblotted with anti-Pfn1 antibody to demonstrate that T89D-Pfn1 is insoluble in non-denaturing lysis buffer. C) HEK-293 cells expressing indicated EGFP-fused Pfn1 constructs were lysed with either non-denaturing (containing 1% NP-40) or denaturing (containing 1% NP-40, 2% SDS for one buffer and the other with 6M urea in addition) extraction buffers. HEK-293 lysates were immunoblotted with anti-GFP antibody to demonstrate that GFP-T89D-Pfn1 is also insoluble in non-denaturing lysis buffer. Note that endogenous Pfn1 level is not affected by expression of any of the ectopic Pfn1 constructs and extractable completely in non-denaturing lysis buffer. D) Fluorescence images of HEK-293 cells expressing indicated EGFP-fused Pfn1 constructs show that EGFP-Pfn1-T89D causes clustering of this fusion protein as indicated by the arrows. Scale bar represents 20 μm. E) HEK-293 cells expressing indicated EGFP-fused Pfn1 constructs were treated with CHX for up to 8 hours. Cell lysates prepared at different time-points after CHX addition were immunoblotted with the indicated antibodies. T89D-Pfn1 undergoes rapid protein degradation while WT- and T89A-Pfn1 are stable over that period of time, similar to the characteristic of endogenous Pfn1 (degradation of p27kip1, a cell-cycle protein that undergoes rapid turnover, validates CHX efficacy). Tubulin blot serves as the loading control. F) The bar graph summarizes quantification of the time-dependent changes in the expression of the indicated GFP-Pfn1 constructs following CHX treatment in HEK-293. Data was summarized from 3 independent experiments (** indicates p
Coomassie Blue, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 93/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/coomassie blue/product/Fisher Scientific
Average 93 stars, based on 20 article reviews
Price from $9.99 to $1999.99
coomassie blue - by Bioz Stars, 2020-08
93/100 stars

Images

1) Product Images from "Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A"

