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  • 99
    Thermo Fisher coomassie brilliant blue r 250
    CtBP2 forms a complex with p300 and Runx2 in vivo . (A) In vivo pull-down of the Flag-HA-CtBP2-associated complexes. The HOB-1 cells were transfected with pCDNA3-2xFlag-3xHA-CtBP2 or pCDNA3-2xFlag-3xHA . After 48 hours, the cells were lysed and subjected to IP analysis. The resulting protein complexes were loaded onto SDS-PAGE gel for separation and then stained with <t>Coomassie</t> Brilliant Blue R 250. The IgG and CtBP2 bands were indicated. (B) Verification of CtBP2-associated proteins identified in LC-MS/MS analysis. The protein samples used in (A) were used to verify the association of CtBP2, p300 and Runx2. (C and D) CtBP2 directly interacted with p300 in HOB-1 cells. The HOB-1 cells were cotransfected with pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc-p300 , pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc , or pCDNA3-2xFlag + pCDNA3-6xMyc-p300 . After 48 hours, the cells were lysed and subjected to IP analysis with either anti-Flag-agarose (C) or anti-Myc-agarose (D) . The pull-down products were then subjected to western blot with the antibodies indicated in the figures. (E and F) CtBP2 cannot directly interact with Runx2 in HOB-1 cells. The HOB-1 cells were cotransfected with pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc-Runx2 , pCDNA3-2xFlag + pCDNA3-6xMyc-Runx2 , or pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc . After 48 hours, the cells were lysed and subjected to IP analysis with either anti-Flag-agarose (E) or anti-Myc-agarose (F) . The pull-down products were then subjected to western blot with the antibodies indicated in the figures.
    Coomassie Brilliant Blue R 250, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 643 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore coomassie brilliant blue r 250
    SDS-PAGE analysis of bovine casein after digestion by Porthidin-1. Lanes: 1) low range molecular weight markers; 2) bovine casein control (25 μg); 3–5) bovine casein with Porthidin-1 at 100:1, 100:5, 100:10 ratios, respectively; 6) Porthidin-1 control (3 μg) (arrow). The samples were run under reducing conditions on a 12.5% gel. The gel was stained with <t>Coomassie</t> Brilliant Blue R-250. α s1 , β and κ represent the casein chains.
    Coomassie Brilliant Blue R 250, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4187 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Bio-Rad coomassie brilliant blue r 250
    SDS-PAGE gel (4–20%) of non-denatured Avidin (n-Av) and denatured Avidin (d-Av) stained with <t>Coomassie</t> Brilliant Blue R-250. B. Native PAGE gel (7.5%) of Avidin (Av), PEG, 1:2 mAv and 1:4 mAv under reverse polarity stained with (left) iodine for PEGs and with (right) Coomassie Brilliant Blue R-250 for protein. C. UPLC analysis of standard Avidin shows peak ‘a’ at 6.29 min. 1:6 mAv and 1:4 mAv formulation have similar peak shape showing a majority of mAv with 4 PEGs (peak ‘b’ at 4.38 min or 4.37 min) and a secondary population of mAv with 2 PEGs (peak ‘d’ at 5.33 min). In addition, 1:2 mAv has three peaks, a majority of mAv with 2 PEGs (peak ‘d’ at 5.35 min), a secondary population of mAv with 3 PEGs (peak ‘c’ at 4.80 min) and a minority of mAv with 1 PEGs (peak ‘e’ at 5.86 min).
    Coomassie Brilliant Blue R 250, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 4114 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad coomassie brilliant blue r 250 staining solution
    Analysis by optical microscopy (100×) after staining with <t>Coomassie</t> blue R-250 of Pichia pastoris GS115 (control) and P. pastoris CL2 cells induced by cold-shock and after the entire treatment. a , c Control cells of P. pastoris GS115 at 12 h and 24 h in stage IV, respectivelly; b , d P. pastoris CL2 cells at 12 and 24 h in stage IV, respectively. Bar 15 µm
    Coomassie Brilliant Blue R 250 Staining Solution, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 414 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Amresco coomassie brilliant blue r 250
    2-DE gel spots subjected to MALDI-TOF-TOF MS Two spots (a and b) identified as differentially-ubiquitinated according to Figure 2 and an adjacent spot (c) were cut from 2-DE gels stained with <t>Coomassie</t> Brilliant Blue R-250 and subjected to MALDI-TOF-TOF MS. All of them were identified as annexin A2.
    Coomassie Brilliant Blue R 250, supplied by Amresco, used in various techniques. Bioz Stars score: 92/100, based on 207 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore coomassie staining
    MeCP2 is physically associated with nucleosome complexes. a MeCP2 antibody immunoprecipitated proteins from mouse OE nuclear extract in SDS gel visualized with <t>Coomassie</t> blue. Nuclear extract is loaded as input; rabbit IgG as a negative control. Star is around 25–30 kDa. b Benzonase treated nuclear extracts were immunoprecipitated either with anti-MeCP2 antibody or anti-histone H1 antibody. Samples of input, IgG and immunoprecipitates were analyzed with western blotting for histone H1 or MeCP2. c Benzonase treated nuclear extracts were immunoprecipitated with a MeCP2 antibody specific to its C-terminus. Input, IgG control and immunoprecipitates were analyzed with Western blotting for the presence of histone H3 and H4. d Z-transformed aggregate plot of the average tag density of MeCP2 binding sites (hotspot, green) at chr19 occupied by: Nucleosome occupancies (gray) and histone H1 (purple). e Z-transformed aggregate plot of the average tag density of MNase-seq (hotspot, gray) at chr19 occupied by: MeCP2 (green) and histone H1 (purple). f Genome-wide inter-correlation among Input, histone H1 ChIP-seq, MeCP2 ChIP-seq, and MNase-seq (binning size = 150 bp). Number in the square indicates the Pearson correlation coefficient. Source data are provided as a Source data file ( b and c ). The shaded areas are up to ±S.D. from the average profile ( d and e ).
    Coomassie Staining, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 930 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck KGaA coomassie brilliant blue r 250
    MeCP2 is physically associated with nucleosome complexes. a MeCP2 antibody immunoprecipitated proteins from mouse OE nuclear extract in SDS gel visualized with <t>Coomassie</t> blue. Nuclear extract is loaded as input; rabbit IgG as a negative control. Star is around 25–30 kDa. b Benzonase treated nuclear extracts were immunoprecipitated either with anti-MeCP2 antibody or anti-histone H1 antibody. Samples of input, IgG and immunoprecipitates were analyzed with western blotting for histone H1 or MeCP2. c Benzonase treated nuclear extracts were immunoprecipitated with a MeCP2 antibody specific to its C-terminus. Input, IgG control and immunoprecipitates were analyzed with Western blotting for the presence of histone H3 and H4. d Z-transformed aggregate plot of the average tag density of MeCP2 binding sites (hotspot, green) at chr19 occupied by: Nucleosome occupancies (gray) and histone H1 (purple). e Z-transformed aggregate plot of the average tag density of MNase-seq (hotspot, gray) at chr19 occupied by: MeCP2 (green) and histone H1 (purple). f Genome-wide inter-correlation among Input, histone H1 ChIP-seq, MeCP2 ChIP-seq, and MNase-seq (binning size = 150 bp). Number in the square indicates the Pearson correlation coefficient. Source data are provided as a Source data file ( b and c ). The shaded areas are up to ±S.D. from the average profile ( d and e ).
    Coomassie Brilliant Blue R 250, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 92/100, based on 318 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad coomassie staining
    SDS-PAGE of PARL with TAMRA probe. To determine orientation of PARL in the proteoliposomes, PARL in PLs was incubated with TAMRA and then separated on a 14% SDS-PAGE gel. The fluorescent TAMRA probe was visualized using an imager (left) and also stained with <t>Coomassie</t> blue (right).
    Coomassie Staining, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1904 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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 118 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Nacalai 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 Nacalai, used in various techniques. Bioz Stars score: 93/100, based on 175 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Merck & Co 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 Merck & Co, used in various techniques. Bioz Stars score: 93/100, based on 100 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    CtBP2 forms a complex with p300 and Runx2 in vivo . (A) In vivo pull-down of the Flag-HA-CtBP2-associated complexes. The HOB-1 cells were transfected with pCDNA3-2xFlag-3xHA-CtBP2 or pCDNA3-2xFlag-3xHA . After 48 hours, the cells were lysed and subjected to IP analysis. The resulting protein complexes were loaded onto SDS-PAGE gel for separation and then stained with Coomassie Brilliant Blue R 250. The IgG and CtBP2 bands were indicated. (B) Verification of CtBP2-associated proteins identified in LC-MS/MS analysis. The protein samples used in (A) were used to verify the association of CtBP2, p300 and Runx2. (C and D) CtBP2 directly interacted with p300 in HOB-1 cells. The HOB-1 cells were cotransfected with pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc-p300 , pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc , or pCDNA3-2xFlag + pCDNA3-6xMyc-p300 . After 48 hours, the cells were lysed and subjected to IP analysis with either anti-Flag-agarose (C) or anti-Myc-agarose (D) . The pull-down products were then subjected to western blot with the antibodies indicated in the figures. (E and F) CtBP2 cannot directly interact with Runx2 in HOB-1 cells. The HOB-1 cells were cotransfected with pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc-Runx2 , pCDNA3-2xFlag + pCDNA3-6xMyc-Runx2 , or pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc . After 48 hours, the cells were lysed and subjected to IP analysis with either anti-Flag-agarose (E) or anti-Myc-agarose (F) . The pull-down products were then subjected to western blot with the antibodies indicated in the figures.

