coomassie brilliant blue r Search Results


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  • 95
    Millipore coomassie brilliant blue r 250
    SDS-PAGE comparison of the NISTmAb, deglycosylated NISTmAb and the eNISTmAb. Two and half microgram of the NISTmAb (lane 1), deglycosylated NISTmAb (lane 2) and eNISTmAb (lane 3) were separated on a 12% SDS-PAGE followed by staining with <t>Coomassie</t> Brilliant Blue R-250. Lane 4, molecular weight marker (kDa); HC, heavy chain; LC, light chain, DG HC, deglycosylated NISTmAb heavy chain.
    Coomassie Brilliant Blue R 250, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 2646 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 95 stars, based on 2646 article reviews
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    coomassie brilliant blue r 250 - by Bioz Stars, 2020-02
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    90
    Thermo Fisher coomassie brilliant blue r 250 cbb
    SDS-PAGE analysis of a the purified native ckGL from C. kessleri and b recombinant ckGL (rckGL) produced in E. coli BL21 . Lane M, protein molecular mass markers; lane 1, purified enzyme (2.9 μg protein); lane 2, recombinant enzyme in TF-ckGL form (0.1 μg); lane 3, rckGL (0.1 μg) produced from TF-ckGL by digestion with Factor Xa. The SDS-PAGE gels a and b were stained with <t>Coomassie</t> Brilliant Blue R-250 and Simply Blue Safe Stain (G-250), respectively
    Coomassie Brilliant Blue R 250 Cbb, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 33 article reviews
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    90
    Bio-Rad coomassie blue r 250
    <t>Coomassie</t> 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.
    Coomassie Blue R 250, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1038 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    coomassie blue r 250 - by Bioz Stars, 2020-02
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    90
    Bio-Rad coomassie brilliant blue
    Identification of a CRMP2/syntaxin 1A interaction. (A) <t>Coomassie</t> 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
    Coomassie Brilliant Blue, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 2639 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    coomassie brilliant blue - by Bioz Stars, 2020-02
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    93
    Promega coomassie blue r 250
    Identification of a CRMP2/syntaxin 1A interaction. (A) <t>Coomassie</t> 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
    Coomassie Blue R 250, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 31 article reviews
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    coomassie blue r 250 - by Bioz Stars, 2020-02
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    99
    Millipore coomassie blue r 250
    Expression of fusion protein in E. coli . The figure shows a glycine-SDS-PAGE gel stained with <t>Coomassie</t> blue R-250 (A) and the results of an ELISA (B) for total cell proteins obtained from the E. coli Origami strain carrying plasmid pCR04 before induction
    Coomassie Blue R 250, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 869 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Koma Biotech coomassie blue r 250
    Expression of fusion protein in E. coli . The figure shows a glycine-SDS-PAGE gel stained with <t>Coomassie</t> blue R-250 (A) and the results of an ELISA (B) for total cell proteins obtained from the E. coli Origami strain carrying plasmid pCR04 before induction
    Coomassie Blue R 250, supplied by Koma Biotech, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 6 article reviews
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    coomassie blue r 250 - by Bioz Stars, 2020-02
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    94
    Thermo Fisher coomassie blue r 250
    Expression of fusion protein in E. coli . The figure shows a glycine-SDS-PAGE gel stained with <t>Coomassie</t> blue R-250 (A) and the results of an ELISA (B) for total cell proteins obtained from the E. coli Origami strain carrying plasmid pCR04 before induction
    Coomassie Blue R 250, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 182 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Merck & Co coomassie blue r 250
    Expression of fusion protein in E. coli . The figure shows a glycine-SDS-PAGE gel stained with <t>Coomassie</t> blue R-250 (A) and the results of an ELISA (B) for total cell proteins obtained from the E. coli Origami strain carrying plasmid pCR04 before induction
    Coomassie Blue R 250, supplied by Merck & Co, used in various techniques. Bioz Stars score: 89/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    GE Healthcare coomassie brilliant blue r
    SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with <t>Coomassie</t> blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).