Article Title: Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A

Journal: PLoS ONE

doi: 10.1371/journal.pone.0156313

Effect of site-specific phosphorylation on biochemical characteristics of Pfn1. A) Pull-down assays of indicated GST-tagged Pfn1 constructs with HEK-293 cell lysate were run on an SDS-PAGE and immunoblotted with anti-actin and anti-VASP antibodies (GST was used as a negative control). Coomassie stain in parallel confirms comparable amounts of GST-tagged proteins in the pull-down assay. Note that virtually negligible amount of T89D-Pfn1 was found to be immobilized on glutathione-linked agarose beads. B) Bacteria expressing indicated GST-tagged Pfn1 constructs were lysed with either non-denaturing (containing 1% NP-40) or denaturing (containing 1% NP-40, 2% SDS for one buffer and the other with 6M urea in addition) extraction buffers. Bacterial lysates were immunoblotted with anti-Pfn1 antibody to demonstrate that T89D-Pfn1 is insoluble in non-denaturing lysis buffer. C) HEK-293 cells expressing indicated EGFP-fused Pfn1 constructs were lysed with either non-denaturing (containing 1% NP-40) or denaturing (containing 1% NP-40, 2% SDS for one buffer and the other with 6M urea in addition) extraction buffers. HEK-293 lysates were immunoblotted with anti-GFP antibody to demonstrate that GFP-T89D-Pfn1 is also insoluble in non-denaturing lysis buffer. Note that endogenous Pfn1 level is not affected by expression of any of the ectopic Pfn1 constructs and extractable completely in non-denaturing lysis buffer. D) Fluorescence images of HEK-293 cells expressing indicated EGFP-fused Pfn1 constructs show that EGFP-Pfn1-T89D causes clustering of this fusion protein as indicated by the arrows. Scale bar represents 20 μm. E) HEK-293 cells expressing indicated EGFP-fused Pfn1 constructs were treated with CHX for up to 8 hours. Cell lysates prepared at different time-points after CHX addition were immunoblotted with the indicated antibodies. T89D-Pfn1 undergoes rapid protein degradation while WT- and T89A-Pfn1 are stable over that period of time, similar to the characteristic of endogenous Pfn1 (degradation of p27kip1, a cell-cycle protein that undergoes rapid turnover, validates CHX efficacy). Tubulin blot serves as the loading control. F) The bar graph summarizes quantification of the time-dependent changes in the expression of the indicated GFP-Pfn1 constructs following CHX treatment in HEK-293. Data was summarized from 3 independent experiments (** indicates p
Figure Legend Snippet: Effect of site-specific phosphorylation on biochemical characteristics of Pfn1. A) Pull-down assays of indicated GST-tagged Pfn1 constructs with HEK-293 cell lysate were run on an SDS-PAGE and immunoblotted with anti-actin and anti-VASP antibodies (GST was used as a negative control). Coomassie stain in parallel confirms comparable amounts of GST-tagged proteins in the pull-down assay. Note that virtually negligible amount of T89D-Pfn1 was found to be immobilized on glutathione-linked agarose beads. B) Bacteria expressing indicated GST-tagged Pfn1 constructs were lysed with either non-denaturing (containing 1% NP-40) or denaturing (containing 1% NP-40, 2% SDS for one buffer and the other with 6M urea in addition) extraction buffers. Bacterial lysates were immunoblotted with anti-Pfn1 antibody to demonstrate that T89D-Pfn1 is insoluble in non-denaturing lysis buffer. C) HEK-293 cells expressing indicated EGFP-fused Pfn1 constructs were lysed with either non-denaturing (containing 1% NP-40) or denaturing (containing 1% NP-40, 2% SDS for one buffer and the other with 6M urea in addition) extraction buffers. HEK-293 lysates were immunoblotted with anti-GFP antibody to demonstrate that GFP-T89D-Pfn1 is also insoluble in non-denaturing lysis buffer. Note that endogenous Pfn1 level is not affected by expression of any of the ectopic Pfn1 constructs and extractable completely in non-denaturing lysis buffer. D) Fluorescence images of HEK-293 cells expressing indicated EGFP-fused Pfn1 constructs show that EGFP-Pfn1-T89D causes clustering of this fusion protein as indicated by the arrows. Scale bar represents 20 μm. E) HEK-293 cells expressing indicated EGFP-fused Pfn1 constructs were treated with CHX for up to 8 hours. Cell lysates prepared at different time-points after CHX addition were immunoblotted with the indicated antibodies. T89D-Pfn1 undergoes rapid protein degradation while WT- and T89A-Pfn1 are stable over that period of time, similar to the characteristic of endogenous Pfn1 (degradation of p27kip1, a cell-cycle protein that undergoes rapid turnover, validates CHX efficacy). Tubulin blot serves as the loading control. F) The bar graph summarizes quantification of the time-dependent changes in the expression of the indicated GFP-Pfn1 constructs following CHX treatment in HEK-293. Data was summarized from 3 independent experiments (** indicates p

Techniques Used: Construct, SDS Page, Negative Control, Staining, Pull Down Assay, Expressing, Lysis, Fluorescence

Related Articles

Electrophoresis:

Article Title: De Novo Isolation Affinity Maturation of yeast-displayed Virion-binding human fibronectin domains by flow cytometric screening against Virions
Article Snippet: .. Gels were stained with Coomassie Blue (Fisher Scientific) following electrophoresis. .. Native PAGE analysis was carried out using 3% stacking/12% resolving Bis-Tris gels with the 0.5–1.0 μg of purified Fn3 noted above loaded into each well.

Article Title: De Novo Isolation Affinity Maturation of yeast-displayed Virion-binding human fibronectin domains by flow cytometric screening against Virions
Article Snippet: .. Two electrophoresis intervals were carried out, an initial 15-min interval at 100 V followed by a 55-min interval at 200 V. Gels were stained with Coomassie Blue following electrophoresis. .. ELISA detection of soluble Fn3s binding to Zika Virions For assays measuring binding of immobilized Fn3s to Zika virions, purified, desalted Fn3s were diluted to 8 μg/mL in pH 7.4 PBS and adsorbed onto MaxiSorp 96-well plates (BioLegend) by overnight incubation of 100 μL of Fn3-containing solution at 4 °C.