    Journal: International Journal of Biological Sciences

    Article Title: The intracellular NADH level regulates atrophic nonunion pathogenesis through the CtBP2-p300-Runx2 transcriptional complex

    doi: 10.7150/ijbs.28302

    Figure Lengend Snippet: CtBP2 forms a complex with p300 and Runx2 in vivo . (A) In vivo pull-down of the Flag-HA-CtBP2-associated complexes. The HOB-1 cells were transfected with pCDNA3-2xFlag-3xHA-CtBP2 or pCDNA3-2xFlag-3xHA . After 48 hours, the cells were lysed and subjected to IP analysis. The resulting protein complexes were loaded onto SDS-PAGE gel for separation and then stained with Coomassie Brilliant Blue R 250. The IgG and CtBP2 bands were indicated. (B) Verification of CtBP2-associated proteins identified in LC-MS/MS analysis. The protein samples used in (A) were used to verify the association of CtBP2, p300 and Runx2. (C and D) CtBP2 directly interacted with p300 in HOB-1 cells. The HOB-1 cells were cotransfected with pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc-p300 , pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc , or pCDNA3-2xFlag + pCDNA3-6xMyc-p300 . After 48 hours, the cells were lysed and subjected to IP analysis with either anti-Flag-agarose (C) or anti-Myc-agarose (D) . The pull-down products were then subjected to western blot with the antibodies indicated in the figures. (E and F) CtBP2 cannot directly interact with Runx2 in HOB-1 cells. The HOB-1 cells were cotransfected with pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc-Runx2 , pCDNA3-2xFlag + pCDNA3-6xMyc-Runx2 , or pCDNA3-2xFlag-CtBP2 + pCDNA3-6xMyc . After 48 hours, the cells were lysed and subjected to IP analysis with either anti-Flag-agarose (E) or anti-Myc-agarose (F) . The pull-down products were then subjected to western blot with the antibodies indicated in the figures.

    Article Snippet: The resulting proteins were immunoprecipitated with anti-HA-agarose for at 4°C for 6 hours, and after washing five times with RIPA buffer, the HA-CtBP2 protein complex was loaded onto SDS-PAGE gels for electrophoresis, followed by staining with Coomassie Brilliant Blue R 250 (Thermo Fisher Scientific, #20278).