    Coomassie Brilliant Blue R, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Biomol GmbH coomassie blue r 250
    SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with <t>Coomassie</t> blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).
    Coomassie Blue R 250, supplied by Biomol GmbH, used in various techniques. Bioz Stars score: 89/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Valiant coomassie brilliant blue r
    SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with <t>Coomassie</t> blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).
    Coomassie Brilliant Blue R, supplied by Valiant, used in various techniques. Bioz Stars score: 78/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Merck KGaA coomassie blue r 250
    SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with <t>Coomassie</t> blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).
    Coomassie Blue R 250, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 34 article reviews
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    92
    Fisher Scientific coomassie blue r 250
    SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with <t>Coomassie</t> blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).
    Coomassie Blue R 250, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 92/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Teknova coomassie blue r 250
    SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with <t>Coomassie</t> blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).
    Coomassie Blue R 250, supplied by Teknova, used in various techniques. Bioz Stars score: 89/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    coomassie blue r 250 - by Bioz Stars, 2020-02
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    89
    Amresco coomassie blue r 250
    SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with <t>Coomassie</t> blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).
    Coomassie Blue R 250, supplied by Amresco, used in various techniques. Bioz Stars score: 89/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Sangon Biotech coomassie blue r 250
    SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with <t>Coomassie</t> blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).
    Coomassie Blue R 250, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    coomassie blue r 250 - by Bioz Stars, 2020-02
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    92
    Beijing Solarbio Science coomassie blue r 250
    SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with <t>Coomassie</t> blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).
    Coomassie Blue R 250, supplied by Beijing Solarbio Science, used in various techniques. Bioz Stars score: 92/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    coomassie blue r 250 - by Bioz Stars, 2020-02
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    99
    GE Healthcare coomassie brilliant blue r 350
    Proteomic and bioinformatic analysis of LGR5 knockdown in SH-SY5Y cells. (A) <t>Coomassie</t> brilliant blue R-350 stained gels after 2D-PAGE. Protein spots in SH-SY5Y cells after treatment with control siRNA or LGR5 siRNA. Common landmarks of protein spots in the SH-SY5Y cells after treatment with control siRNA and LGR5 siRNA are indicated. (B) Identification of protein spots. Protein spots exhibiting a change greater than twofold in the expression in SH-SY5Y cells treated with LGR5 siRNA compared to control cells. (C) Detailed information of the 12 selected protein spots. (D) Proteins with increased and decreased expression after LGR5 inhibition compared to control-treated cells. (E) Identification of different expression levels of hnRNPA2B1 and hnRNPH3 in SH-SY5Y cells after treatment with LGR5 siRNA or control siRNA by western blotting. (F) LGR5-associated protein-protein interaction network. An LGR5-associated protein-protein interaction network was constructed using a bioinformatics approach. Circles indicate LGR5 and the 12 proteins found to be associated with LGR5 in neuroblastoma cells by a proteomics approach. The thickness of the line between any two proteins represents the degree of confidence in the interaction between the two proteins, with thicker lines indicating higher confidence (left upper). The types of interactions between proteins are represented by action types and effects (right lower).
    Coomassie Brilliant Blue R 350, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 58 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Merck & Co coomassie brilliant blue r 350