Staining:

Article Title: Estradiol Dose-Dependent Regulation of Membrane Estrogen Receptor-α, Metabotropic Glutamate Receptor-1a, and Their Complexes in the Arcuate Nucleus of the Hypothalamus in Female Rats
Article Snippet: .. Successful transfer of protein to the membranes was confirmed using a removable Ponceau S staining solution on the membranes and a coomassie blue stain on the gels (Fisher Scientific, Fair lawn, New Jersey). .. The membranes were blocked with 10% nonfat milk overnight at 4°C on an orbital shaker (LabScientific Inc, Livingston, New Jersey).

Article Title: The effect of physiological stretch and the valvular endothelium on mitral valve proteomes
Article Snippet: .. Coomassie blue stain was performed using 1 g/L of Coomassie R250 dye in 45% ethanol and 10% glacial acetic acid (all Fisher Scientific) for 1 h. The stain was washed in excess 10% ethanol and 10% glacial acetic acid. .. Coomassie-stained gel bands were cut in 4 sections according to molecular weight.

Article Title: Development of a liquid chromatography high resolution mass spectrometry method for the quantitation of viral envelope glycoprotein in Ebola virus-like particle vaccine preparations
Article Snippet: .. For this experiment, 2.5 µg of rGP1 and 3.3 µg of unfractionated rGP were resolved on a 4–12 % BOLT SDS PAGE gel (Life Technologies) and stained with Coomassie Blue (Imperial protein stain, Fisher Scientific). .. Lastly, the protein content of the pooled and purified rGP1 preparation was determined by amino acid analysis (AAA) following acid catalyzed hydrolysis by Biosynthesis (Lewisville, TX).

Article Title: Revealing CD38 Cellular Localization Using a Cell Permeable, Mechanism-Based Fluorescent Small-Molecule Probe
Article Snippet: .. Before staining with Coomassie blue, the gel was irradiated under UV light (Transillum, Fisher Scientific, model DLT-A), and the fluorescence image was recorded with a digital camera (Nikon Coolpix L22). .. Labeling of CD38 in Live Cells HL-60 cells were treated with 1 μM RA in cell culture media (GIBCO RPMI Medium 1640 with 10% GIBCO Heat-inactivated Fetal Bovine Serum) for 24 h in a 5% CO2 incubator at 37 °C.

Article Title: De Novo Isolation Affinity Maturation of yeast-displayed Virion-binding human fibronectin domains by flow cytometric screening against Virions
Article Snippet: .. Gels were stained with Coomassie Blue (Fisher Scientific) following electrophoresis. .. Native PAGE analysis was carried out using 3% stacking/12% resolving Bis-Tris gels with the 0.5–1.0 μg of purified Fn3 noted above loaded into each well.

Article Title: Peptic digestion of beef myofibrils is modified by prior marination
Article Snippet: .. Gels were stained with Coomassie blue and de-stained with 10% acetic acid (Fisher Scientific, Loughborough, Leicestershire, UK) over 2 days. .. Digestion of myofibrils for determination of rate of digestion Myofibrils were prepared from meat samples (n=5/group) as described, resuspended at a concentration of 5 mg/ml and digested with pepsin (5 mg/ml final concentration) at 37°C for 60 min.

Article Title: Threonine 89 Is an Important Residue of Profilin-1 That Is Phosphorylatable by Protein Kinase A
Article Snippet: .. The gels were washed twice with MilliQ water for 5 minutes each and then stained with Coomassie blue [0.1% (w/v) R250 (Fisher Scientific, Waltham, MA, USA), 40% (v/v) ethanol (Decon, King of Prussia, PA, USA), 10% (v/v) Acetic Acid (Fisher Scientific, Waltham, MA, USA)]. .. After destaining gels with a destaining solution [10% (v/v) ethanol, 7.5% (v/v) acetic acid], His-tagged Pfn1 gel band was excised, washed with HPLC water and destained with 50% acetonitrile (ACN)/25mM ammonium bicarbonate until staining was no longer visible.

Article Title: De Novo Isolation Affinity Maturation of yeast-displayed Virion-binding human fibronectin domains by flow cytometric screening against Virions
Article Snippet: .. Two electrophoresis intervals were carried out, an initial 15-min interval at 100 V followed by a 55-min interval at 200 V. Gels were stained with Coomassie Blue following electrophoresis. .. ELISA detection of soluble Fn3s binding to Zika Virions For assays measuring binding of immobilized Fn3s to Zika virions, purified, desalted Fn3s were diluted to 8 μg/mL in pH 7.4 PBS and adsorbed onto MaxiSorp 96-well plates (BioLegend) by overnight incubation of 100 μL of Fn3-containing solution at 4 °C.