    Techniques: In Vivo, Transfection, SDS Page, Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Western Blot

    Purified proteins were electrophoresed by 12% SDS-PAGE and stained with Coomassie Brilliant Blue R250. Tri-fusion, Ppe44, EsxV, and HspX were detected as 70, 65, 40, and 16 kDa bands.

    Journal: Reports of Biochemistry & Molecular Biology

    Article Title: Heterologous Expression, Purification, and Characterization of the HspX, Ppe44, and EsxV Proteins of Mycobacterium tuberculosis

    doi:

    Figure Lengend Snippet: Purified proteins were electrophoresed by 12% SDS-PAGE and stained with Coomassie Brilliant Blue R250. Tri-fusion, Ppe44, EsxV, and HspX were detected as 70, 65, 40, and 16 kDa bands.

    Article Snippet: Protein bands were stained with Coomassie Brilliant Blue R250 and band sizes were determined using a protein ladder (Thermo Scientific).

    Techniques: Purification, SDS Page, Staining

    SDS-PAGE analysis of bovine casein after digestion by Porthidin-1. Lanes: 1) low range molecular weight markers; 2) bovine casein control (25 μg); 3–5) bovine casein with Porthidin-1 at 100:1, 100:5, 100:10 ratios, respectively; 6) Porthidin-1 control (3 μg) (arrow). The samples were run under reducing conditions on a 12.5% gel. The gel was stained with Coomassie Brilliant Blue R-250. α s1 , β and κ represent the casein chains.

    Journal: Toxicon

    Article Title: Purification and characterization of a metalloproteinase, Porthidin-1, from the venom of Lansberg's hog-nosed pitvipers (Porthidium lansbergii hutmanni)

    doi: 10.1016/j.toxicon.2011.01.003

    Figure Lengend Snippet: SDS-PAGE analysis of bovine casein after digestion by Porthidin-1. Lanes: 1) low range molecular weight markers; 2) bovine casein control (25 μg); 3–5) bovine casein with Porthidin-1 at 100:1, 100:5, 100:10 ratios, respectively; 6) Porthidin-1 control (3 μg) (arrow). The samples were run under reducing conditions on a 12.5% gel. The gel was stained with Coomassie Brilliant Blue R-250. α s1 , β and κ represent the casein chains.

    Article Snippet: Coomassie Brilliant Blue R-250, Benzamidine/HCL, 1–10 phenantroline, phenylmethylsulfonyl fluoride (PMSF), ethylene glycol-bis-N,N,N′,N′-tetraacetic acid (EGTA), ethylenediaminetetraacetic acid (EDTA), iodoacetic acid and other chemicals and solvents were obtained from Sigma (St. Louis, MO, USA).

    Techniques: SDS Page, Molecular Weight, Staining

    SDS/PAGE of the mAb SO57 purified from transgenic plants. Purified mAbs were loaded onto the gels and stained with Coomassie brilliant blue R250. TPS, total protein extract from plant leaves; mAb H , hybridoma-derived mAb SO57; mAb P , non-KDEL-tagged mAb P ; mAb P K, KDEL-tagged mAb P ; HC, heavy chains of mAb P ; LC, light chain of mAb P .

    Journal: PLoS ONE

    Article Title: Intracellular Reprogramming of Expression, Glycosylation, and Function of a Plant-Derived Antiviral Therapeutic Monoclonal Antibody

    doi: 10.1371/journal.pone.0068772

    Figure Lengend Snippet: SDS/PAGE of the mAb SO57 purified from transgenic plants. Purified mAbs were loaded onto the gels and stained with Coomassie brilliant blue R250. TPS, total protein extract from plant leaves; mAb H , hybridoma-derived mAb SO57; mAb P , non-KDEL-tagged mAb P ; mAb P K, KDEL-tagged mAb P ; HC, heavy chains of mAb P ; LC, light chain of mAb P .

    Article Snippet: The proteins in the homogenates were resolved by 12.5% SDS-PAGE and either stained by using Coomassie brilliant blue R250 or transferred to a nitrocellulose membrane (Millipore, Billerica, MA).

    Techniques: SDS Page, Purification, Transgenic Assay, Staining, Derivative Assay

    Analysis of total protein isolated from quiescent cells. Total protein from DS941 hns-205 pCm(ss)-19 was isolated at various times after the induction of Rcd expression. Proteins were separated on an SDS–12.5% polyacrylamide gel and stained with Coomassie brilliant blue R. Lanes: 1, purified CAT protein (0.4 μg); 2, total protein from DS941 hns-205 pACYC/ c I ts 857 grown at 42°C for 160 min (OD 600 = 0.219); 3, DS941 hns-205 pCm(ss)-19 grown at 42°C for 1 h (OD 600 = 0.147); 4, for 2 h (OD 600 = 0.211); 5, for 7 h (OD 600 = 0.279); or 6, for 10 h (OD 600 = 0.285).

    Journal: Applied and Environmental Microbiology

    Article Title: The Quiescent-Cell Expression System for Protein Synthesis in Escherichia coli

    doi:

    Figure Lengend Snippet: Analysis of total protein isolated from quiescent cells. Total protein from DS941 hns-205 pCm(ss)-19 was isolated at various times after the induction of Rcd expression. Proteins were separated on an SDS–12.5% polyacrylamide gel and stained with Coomassie brilliant blue R. Lanes: 1, purified CAT protein (0.4 μg); 2, total protein from DS941 hns-205 pACYC/ c I ts 857 grown at 42°C for 160 min (OD 600 = 0.219); 3, DS941 hns-205 pCm(ss)-19 grown at 42°C for 1 h (OD 600 = 0.147); 4, for 2 h (OD 600 = 0.211); 5, for 7 h (OD 600 = 0.279); or 6, for 10 h (OD 600 = 0.285).