    Proteomic and bioinformatic analysis of LGR5 knockdown in SH-SY5Y cells. (A) <t>Coomassie</t> brilliant blue R-350 stained gels after 2D-PAGE. Protein spots in SH-SY5Y cells after treatment with control siRNA or LGR5 siRNA. Common landmarks of protein spots in the SH-SY5Y cells after treatment with control siRNA and LGR5 siRNA are indicated. (B) Identification of protein spots. Protein spots exhibiting a change greater than twofold in the expression in SH-SY5Y cells treated with LGR5 siRNA compared to control cells. (C) Detailed information of the 12 selected protein spots. (D) Proteins with increased and decreased expression after LGR5 inhibition compared to control-treated cells. (E) Identification of different expression levels of hnRNPA2B1 and hnRNPH3 in SH-SY5Y cells after treatment with LGR5 siRNA or control siRNA by western blotting. (F) LGR5-associated protein-protein interaction network. An LGR5-associated protein-protein interaction network was constructed using a bioinformatics approach. Circles indicate LGR5 and the 12 proteins found to be associated with LGR5 in neuroblastoma cells by a proteomics approach. The thickness of the line between any two proteins represents the degree of confidence in the interaction between the two proteins, with thicker lines indicating higher confidence (left upper). The types of interactions between proteins are represented by action types and effects (right lower).
    Coomassie Brilliant Blue R 350, supplied by Merck & Co, used in various techniques. Bioz Stars score: 78/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Millipore coomassie brilliant blue r 20
    Proteomic and bioinformatic analysis of LGR5 knockdown in SH-SY5Y cells. (A) <t>Coomassie</t> brilliant blue R-350 stained gels after 2D-PAGE. Protein spots in SH-SY5Y cells after treatment with control siRNA or LGR5 siRNA. Common landmarks of protein spots in the SH-SY5Y cells after treatment with control siRNA and LGR5 siRNA are indicated. (B) Identification of protein spots. Protein spots exhibiting a change greater than twofold in the expression in SH-SY5Y cells treated with LGR5 siRNA compared to control cells. (C) Detailed information of the 12 selected protein spots. (D) Proteins with increased and decreased expression after LGR5 inhibition compared to control-treated cells. (E) Identification of different expression levels of hnRNPA2B1 and hnRNPH3 in SH-SY5Y cells after treatment with LGR5 siRNA or control siRNA by western blotting. (F) LGR5-associated protein-protein interaction network. An LGR5-associated protein-protein interaction network was constructed using a bioinformatics approach. Circles indicate LGR5 and the 12 proteins found to be associated with LGR5 in neuroblastoma cells by a proteomics approach. The thickness of the line between any two proteins represents the degree of confidence in the interaction between the two proteins, with thicker lines indicating higher confidence (left upper). The types of interactions between proteins are represented by action types and effects (right lower).
    Coomassie Brilliant Blue R 20, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore coomassie brilliant blue r 230
    Proteomic and bioinformatic analysis of LGR5 knockdown in SH-SY5Y cells. (A) <t>Coomassie</t> brilliant blue R-350 stained gels after 2D-PAGE. Protein spots in SH-SY5Y cells after treatment with control siRNA or LGR5 siRNA. Common landmarks of protein spots in the SH-SY5Y cells after treatment with control siRNA and LGR5 siRNA are indicated. (B) Identification of protein spots. Protein spots exhibiting a change greater than twofold in the expression in SH-SY5Y cells treated with LGR5 siRNA compared to control cells. (C) Detailed information of the 12 selected protein spots. (D) Proteins with increased and decreased expression after LGR5 inhibition compared to control-treated cells. (E) Identification of different expression levels of hnRNPA2B1 and hnRNPH3 in SH-SY5Y cells after treatment with LGR5 siRNA or control siRNA by western blotting. (F) LGR5-associated protein-protein interaction network. An LGR5-associated protein-protein interaction network was constructed using a bioinformatics approach. Circles indicate LGR5 and the 12 proteins found to be associated with LGR5 in neuroblastoma cells by a proteomics approach. The thickness of the line between any two proteins represents the degree of confidence in the interaction between the two proteins, with thicker lines indicating higher confidence (left upper). The types of interactions between proteins are represented by action types and effects (right lower).
    Coomassie Brilliant Blue R 230, supplied by Millipore, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    coomassie brilliant blue r 230 - by Bioz Stars, 2020-02
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    80
    Abcam coomassie brilliant blue r 250 staining