SDS Page:

Article Title: Development of a liquid chromatography high resolution mass spectrometry method for the quantitation of viral envelope glycoprotein in Ebola virus-like particle vaccine preparations
Article Snippet: .. For this experiment, 2.5 µg of rGP1 and 3.3 µg of unfractionated rGP were resolved on a 4–12 % BOLT SDS PAGE gel (Life Technologies) and stained with Coomassie Blue (Imperial protein stain, Fisher Scientific). .. Lastly, the protein content of the pooled and purified rGP1 preparation was determined by amino acid analysis (AAA) following acid catalyzed hydrolysis by Biosynthesis (Lewisville, TX).

Fluorescence:

Article Title: Revealing CD38 Cellular Localization Using a Cell Permeable, Mechanism-Based Fluorescent Small-Molecule Probe
Article Snippet: .. Before staining with Coomassie blue, the gel was irradiated under UV light (Transillum, Fisher Scientific, model DLT-A), and the fluorescence image was recorded with a digital camera (Nikon Coolpix L22). .. Labeling of CD38 in Live Cells HL-60 cells were treated with 1 μM RA in cell culture media (GIBCO RPMI Medium 1640 with 10% GIBCO Heat-inactivated Fetal Bovine Serum) for 24 h in a 5% CO2 incubator at 37 °C.

Irradiation:

Article Title: Revealing CD38 Cellular Localization Using a Cell Permeable, Mechanism-Based Fluorescent Small-Molecule Probe
Article Snippet: .. Before staining with Coomassie blue, the gel was irradiated under UV light (Transillum, Fisher Scientific, model DLT-A), and the fluorescence image was recorded with a digital camera (Nikon Coolpix L22). .. Labeling of CD38 in Live Cells HL-60 cells were treated with 1 μM RA in cell culture media (GIBCO RPMI Medium 1640 with 10% GIBCO Heat-inactivated Fetal Bovine Serum) for 24 h in a 5% CO2 incubator at 37 °C.

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 91
    Fisher Scientific coomassie brilliant blue
    <t>Coomassie-stained</t> 1D SDS-PAGE gels used in the second in-gel digestion. Fractions of acetone precipitated serum protein samples from a healthy sheep were used. One well in Gel A was loaded with BSA standard ( arrow ), and two other wells were loaded with 100 μg and 50 μg of protein each. Three wells in Gel B were loaded with 50 μg, 100 μg and 50 μg each of protein
    Coomassie Brilliant Blue, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 91/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/coomassie brilliant blue/product/Fisher Scientific
    Average 91 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    coomassie brilliant blue - by Bioz Stars, 2020-08
    91/100 stars
      Buy from Supplier

    90
    Fisher Scientific coomassie blue staining
    RNA, protein and chloroplast DNA. (A) Ethidium bromide-stained denaturing gel of total cell RNAs extracted from 7 week-old wild type Col-0 and im leaves (white and green sectors). The RNAs were loaded on the gel on a fresh weight basis. The rRNA bands are labeled. (B) Chloroplast DNA-specific primers. Real-time qPCR revealed 4 times the amount of chloroplast DNA in white tissues compared to green and wild-type tissues. Same samples as in (A). (C) <t>Coomassie</t> blue-stained 12.5% SDS-polyacrylamide gel of total cell proteins using the same samples as in (A). The proteins were loaded on a fresh weight basis. The large subunit (LS) of Rubisco is indicated; it comprises nearly all of the band migrating at 55 kDa. (D) Protein amounts in the gel lanes were quantified using ImageJ software. Asterisks indicate a significant difference (t-test, p
    Coomassie Blue Staining, supplied by Fisher Scientific, 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/result/coomassie blue staining/product/Fisher Scientific
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    coomassie blue staining - by Bioz Stars, 2020-08
    90/100 stars
      Buy from Supplier