    Article Snippet: Two to 4 μl of proteins was also separated on a 12.5% homogenous SDS-PAGE Phast-Gel, stained with Coomassie brilliant blue R (Sigma-Aldrich), and destained in methanol-water-acetic acid (40:53:7).

    Techniques: Isolation, Expressing, Staining, Purification

    SDS-PAGE gel (4–20%) of non-denatured Avidin (n-Av) and denatured Avidin (d-Av) stained with Coomassie Brilliant Blue R-250. B. Native PAGE gel (7.5%) of Avidin (Av), PEG, 1:2 mAv and 1:4 mAv under reverse polarity stained with (left) iodine for PEGs and with (right) Coomassie Brilliant Blue R-250 for protein. C. UPLC analysis of standard Avidin shows peak ‘a’ at 6.29 min. 1:6 mAv and 1:4 mAv formulation have similar peak shape showing a majority of mAv with 4 PEGs (peak ‘b’ at 4.38 min or 4.37 min) and a secondary population of mAv with 2 PEGs (peak ‘d’ at 5.33 min). In addition, 1:2 mAv has three peaks, a majority of mAv with 2 PEGs (peak ‘d’ at 5.35 min), a secondary population of mAv with 3 PEGs (peak ‘c’ at 4.80 min) and a minority of mAv with 1 PEGs (peak ‘e’ at 5.86 min).

    Journal: MethodsX

    Article Title: Avidin-biotin technology to synthesize multi-arm nano-construct for drug delivery

    doi: 10.1016/j.mex.2020.100882

    Figure Lengend Snippet: SDS-PAGE gel (4–20%) of non-denatured Avidin (n-Av) and denatured Avidin (d-Av) stained with Coomassie Brilliant Blue R-250. B. Native PAGE gel (7.5%) of Avidin (Av), PEG, 1:2 mAv and 1:4 mAv under reverse polarity stained with (left) iodine for PEGs and with (right) Coomassie Brilliant Blue R-250 for protein. C. UPLC analysis of standard Avidin shows peak ‘a’ at 6.29 min. 1:6 mAv and 1:4 mAv formulation have similar peak shape showing a majority of mAv with 4 PEGs (peak ‘b’ at 4.38 min or 4.37 min) and a secondary population of mAv with 2 PEGs (peak ‘d’ at 5.33 min). In addition, 1:2 mAv has three peaks, a majority of mAv with 2 PEGs (peak ‘d’ at 5.35 min), a secondary population of mAv with 3 PEGs (peak ‘c’ at 4.80 min) and a minority of mAv with 1 PEGs (peak ‘e’ at 5.86 min).

    Article Snippet: 2x Laemmli Sample Buffer, 4–20% Mini-PROTEAN® TGX™ Precast Protein Gels (12-well), Coomassie Brilliant Blue R-250 were purchased from Bio-Rad (Hercules, CA).

    Techniques: SDS Page, Avidin-Biotin Assay, Staining, Clear Native PAGE

    Coomassie Blue Staining and Western Blot Analysis of the Purified rgD5. (A) After purification steps, different concentrations of purified rgD5 protein (55 kDa) were separated by SDS-PAGE in a 12% gel and stained overnight with Coomassie Blue R-250. Lane kDa: Unstained Protein MW Marker (Fermentas/Thermo Fisher Scientific); Lane 10: 10 μg rgD5; Lane 5: 5 μg rgD5; Lane 2: 2 μg of rgD5; (B) Western blot was performed with mouse monoclonal antibody (MAb) Anti-6xHis HRP conjugated (Anti-6xHis) or with polyclonal antibodies (PAb) from bovine immunized with inactivated BoHV-5 (Anti-BoHV-5). Lane M: Prestained Low Range Protein MW Standard (Bio-Rad); Lane 1: Purified rgD5; Lane 2: KM71H supernatant of non-transformed yeast cells after methanol induction used as negative control.

    Journal: PLoS ONE

    Article Title: Development of an Indirect ELISA for Serological Diagnosis of Bovine herpesvirus 5

    doi: 10.1371/journal.pone.0149134

    Figure Lengend Snippet: Coomassie Blue Staining and Western Blot Analysis of the Purified rgD5. (A) After purification steps, different concentrations of purified rgD5 protein (55 kDa) were separated by SDS-PAGE in a 12% gel and stained overnight with Coomassie Blue R-250. Lane kDa: Unstained Protein MW Marker (Fermentas/Thermo Fisher Scientific); Lane 10: 10 μg rgD5; Lane 5: 5 μg rgD5; Lane 2: 2 μg of rgD5; (B) Western blot was performed with mouse monoclonal antibody (MAb) Anti-6xHis HRP conjugated (Anti-6xHis) or with polyclonal antibodies (PAb) from bovine immunized with inactivated BoHV-5 (Anti-BoHV-5). Lane M: Prestained Low Range Protein MW Standard (Bio-Rad); Lane 1: Purified rgD5; Lane 2: KM71H supernatant of non-transformed yeast cells after methanol induction used as negative control.

    Article Snippet: The gels were either stained overnight with Coomassie Blue R-250 (Bio-Rad) or electroblotted onto nitrocellulose membrane (Bio-Rad) using Bio-Rad Mini Trans-Blot Cell (Bio-Rad).

    Techniques: Staining, Western Blot, Purification, SDS Page, Marker, Transformation Assay, Negative Control

    T1-like structural proteins (Lane 2-5) alongside the standard marker (Lane1) separated on 12% SDS-PAGE gel and visualized by Coomassie brilliant blue R250 stain. A, tail fiber protein; B, tail tape measure protein; C, portal protein; D, major capsid protein; E, minor tail protein; F, major tail protein; G, conserved hypothetical protein.