    Proteomic and bioinformatic analysis of LGR5 knockdown in SH-SY5Y cells. (A) <t>Coomassie</t> brilliant blue R-350 stained gels after 2D-PAGE. Protein spots in SH-SY5Y cells after treatment with control siRNA or LGR5 siRNA. Common landmarks of protein spots in the SH-SY5Y cells after treatment with control siRNA and LGR5 siRNA are indicated. (B) Identification of protein spots. Protein spots exhibiting a change greater than twofold in the expression in SH-SY5Y cells treated with LGR5 siRNA compared to control cells. (C) Detailed information of the 12 selected protein spots. (D) Proteins with increased and decreased expression after LGR5 inhibition compared to control-treated cells. (E) Identification of different expression levels of hnRNPA2B1 and hnRNPH3 in SH-SY5Y cells after treatment with LGR5 siRNA or control siRNA by western blotting. (F) LGR5-associated protein-protein interaction network. An LGR5-associated protein-protein interaction network was constructed using a bioinformatics approach. Circles indicate LGR5 and the 12 proteins found to be associated with LGR5 in neuroblastoma cells by a proteomics approach. The thickness of the line between any two proteins represents the degree of confidence in the interaction between the two proteins, with thicker lines indicating higher confidence (left upper). The types of interactions between proteins are represented by action types and effects (right lower).
    Coomassie Brilliant Blue R 250 Staining, supplied by Abcam, used in various techniques. Bioz Stars score: 80/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Thermo Fisher coomassie blue r 250 solution
    Proteomic and bioinformatic analysis of LGR5 knockdown in SH-SY5Y cells. (A) <t>Coomassie</t> brilliant blue R-350 stained gels after 2D-PAGE. Protein spots in SH-SY5Y cells after treatment with control siRNA or LGR5 siRNA. Common landmarks of protein spots in the SH-SY5Y cells after treatment with control siRNA and LGR5 siRNA are indicated. (B) Identification of protein spots. Protein spots exhibiting a change greater than twofold in the expression in SH-SY5Y cells treated with LGR5 siRNA compared to control cells. (C) Detailed information of the 12 selected protein spots. (D) Proteins with increased and decreased expression after LGR5 inhibition compared to control-treated cells. (E) Identification of different expression levels of hnRNPA2B1 and hnRNPH3 in SH-SY5Y cells after treatment with LGR5 siRNA or control siRNA by western blotting. (F) LGR5-associated protein-protein interaction network. An LGR5-associated protein-protein interaction network was constructed using a bioinformatics approach. Circles indicate LGR5 and the 12 proteins found to be associated with LGR5 in neuroblastoma cells by a proteomics approach. The thickness of the line between any two proteins represents the degree of confidence in the interaction between the two proteins, with thicker lines indicating higher confidence (left upper). The types of interactions between proteins are represented by action types and effects (right lower).
    Coomassie Blue R 250 Solution, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Solubilized MSC and SB623-derived ECM analyzed by SDS-PAGE. SDS/urea-soluble SB623-derived ECM (SB) and corresponding MSC. M: molecular weight markers. SDS/urea samples were precipitated, re-suspended in 2X loading buffer, loaded on a 1.5-mm 4–20% Tris-acetate gel, electrophoresed and stained with <t>Coomassie</t> Blue R-250.
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    Solubilized MSC and SB623-derived ECM analyzed by SDS-PAGE. SDS/urea-soluble SB623-derived ECM (SB) and corresponding MSC. M: molecular weight markers. SDS/urea samples were precipitated, re-suspended in 2X loading buffer, loaded on a 1.5-mm 4–20% Tris-acetate gel, electrophoresed and stained with <t>Coomassie</t> Blue R-250.
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    Solubilized MSC and SB623-derived ECM analyzed by SDS-PAGE. SDS/urea-soluble SB623-derived ECM (SB) and corresponding MSC. M: molecular weight markers. SDS/urea samples were precipitated, re-suspended in 2X loading buffer, loaded on a 1.5-mm 4–20% Tris-acetate gel, electrophoresed and stained with <t>Coomassie</t> Blue R-250.
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    Solubilized MSC and SB623-derived ECM analyzed by SDS-PAGE. SDS/urea-soluble SB623-derived ECM (SB) and corresponding MSC. M: molecular weight markers. SDS/urea samples were precipitated, re-suspended in 2X loading buffer, loaded on a 1.5-mm 4–20% Tris-acetate gel, electrophoresed and stained with <t>Coomassie</t> Blue R-250.
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    Solubilized MSC and SB623-derived ECM analyzed by SDS-PAGE. SDS/urea-soluble SB623-derived ECM (SB) and corresponding MSC. M: molecular weight markers. SDS/urea samples were precipitated, re-suspended in 2X loading buffer, loaded on a 1.5-mm 4–20% Tris-acetate gel, electrophoresed and stained with <t>Coomassie</t> Blue R-250.
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    Image Search Results