    92
    Fisher Scientific coomassie brilliant blue r 250
    Horizontal nondenaturing PAGE displaying migration of anionic (BSA) and cationic (lysozyme) proteins. PAGE was performed by loading 15 μL of 2 μg/μL protein solution mixed with 3μL 6X mixed dyes solution on the wells in the middle of a gel (5% Acrylamide-N,N-bisacrylamide, 38:2). After running with non-denaturing buffer (30 mM MOPS-25 mM histidine pH 6.5), at constant voltage (100V) for 1 hour, at 4 °C, the gel was stained with <t>Coomassie</t> Blue R-250 according to the protocol published by Dong et al. [ 5 ]. The figure displays migration of BSA (pI 4.8) toward the anode and migration of lysozyme (pI 11.3) toward the cathode.
    Coomassie Brilliant Blue R 250, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 92/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/coomassie brilliant blue r 250/product/Fisher Scientific
    Average 92 stars, based on 17 article reviews
    Price from $9.99 to $1999.99
    coomassie brilliant blue r 250 - by Bioz Stars, 2020-08
    92/100 stars
      Buy from Supplier

    Image Search Results


    Coomassie-stained 1D SDS-PAGE gels used in the second in-gel digestion. Fractions of acetone precipitated serum protein samples from a healthy sheep were used. One well in Gel A was loaded with BSA standard ( arrow ), and two other wells were loaded with 100 μg and 50 μg of protein each. Three wells in Gel B were loaded with 50 μg, 100 μg and 50 μg each of protein

    Journal: Proteome Science

    Article Title: Characterisation of the circulating acellular proteome of healthy sheep using LC-MS/MS-based proteomics analysis of serum

    doi: 10.1186/s12953-017-0119-z

    Figure Lengend Snippet: Coomassie-stained 1D SDS-PAGE gels used in the second in-gel digestion. Fractions of acetone precipitated serum protein samples from a healthy sheep were used. One well in Gel A was loaded with BSA standard ( arrow ), and two other wells were loaded with 100 μg and 50 μg of protein each. Three wells in Gel B were loaded with 50 μg, 100 μg and 50 μg each of protein

    Article Snippet: The gels were stained with Coomassie brilliant blue (EZ-Run™, Protein Gel Staining Solution, Fisher Scientific) according to the manufacturer’s instructions and then photographed using a handheld camera (5.7-inch Quad HD Super AMOLED®, Samsung; or New 8-megapixel iSight camera with 1.5 μ pixels with Optical image stabilisation, iPhone 6, Apple Inc.).

    Techniques: Staining, SDS Page

    Coomassie-stained 1D SDS-PAGE gels used for the third in-gel digestion. Fractions of pooled serum protein samples from six healthy sheep were used. In Gel A, one well was loaded with 200 μg of crude serum protein and the other well was loaded with 100 μg. Three 100 μg of serum protein for Gel B and C were loaded identically and treated as follows: one well was loaded with crude serum with a protease inhibitor (SP 100 μg + Pi), the second well had acetone precipitated serum and a protease inhibitor (SP 100 μg + Pi + Ac); the third well was loaded with crude serum only (SP 100 μg)

    Journal: Proteome Science

    Article Title: Characterisation of the circulating acellular proteome of healthy sheep using LC-MS/MS-based proteomics analysis of serum

    doi: 10.1186/s12953-017-0119-z

    Figure Lengend Snippet: Coomassie-stained 1D SDS-PAGE gels used for the third in-gel digestion. Fractions of pooled serum protein samples from six healthy sheep were used. In Gel A, one well was loaded with 200 μg of crude serum protein and the other well was loaded with 100 μg. Three 100 μg of serum protein for Gel B and C were loaded identically and treated as follows: one well was loaded with crude serum with a protease inhibitor (SP 100 μg + Pi), the second well had acetone precipitated serum and a protease inhibitor (SP 100 μg + Pi + Ac); the third well was loaded with crude serum only (SP 100 μg)

    Article Snippet: The gels were stained with Coomassie brilliant blue (EZ-Run™, Protein Gel Staining Solution, Fisher Scientific) according to the manufacturer’s instructions and then photographed using a handheld camera (5.7-inch Quad HD Super AMOLED®, Samsung; or New 8-megapixel iSight camera with 1.5 μ pixels with Optical image stabilisation, iPhone 6, Apple Inc.).