    Journal: PLoS ONE

    Article Title: Four Escherichia coli O157:H7 Phages: A New Bacteriophage Genus and Taxonomic Classification of T1-Like Phages

    doi: 10.1371/journal.pone.0100426

    Figure Lengend Snippet: T1-like structural proteins (Lane 2-5) alongside the standard marker (Lane1) separated on 12% SDS-PAGE gel and visualized by Coomassie brilliant blue R250 stain. A, tail fiber protein; B, tail tape measure protein; C, portal protein; D, major capsid protein; E, minor tail protein; F, major tail protein; G, conserved hypothetical protein.

    Article Snippet: Proteins were stained with Coomassie brilliant blue R250 (Bio-Rad Laboratories, Mississauga, ON, Canada) and subsequently characterized using Bionumerics 6.6 software (Applied Maths, Austin, TX, USA).

    Techniques: Marker, SDS Page, Staining

    Analysis by optical microscopy (100×) after staining with Coomassie blue R-250 of Pichia pastoris GS115 (control) and P. pastoris CL2 cells induced by cold-shock and after the entire treatment. a , c Control cells of P. pastoris GS115 at 12 h and 24 h in stage IV, respectivelly; b , d P. pastoris CL2 cells at 12 and 24 h in stage IV, respectively. Bar 15 µm

    Journal: AMB Express

    Article Title: Autolysis of Pichia pastoris induced by cold

    doi: 10.1186/s13568-017-0397-y

    Figure Lengend Snippet: Analysis by optical microscopy (100×) after staining with Coomassie blue R-250 of Pichia pastoris GS115 (control) and P. pastoris CL2 cells induced by cold-shock and after the entire treatment. a , c Control cells of P. pastoris GS115 at 12 h and 24 h in stage IV, respectivelly; b , d P. pastoris CL2 cells at 12 and 24 h in stage IV, respectively. Bar 15 µm

    Article Snippet: After centrifugation the cells were suspended in 1.0 ml distilled water and mixed with Coomassie brilliant blue R-250 staining solution (5:1; Bio-Rad).

    Techniques: Microscopy, Staining

    2-DE gel spots subjected to MALDI-TOF-TOF MS Two spots (a and b) identified as differentially-ubiquitinated according to Figure 2 and an adjacent spot (c) were cut from 2-DE gels stained with Coomassie Brilliant Blue R-250 and subjected to MALDI-TOF-TOF MS. All of them were identified as annexin A2.

    Journal: Genomics, Proteomics & Bioinformatics

    Article Title: Overexpression of Annexin A2 Is Associated with Abnormal Ubiquitination in Breast Cancer

    doi: 10.1016/j.gpb.2011.12.001

    Figure Lengend Snippet: 2-DE gel spots subjected to MALDI-TOF-TOF MS Two spots (a and b) identified as differentially-ubiquitinated according to Figure 2 and an adjacent spot (c) were cut from 2-DE gels stained with Coomassie Brilliant Blue R-250 and subjected to MALDI-TOF-TOF MS. All of them were identified as annexin A2.

    Article Snippet: After Western blotting, we aligned the membrane with the duplicate gels stained with Coomassie Brilliant Blue R-250.

    Techniques: Mass Spectrometry, Staining

    MeCP2 is physically associated with nucleosome complexes. a MeCP2 antibody immunoprecipitated proteins from mouse OE nuclear extract in SDS gel visualized with Coomassie blue. Nuclear extract is loaded as input; rabbit IgG as a negative control. Star is around 25–30 kDa. b Benzonase treated nuclear extracts were immunoprecipitated either with anti-MeCP2 antibody or anti-histone H1 antibody. Samples of input, IgG and immunoprecipitates were analyzed with western blotting for histone H1 or MeCP2. c Benzonase treated nuclear extracts were immunoprecipitated with a MeCP2 antibody specific to its C-terminus. Input, IgG control and immunoprecipitates were analyzed with Western blotting for the presence of histone H3 and H4. d Z-transformed aggregate plot of the average tag density of MeCP2 binding sites (hotspot, green) at chr19 occupied by: Nucleosome occupancies (gray) and histone H1 (purple). e Z-transformed aggregate plot of the average tag density of MNase-seq (hotspot, gray) at chr19 occupied by: MeCP2 (green) and histone H1 (purple). f Genome-wide inter-correlation among Input, histone H1 ChIP-seq, MeCP2 ChIP-seq, and MNase-seq (binning size = 150 bp). Number in the square indicates the Pearson correlation coefficient. Source data are provided as a Source data file ( b and c ). The shaded areas are up to ±S.D. from the average profile ( d and e ).

    Journal: Nature Communications

    Article Title: MeCP2 regulates gene expression through recognition of H3K27me3

    doi: 10.1038/s41467-020-16907-0

    Figure Lengend Snippet: MeCP2 is physically associated with nucleosome complexes. a MeCP2 antibody immunoprecipitated proteins from mouse OE nuclear extract in SDS gel visualized with Coomassie blue. Nuclear extract is loaded as input; rabbit IgG as a negative control. Star is around 25–30 kDa. b Benzonase treated nuclear extracts were immunoprecipitated either with anti-MeCP2 antibody or anti-histone H1 antibody. Samples of input, IgG and immunoprecipitates were analyzed with western blotting for histone H1 or MeCP2. c Benzonase treated nuclear extracts were immunoprecipitated with a MeCP2 antibody specific to its C-terminus. Input, IgG control and immunoprecipitates were analyzed with Western blotting for the presence of histone H3 and H4. d Z-transformed aggregate plot of the average tag density of MeCP2 binding sites (hotspot, green) at chr19 occupied by: Nucleosome occupancies (gray) and histone H1 (purple). e Z-transformed aggregate plot of the average tag density of MNase-seq (hotspot, gray) at chr19 occupied by: MeCP2 (green) and histone H1 (purple). f Genome-wide inter-correlation among Input, histone H1 ChIP-seq, MeCP2 ChIP-seq, and MNase-seq (binning size = 150 bp). Number in the square indicates the Pearson correlation coefficient. Source data are provided as a Source data file ( b and c ). The shaded areas are up to ±S.D. from the average profile ( d and e ).