    SDS-PAGE comparison of the NISTmAb, deglycosylated NISTmAb and the eNISTmAb. Two and half microgram of the NISTmAb (lane 1), deglycosylated NISTmAb (lane 2) and eNISTmAb (lane 3) were separated on a 12% SDS-PAGE followed by staining with Coomassie Brilliant Blue R-250. Lane 4, molecular weight marker (kDa); HC, heavy chain; LC, light chain, DG HC, deglycosylated NISTmAb heavy chain.

    Journal: mAbs

    Article Title: Platform development for expression and purification of stable isotope labeled monoclonal antibodies in Escherichia coli

    doi: 10.1080/19420862.2018.1496879

    Figure Lengend Snippet: SDS-PAGE comparison of the NISTmAb, deglycosylated NISTmAb and the eNISTmAb. Two and half microgram of the NISTmAb (lane 1), deglycosylated NISTmAb (lane 2) and eNISTmAb (lane 3) were separated on a 12% SDS-PAGE followed by staining with Coomassie Brilliant Blue R-250. Lane 4, molecular weight marker (kDa); HC, heavy chain; LC, light chain, DG HC, deglycosylated NISTmAb heavy chain.

    Article Snippet: Purified fractions were analyzed by SDS-PAGE and visualized by staining with Coomassie Brilliant Blue R-250 (Sigma-Aldrich, B7920).

    Techniques: SDS Page, Staining, Molecular Weight, Marker

    The effect of the GTG to GTT substitution at the rare initiation site on the expression of the eNISTmAb. SDS-PAGE analysis of the eNISTmAb after purification on Protein-A. Lane 1 is the purified protein after expression from the clone in which GTG encodes for V 214 . Lane 2 is the purified protein after expression from the clone in which GTT encodes for V 214 . Five micrograms of each protein were separated on a 12% SDS-PAGE followed by staining with Coomassie Brilliant Blue R-250. Lane 3, molecular weight marker (kDa); HC, heavy chain; LC, light chain, *, truncated heavy chain.

    Journal: mAbs

    Article Title: Platform development for expression and purification of stable isotope labeled monoclonal antibodies in Escherichia coli

    doi: 10.1080/19420862.2018.1496879

    Figure Lengend Snippet: The effect of the GTG to GTT substitution at the rare initiation site on the expression of the eNISTmAb. SDS-PAGE analysis of the eNISTmAb after purification on Protein-A. Lane 1 is the purified protein after expression from the clone in which GTG encodes for V 214 . Lane 2 is the purified protein after expression from the clone in which GTT encodes for V 214 . Five micrograms of each protein were separated on a 12% SDS-PAGE followed by staining with Coomassie Brilliant Blue R-250. Lane 3, molecular weight marker (kDa); HC, heavy chain; LC, light chain, *, truncated heavy chain.