    Techniques: Staining, SDS Page, Protease Inhibitor

    Coomassie-stained 1D SDS-PAGE gels used in first in-gel digestion. Fractions of acetone precipitated serum protein from a healthy sheep were loaded alongside bovine serum albumin (BSA) in Gel A. Gel A suffered a handling artefact to the top right corner of the gel. The leftmost well of both gels were loaded with 4 μL of a protein molecular weight standard (Precision Plus Protein™ Dual Xtra, Bio-Rad Laboratories). One well in Gel A was loaded with 500 fm of BSA standard; other three wells were loaded with 22 μg, 10 μg and 2 μg each of sheep serum protein sample. After the molecular weight standard, the other three wells in Gel B were loaded with 500 fm, 2500 fm and 250 fm each of BSA standard. Arrows show BSA standard

    Journal: Proteome Science

    Article Title: Characterisation of the circulating acellular proteome of healthy sheep using LC-MS/MS-based proteomics analysis of serum

    doi: 10.1186/s12953-017-0119-z

    Figure Lengend Snippet: Coomassie-stained 1D SDS-PAGE gels used in first in-gel digestion. Fractions of acetone precipitated serum protein from a healthy sheep were loaded alongside bovine serum albumin (BSA) in Gel A. Gel A suffered a handling artefact to the top right corner of the gel. The leftmost well of both gels were loaded with 4 μL of a protein molecular weight standard (Precision Plus Protein™ Dual Xtra, Bio-Rad Laboratories). One well in Gel A was loaded with 500 fm of BSA standard; other three wells were loaded with 22 μg, 10 μg and 2 μg each of sheep serum protein sample. After the molecular weight standard, the other three wells in Gel B were loaded with 500 fm, 2500 fm and 250 fm each of BSA standard. Arrows show BSA standard

    Article Snippet: The gels were stained with Coomassie brilliant blue (EZ-Run™, Protein Gel Staining Solution, Fisher Scientific) according to the manufacturer’s instructions and then photographed using a handheld camera (5.7-inch Quad HD Super AMOLED®, Samsung; or New 8-megapixel iSight camera with 1.5 μ pixels with Optical image stabilisation, iPhone 6, Apple Inc.).

    Techniques: Staining, SDS Page, Molecular Weight

    RNA, protein and chloroplast DNA. (A) Ethidium bromide-stained denaturing gel of total cell RNAs extracted from 7 week-old wild type Col-0 and im leaves (white and green sectors). The RNAs were loaded on the gel on a fresh weight basis. The rRNA bands are labeled. (B) Chloroplast DNA-specific primers. Real-time qPCR revealed 4 times the amount of chloroplast DNA in white tissues compared to green and wild-type tissues. Same samples as in (A). (C) Coomassie blue-stained 12.5% SDS-polyacrylamide gel of total cell proteins using the same samples as in (A). The proteins were loaded on a fresh weight basis. The large subunit (LS) of Rubisco is indicated; it comprises nearly all of the band migrating at 55 kDa. (D) Protein amounts in the gel lanes were quantified using ImageJ software. Asterisks indicate a significant difference (t-test, p

    Journal: PLoS ONE

    Article Title: Impaired Chloroplast Biogenesis in Immutans, an Arabidopsis Variegation Mutant, Modifies Developmental Programming, Cell Wall Composition and Resistance to Pseudomonas syringae

    doi: 10.1371/journal.pone.0150983

    Figure Lengend Snippet: RNA, protein and chloroplast DNA. (A) Ethidium bromide-stained denaturing gel of total cell RNAs extracted from 7 week-old wild type Col-0 and im leaves (white and green sectors). The RNAs were loaded on the gel on a fresh weight basis. The rRNA bands are labeled. (B) Chloroplast DNA-specific primers. Real-time qPCR revealed 4 times the amount of chloroplast DNA in white tissues compared to green and wild-type tissues. Same samples as in (A). (C) Coomassie blue-stained 12.5% SDS-polyacrylamide gel of total cell proteins using the same samples as in (A). The proteins were loaded on a fresh weight basis. The large subunit (LS) of Rubisco is indicated; it comprises nearly all of the band migrating at 55 kDa. (D) Protein amounts in the gel lanes were quantified using ImageJ software. Asterisks indicate a significant difference (t-test, p

    Article Snippet: After centrifugation (5,000g for 15 minutes), equal fresh weights of the protein extracts were subjected to 10% SDS-PAGE analysis, followed by Coomassie Blue staining (Fisher Scientific).