    Article Snippet: The pull-down complex was boiled in 2x SDS buffer to elute protein for SDS-PAGE gel, and visualized by Coomassie staining.

    Techniques: Immunoprecipitation, SDS-Gel, Negative Control, Western Blot, Transformation Assay, Binding Assay, Genome Wide, Chromatin Immunoprecipitation

    Affinity of HscA and Ssq1 for protein substrate (IscU/Isu1) in the presence of ATP or ADP. ( left ) IscU-GST (15 μM) or GST (15 μM) were incubated in the presence of ATP or ADP (4 mM) with increasing concentrations of HscA, as indicated. Glutathione resin was added to pull-down GST and associated proteins, which were then separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and stained with Coomassie Blue. “M” indicates lanes having molecular weight markers; controls of loading are shown in Supplementary Figure S4 . Bound HscA was quantitated by densitometry. Values were plotted as relative units (r.u.) with maximal signal for HscA set as 1. Curves represent best fit of the data to the Michaelis-Menten hyperbolic equation. The Km value obtained in the presence of ADP (Km ADP ) is listed. Error bars represent SD for three independent measurements. ( right ) Isu1-GST or GST (30 μM) were incubated in the presence of ATP or ADP (4 mM) with increasing concentrations of Ssq1. Procedure was as described above for HscA/IscU.

    Journal: International Journal of Molecular Sciences

    Article Title: Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron–Sulfur Cluster Biogenesis

    doi: 10.3390/ijms21093326

    Figure Lengend Snippet: Affinity of HscA and Ssq1 for protein substrate (IscU/Isu1) in the presence of ATP or ADP. ( left ) IscU-GST (15 μM) or GST (15 μM) were incubated in the presence of ATP or ADP (4 mM) with increasing concentrations of HscA, as indicated. Glutathione resin was added to pull-down GST and associated proteins, which were then separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and stained with Coomassie Blue. “M” indicates lanes having molecular weight markers; controls of loading are shown in Supplementary Figure S4 . Bound HscA was quantitated by densitometry. Values were plotted as relative units (r.u.) with maximal signal for HscA set as 1. Curves represent best fit of the data to the Michaelis-Menten hyperbolic equation. The Km value obtained in the presence of ADP (Km ADP ) is listed. Error bars represent SD for three independent measurements. ( right ) Isu1-GST or GST (30 μM) were incubated in the presence of ATP or ADP (4 mM) with increasing concentrations of Ssq1. Procedure was as described above for HscA/IscU.

    Article Snippet: After the wash steps with PD buffer, proteins bound to the beads were incubated with 20 μL of 4-fold concentrated Laemmli sample buffer for 10 min at 100 °C and aliquots were loaded on SDS-PAGE and visualized by Coomassie Blue staining.

    Techniques: Incubation, Polyacrylamide Gel Electrophoresis, SDS Page, Staining, Molecular Weight

    Affinity of HscA/Ssq1 for HscB/Hsc20 cochaperones. ( A ) Stimulation of HscA/Ssq1 ATPase activity at increasing concentrations of cochaperones. ATPase activities were measured with radioactive assay as described in Figure 2 B but with increasing concentrations of HscB or Hsc20, as indicated. Curves represent best fit of the data to the Michaelis-Menten equation. Error bars represent SD for three independent measurements. ( B ) Stimulation of HscA/Ssq1 interaction with IscU/Isu1-GST in the presence of cochaperones and ATP. ( left ) IscU-GST (30 μM) was incubated with HscA (30 μM) in the presence of ATP (4 mM) and increasing concentrations of HscB (0.01; 0.02; 0.06; 0.125; 0.25; 0.5; 1 μM). Glutathione resin was added to pull-down GST and associated proteins, which were separated by SDS-PAGE and stained with Coomassie Blue. Lane 9: a control where IscU-GST was replaced by GST and 1 μM HscB + 30 μM HscA were present in the reaction mixture (“K”). Lanes 10-12: Five percent of the reaction mixtures that were run in lanes 1, 9 and 8, were run as loading control (Load 5%: L1, L9, L8). M: lane having molecular weight markers. Bound HscA was quantitated by densitometry. Values were plotted as relative units (r.u.) with maximal signal for HscA set at 1. Curve represent best fit of the data to the Michaelis-Menten equation. ( right ) Isu1-GST (2.5 μM) was incubated with Ssq1 (4 μM) in the presence of ATP (4 mM) and increasing concentrations of Hsc20 (0.0025; 0.005; 0.01; 0.02; 0.06; 0.125; 0.25 μM). Glutathione resin was added to pull-down GST and associated proteins, which were separated by SDS-PAGE and stained with Coomassie Blue. Lane 9: control where Isu1-GST was replaced by GST and 0.25 μM Hsc20 + 4 μM Ssq1 were added to the reaction mixture (“K”). Lanes 10–12: Five percent of the reaction mixtures run in lanes 1, 8 and 9, were run as loading controls (Load 5%: L1, L8, L9). M: lane having molecular weight markers. Bound Ssq1 was quantitated by densitometry. Values were plotted as relative units (r.u.) with maximal signal for Ssq1 set at 1. Curve represent best fit of the data to the Michaelis-Menten equation.