    Article Snippet: Purified fractions were analyzed by SDS-PAGE and visualized by staining with Coomassie Brilliant Blue R-250 (Sigma-Aldrich, B7920).

    Techniques: Expressing, SDS Page, Purification, Staining, Molecular Weight, Marker

    SDS-PAGE analysis of eNISTmAb purification steps. SDS-PAGE analysis of the eNISTmAb after purification on Protein-A (lane 1) or CH1 (lane 2) column and after SEC purification of the eluted proteins from the Protein-A column (lane 3). NISTmAb was used as a reference (lane 4). Five micrograms of each protein were separated on a 10% SDS-PAGE followed by staining with Coomassie Brilliant Blue R-250. Lane 5, molecular weight marker (kDa); HC, heavy chain; LC, light chain, *, truncated heavy chain.

    Journal: mAbs

    Article Title: Platform development for expression and purification of stable isotope labeled monoclonal antibodies in Escherichia coli

    doi: 10.1080/19420862.2018.1496879

    Figure Lengend Snippet: SDS-PAGE analysis of eNISTmAb purification steps. SDS-PAGE analysis of the eNISTmAb after purification on Protein-A (lane 1) or CH1 (lane 2) column and after SEC purification of the eluted proteins from the Protein-A column (lane 3). NISTmAb was used as a reference (lane 4). Five micrograms of each protein were separated on a 10% SDS-PAGE followed by staining with Coomassie Brilliant Blue R-250. Lane 5, molecular weight marker (kDa); HC, heavy chain; LC, light chain, *, truncated heavy chain.

    Article Snippet: Purified fractions were analyzed by SDS-PAGE and visualized by staining with Coomassie Brilliant Blue R-250 (Sigma-Aldrich, B7920).

    Techniques: SDS Page, Purification, Size-exclusion Chromatography, Staining, Molecular Weight, Marker

    The eNISTmAb forms a tetrameric complex. A) The eNISTmAb protein solution (300 μg) and molecular mass standards were subjected to Superdex-200 gel filtration analysis. The protein concentration in each eluted fraction was measured by ultraviolet absorption at 280nm. Blue, eNISTmAb; green, molecular mass standards. B) Proteins in aliquots (20 μL) from each indicated fraction were separated by electrophoresis through 4% – 20% SDS-PAGE and stained with Coomassie Brilliant Blue R-250. Lane1, molecular mass standards (kDa); lane 2, NISTmAb; lane 3, load on sample of eNISTmAb; lanes 4–12, column fractions. HC, heavy chain; LC, light chain.

    Journal: mAbs

    Article Title: Platform development for expression and purification of stable isotope labeled monoclonal antibodies in Escherichia coli

    doi: 10.1080/19420862.2018.1496879

    Figure Lengend Snippet: The eNISTmAb forms a tetrameric complex. A) The eNISTmAb protein solution (300 μg) and molecular mass standards were subjected to Superdex-200 gel filtration analysis. The protein concentration in each eluted fraction was measured by ultraviolet absorption at 280nm. Blue, eNISTmAb; green, molecular mass standards. B) Proteins in aliquots (20 μL) from each indicated fraction were separated by electrophoresis through 4% – 20% SDS-PAGE and stained with Coomassie Brilliant Blue R-250. Lane1, molecular mass standards (kDa); lane 2, NISTmAb; lane 3, load on sample of eNISTmAb; lanes 4–12, column fractions. HC, heavy chain; LC, light chain.

    Article Snippet: Purified fractions were analyzed by SDS-PAGE and visualized by staining with Coomassie Brilliant Blue R-250 (Sigma-Aldrich, B7920).

    Techniques: Filtration, Protein Concentration, Electrophoresis, SDS Page, Staining

    2-DE analysis of T. spiralis muscle larval surface proteins. 2-DE gel of surface proteins separated in the first dimension in the pH range 4–7 and then in the second dimension on a 12% polyacrylamide gel. The gel was stained with Coomassie blue R-250, molecular weight standard is on the left, and pI values are indicated. Protein spots selected for further analysis are numbered.