    Techniques: Staining, Labeling, Real-time Polymerase Chain Reaction, Software, T-Test

    Horizontal nondenaturing PAGE displaying migration of anionic (BSA) and cationic (lysozyme) proteins. PAGE was performed by loading 15 μL of 2 μg/μL protein solution mixed with 3μL 6X mixed dyes solution on the wells in the middle of a gel (5% Acrylamide-N,N-bisacrylamide, 38:2). After running with non-denaturing buffer (30 mM MOPS-25 mM histidine pH 6.5), at constant voltage (100V) for 1 hour, at 4 °C, the gel was stained with Coomassie Blue R-250 according to the protocol published by Dong et al. [ 5 ]. The figure displays migration of BSA (pI 4.8) toward the anode and migration of lysozyme (pI 11.3) toward the cathode.

    Journal: bioRxiv

    Article Title: Label-free horizontal EMSA for analysis of protein-RNA interactions

    doi: 10.1101/825679

    Figure Lengend Snippet: Horizontal nondenaturing PAGE displaying migration of anionic (BSA) and cationic (lysozyme) proteins. PAGE was performed by loading 15 μL of 2 μg/μL protein solution mixed with 3μL 6X mixed dyes solution on the wells in the middle of a gel (5% Acrylamide-N,N-bisacrylamide, 38:2). After running with non-denaturing buffer (30 mM MOPS-25 mM histidine pH 6.5), at constant voltage (100V) for 1 hour, at 4 °C, the gel was stained with Coomassie Blue R-250 according to the protocol published by Dong et al. [ 5 ]. The figure displays migration of BSA (pI 4.8) toward the anode and migration of lysozyme (pI 11.3) toward the cathode.

    Article Snippet: Coomassie Brilliant Blue R-250 was purchased from Fisher Scientific (Fair Lawn, NJ, USA).

    Techniques: Polyacrylamide Gel Electrophoresis, Migration, Staining

    BChE resolved by nondenaturing polyacrylamide gel electrophoresis (PAGE). Lanes 1 to 4 were stained for BChE activity. Lanes 5 and 6 were stained with Coomassie Blue R-250. Lane 1, human serum 5 μl; lane 2, horse serum 5 μl; lane 3, not boiled purified horse BChE (0.015 units = 0.02 μg); lane 4, boiled purified horse BChE 0.02 μg; lane 5, not boiled purified horse BChE 2 μg; lane 6, boiled purified horse BChE 2 μg. The arrow indicates the direction of migration toward the positive electrode.

    Journal: The FEBS journal

    Article Title: The Proline Rich Tetramerization Peptides in Equine Serum Butyrylcholinesterase

    doi: 10.1111/j.1742-4658.2012.08744.x

    Figure Lengend Snippet: BChE resolved by nondenaturing polyacrylamide gel electrophoresis (PAGE). Lanes 1 to 4 were stained for BChE activity. Lanes 5 and 6 were stained with Coomassie Blue R-250. Lane 1, human serum 5 μl; lane 2, horse serum 5 μl; lane 3, not boiled purified horse BChE (0.015 units = 0.02 μg); lane 4, boiled purified horse BChE 0.02 μg; lane 5, not boiled purified horse BChE 2 μg; lane 6, boiled purified horse BChE 2 μg. The arrow indicates the direction of migration toward the positive electrode.

    Article Snippet: Acetonitrile (DNA sequencing grade, catalog number BP-1170), dithiothreitol (electrophoresis grade, catalog number BP172), bromophenol blue (electrophoresis grade, catalog number BP114) and Coomassie Brilliant Blue R-250 (electrophoresis grade, catalog number BP101) were from Fisher Scientific (a member of the Thermo Fisher Scientific group, Waltham MA, U.S.A.).

    Techniques: Polyacrylamide Gel Electrophoresis, Staining, Activity Assay, Purification, Migration