    Journal: International Journal of Molecular Sciences

    Article Title: Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron–Sulfur Cluster Biogenesis

    doi: 10.3390/ijms21093326

    Figure Lengend Snippet: Affinity of HscA/Ssq1 for HscB/Hsc20 cochaperones. ( A ) Stimulation of HscA/Ssq1 ATPase activity at increasing concentrations of cochaperones. ATPase activities were measured with radioactive assay as described in Figure 2 B but with increasing concentrations of HscB or Hsc20, as indicated. Curves represent best fit of the data to the Michaelis-Menten equation. Error bars represent SD for three independent measurements. ( B ) Stimulation of HscA/Ssq1 interaction with IscU/Isu1-GST in the presence of cochaperones and ATP. ( left ) IscU-GST (30 μM) was incubated with HscA (30 μM) in the presence of ATP (4 mM) and increasing concentrations of HscB (0.01; 0.02; 0.06; 0.125; 0.25; 0.5; 1 μM). Glutathione resin was added to pull-down GST and associated proteins, which were separated by SDS-PAGE and stained with Coomassie Blue. Lane 9: a control where IscU-GST was replaced by GST and 1 μM HscB + 30 μM HscA were present in the reaction mixture (“K”). Lanes 10-12: Five percent of the reaction mixtures that were run in lanes 1, 9 and 8, were run as loading control (Load 5%: L1, L9, L8). M: lane having molecular weight markers. Bound HscA was quantitated by densitometry. Values were plotted as relative units (r.u.) with maximal signal for HscA set at 1. Curve represent best fit of the data to the Michaelis-Menten equation. ( right ) Isu1-GST (2.5 μM) was incubated with Ssq1 (4 μM) in the presence of ATP (4 mM) and increasing concentrations of Hsc20 (0.0025; 0.005; 0.01; 0.02; 0.06; 0.125; 0.25 μM). Glutathione resin was added to pull-down GST and associated proteins, which were separated by SDS-PAGE and stained with Coomassie Blue. Lane 9: control where Isu1-GST was replaced by GST and 0.25 μM Hsc20 + 4 μM Ssq1 were added to the reaction mixture (“K”). Lanes 10–12: Five percent of the reaction mixtures run in lanes 1, 8 and 9, were run as loading controls (Load 5%: L1, L8, L9). M: lane having molecular weight markers. Bound Ssq1 was quantitated by densitometry. Values were plotted as relative units (r.u.) with maximal signal for Ssq1 set at 1. Curve represent best fit of the data to the Michaelis-Menten equation.

    Article Snippet: After the wash steps with PD buffer, proteins bound to the beads were incubated with 20 μL of 4-fold concentrated Laemmli sample buffer for 10 min at 100 °C and aliquots were loaded on SDS-PAGE and visualized by Coomassie Blue staining.

    Techniques: Activity Assay, Radioactivity, Incubation, SDS Page, Staining, Molecular Weight

    SDS-PAGE of PARL with TAMRA probe. To determine orientation of PARL in the proteoliposomes, PARL in PLs was incubated with TAMRA and then separated on a 14% SDS-PAGE gel. The fluorescent TAMRA probe was visualized using an imager (left) and also stained with Coomassie blue (right).

    Journal: bioRxiv

    Article Title: Insights into the catalytic properties of the mitochondrial rhomboid protease PARL

    doi: 10.1101/2020.07.27.224220

    Figure Lengend Snippet: SDS-PAGE of PARL with TAMRA probe. To determine orientation of PARL in the proteoliposomes, PARL in PLs was incubated with TAMRA and then separated on a 14% SDS-PAGE gel. The fluorescent TAMRA probe was visualized using an imager (left) and also stained with Coomassie blue (right).

    Article Snippet: The reaction was quenched with addition of SDS-containing sample buffer and the protein samples were visualized with SDS-PAGE followed by fluorescent gel scanning and Coomassie staining.

    Techniques: SDS Page, Incubation, Staining

    Identification of a CRMP2/syntaxin 1A interaction. (A) Coomassie brilliant blue staining of an eluate from CRMP2 immunoprecipitation (or isotype-specific control IgG) in the presence of 10 µM t-CNRP1 or 0.1% DMSO as a control. The band corresponding to CRMP2 is indicated. (B) Venn diagram of the proteins identified in the indicated immunoprecipitations. (C) Bar graph showing the number of peptides detected for syntaxin 1A in CRMP2 immunoprecipitates with 10 µM t-CNRP1 or 0.1% DMSO. (D) Far-Western assay on full-length CRMP2 tiled as 15-mer peptides with an increment of 5 amino acids. Syntaxin 1A binding to each peptide is shown as mean ± SEM ( n = 4). Strong syntaxin 1A binding was found for peptides #92 to 95 from CRMP2 whose sequence is indicated next to the bar graph. Representative dot blot fluorescence is shown for these peptides. (E) Representative immunoblot showing neurofibromin knockdown after Nf1 siRNA transfection in CAD cells. (F) Bar graph showing neurofibromin expression level relative to control siRNA transfection, mean ± SEM (n = 3). (G) Representative immunoblot showing syntaxin 1A binding to CRMP2 after neurofibromin knockdown in CAD cells. (H) Bar graph showing increased syntaxin 1A binding to CRMP2 after neurofibromin knockdown, mean ± SEM ( n = 3). (I) Representative immunoblot showing inhibition of syntaxin 1A binding to CRMP2 by 10 µM t-CNRP1 after neurofibromin knockdown, compared with 0.1% DMSO as a control. (J) Bar graph showing decreased syntaxin 1A binding to CRMP2 by 10 µM t-CNRP1 compared with 0.1% DMSO, mean ± SEM (n = 3). * P

    Journal: Pain

    Article Title: Dissecting the role of the CRMP2–neurofibromin complex on pain behaviors

    doi: 10.1097/j.pain.0000000000001026

    Figure Lengend Snippet: Identification of a CRMP2/syntaxin 1A interaction. (A) Coomassie brilliant blue staining of an eluate from CRMP2 immunoprecipitation (or isotype-specific control IgG) in the presence of 10 µM t-CNRP1 or 0.1% DMSO as a control. The band corresponding to CRMP2 is indicated. (B) Venn diagram of the proteins identified in the indicated immunoprecipitations. (C) Bar graph showing the number of peptides detected for syntaxin 1A in CRMP2 immunoprecipitates with 10 µM t-CNRP1 or 0.1% DMSO. (D) Far-Western assay on full-length CRMP2 tiled as 15-mer peptides with an increment of 5 amino acids. Syntaxin 1A binding to each peptide is shown as mean ± SEM ( n = 4). Strong syntaxin 1A binding was found for peptides #92 to 95 from CRMP2 whose sequence is indicated next to the bar graph. Representative dot blot fluorescence is shown for these peptides. (E) Representative immunoblot showing neurofibromin knockdown after Nf1 siRNA transfection in CAD cells. (F) Bar graph showing neurofibromin expression level relative to control siRNA transfection, mean ± SEM (n = 3). (G) Representative immunoblot showing syntaxin 1A binding to CRMP2 after neurofibromin knockdown in CAD cells. (H) Bar graph showing increased syntaxin 1A binding to CRMP2 after neurofibromin knockdown, mean ± SEM ( n = 3). (I) Representative immunoblot showing inhibition of syntaxin 1A binding to CRMP2 by 10 µM t-CNRP1 after neurofibromin knockdown, compared with 0.1% DMSO as a control. (J) Bar graph showing decreased syntaxin 1A binding to CRMP2 by 10 µM t-CNRP1 compared with 0.1% DMSO, mean ± SEM (n = 3). * P

    Article Snippet: Gels were stained with Coomassie brilliant blue (Cat# 1610436; Biorad, Hercules, CA).

    Techniques: Staining, Immunoprecipitation, Western Blot, Binding Assay, Sequencing, Dot Blot, Fluorescence, Transfection, Expressing, Inhibition

    SDS-PAGE gels of MBP, AtBBD1 and AtBBD2 Proteins. ( A ) SDS-PAGE of MBP-BBD1 and MBP-BBD2 proteins in pellets and soluble fractions. Total proteins were electrophoresed on a 12% SDS-PAGE gel and stained with Coomassie blue R-250. Lane M, protein marker; 1, uninduced cells; 2, induced cells. Target proteins are indicated by red arrowheads. ( B ) SDS-PAGE of the purified MBP, MBP-BBD1 and MBP-BBD2 proteins. Purified proteins were electrophoresed on a 12% SDS-PAGE gel and stained with Coomassie blue R-250. Purified target proteins are indicated by red arrowheads. Lanes M, protein marker; 1, purified MBP; 2, purified MBP-BBD1; 3, purified MBP-BBD2.

    Journal: Molecules

    Article Title: Phylogenetic Analysis and In Vitro Bifunctional Nuclease Assay of Arabidopsis BBD1 and BBD2

    doi: 10.3390/molecules25092169

    Figure Lengend Snippet: SDS-PAGE gels of MBP, AtBBD1 and AtBBD2 Proteins. ( A ) SDS-PAGE of MBP-BBD1 and MBP-BBD2 proteins in pellets and soluble fractions. Total proteins were electrophoresed on a 12% SDS-PAGE gel and stained with Coomassie blue R-250. Lane M, protein marker; 1, uninduced cells; 2, induced cells. Target proteins are indicated by red arrowheads. ( B ) SDS-PAGE of the purified MBP, MBP-BBD1 and MBP-BBD2 proteins. Purified proteins were electrophoresed on a 12% SDS-PAGE gel and stained with Coomassie blue R-250. Purified target proteins are indicated by red arrowheads. Lanes M, protein marker; 1, purified MBP; 2, purified MBP-BBD1; 3, purified MBP-BBD2.

    Article Snippet: Samples of eluted proteins (15 μL) were electrophoresed on 12% SDS-polyacrylamide gels (SDS-PAGE) and visualized with Coomassie blue staining.

    Techniques: SDS Page, Staining, Marker, Purification

    Identification of XDH as a protein marker associated with the bulk of microRNAs in commercial milk. (a) Proteins extracted from the pellets obtained by ultracentrifugation of 100 mL of commercial milk were analysed by SDS-PAGE and Coomassie blue staining. The bands corresponding to those enriched in low-speed ultracentrifugation pellets were excised and submitted to LC-MS/MS analysis. The most enriched proteins in each pellet are displayed, based on the number of exclusive peptide count, percentage coverage of the protein and molecular weight match to the respective band. (b) The XDH protein content of the four ultracentrifugation pellets was assessed by Western blot (most representative of the three replicates, upper panel) and quantitative densitometry (lower panel) analyses (mean ± SD; n = 3). Western blot results are expressed as a percentage (%; mean ± SD) of the XDH proteins present in the four pellets. The statistical significance of the differences observed was assessed by an RM one-way ANOVA with Geisser–Greenhouse correction coupled with a post-hoc comparison of the means with Tukey’s correction with p

    Journal: Journal of Extracellular Vesicles

    Article Title: A subset of extracellular vesicles carries the bulk of microRNAs in commercial dairy cow’s milk

    doi: 10.1080/20013078.2017.1401897

    Figure Lengend Snippet: Identification of XDH as a protein marker associated with the bulk of microRNAs in commercial milk. (a) Proteins extracted from the pellets obtained by ultracentrifugation of 100 mL of commercial milk were analysed by SDS-PAGE and Coomassie blue staining. The bands corresponding to those enriched in low-speed ultracentrifugation pellets were excised and submitted to LC-MS/MS analysis. The most enriched proteins in each pellet are displayed, based on the number of exclusive peptide count, percentage coverage of the protein and molecular weight match to the respective band. (b) The XDH protein content of the four ultracentrifugation pellets was assessed by Western blot (most representative of the three replicates, upper panel) and quantitative densitometry (lower panel) analyses (mean ± SD; n = 3). Western blot results are expressed as a percentage (%; mean ± SD) of the XDH proteins present in the four pellets. The statistical significance of the differences observed was assessed by an RM one-way ANOVA with Geisser–Greenhouse correction coupled with a post-hoc comparison of the means with Tukey’s correction with p

    Article Snippet: After the run, the gels were stained with Coomassie blue (Coomassie Brilliant Blue R-250 Staining Solution; Bio-Rad Laboratories, Hercules, CA, USA; 0.2%) in 40% methanol and 10% acetic acid for 1 h and destained overnight with a destaining solution composed of 10% methanol and 10% glacial acetic acid.

    Techniques: Marker, SDS Page, Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Molecular Weight, Western Blot

    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