    Journal: Parasites & Vectors

    Article Title: Proteomic analysis of surface proteins of Trichinella spiralis muscle larvae by two-dimensional gel electrophoresis and mass spectrometry

    doi: 10.1186/1756-3305-6-355

    Figure Lengend Snippet: 2-DE analysis of T. spiralis muscle larval surface proteins. 2-DE gel of surface proteins separated in the first dimension in the pH range 4–7 and then in the second dimension on a 12% polyacrylamide gel. The gel was stained with Coomassie blue R-250, molecular weight standard is on the left, and pI values are indicated. Protein spots selected for further analysis are numbered.

    Article Snippet: After electrophoresis, the gel was stained with 0.25% Coomassie brilliant blue R-250 (Sigma, USA) for 4 h, and then bleached with the eluate (100 mL acetic acid, 50 mL ethanol, 850 mL dH2 O).

    Techniques: Staining, Molecular Weight

    SDS-PAGE analysis of a the purified native ckGL from C. kessleri and b recombinant ckGL (rckGL) produced in E. coli BL21 . Lane M, protein molecular mass markers; lane 1, purified enzyme (2.9 μg protein); lane 2, recombinant enzyme in TF-ckGL form (0.1 μg); lane 3, rckGL (0.1 μg) produced from TF-ckGL by digestion with Factor Xa. The SDS-PAGE gels a and b were stained with Coomassie Brilliant Blue R-250 and Simply Blue Safe Stain (G-250), respectively

    Journal: Applied Microbiology and Biotechnology

    Article Title: A novel galactolipase from a green microalga Chlorella kessleri: purification, characterization, molecular cloning, and heterologous expression

    doi: 10.1007/s00253-017-8713-7

    Figure Lengend Snippet: SDS-PAGE analysis of a the purified native ckGL from C. kessleri and b recombinant ckGL (rckGL) produced in E. coli BL21 . Lane M, protein molecular mass markers; lane 1, purified enzyme (2.9 μg protein); lane 2, recombinant enzyme in TF-ckGL form (0.1 μg); lane 3, rckGL (0.1 μg) produced from TF-ckGL by digestion with Factor Xa. The SDS-PAGE gels a and b were stained with Coomassie Brilliant Blue R-250 and Simply Blue Safe Stain (G-250), respectively

    Article Snippet: Gels were stained with Coomassie Brilliant Blue R-250 (CBB), Simply Blue Safe Stain (Thermo Fisher Scientific), or periodate-Schiff reagent (Irvin et al. ).

    Techniques: SDS Page, Purification, Recombinant, Produced, Staining

    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

    Heterologous expression of surface and secreted P. falciparum sexual-stage proteins. A , Coomassie brilliant blue R-250 staining of recombinant proteins resolved by reducing SDS-PAGE. Each protein has a C-terminal BAP and 6HIS and was purified from whole HEK293E cell supernatant by HisTrap Excel Ni-Sepharose column prior to visualization. B , Western blotting detection of hexahistidine tag affinity-purified proteins, which were resolved by reducing SDS-page, blotted, and probed with monoclonal anti-pentahistidine antibody. Each protein is shown with and without treatment by PNGaseF, an amidase which cleaves N -linked glycan residues. C , Western blotting detection of affinity-purified Pfs25 by 4B7 monoclonal antibody after SDS-PAGE under reducing and non-reducing conditions and nitrocellulose transfer.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title: Functional Characterization and Comparison of Plasmodium falciparum Proteins as Targets of Transmission-blocking Antibodies *

    doi: 10.1074/mcp.RA117.000036

    Figure Lengend Snippet: Heterologous expression of surface and secreted P. falciparum sexual-stage proteins. A , Coomassie brilliant blue R-250 staining of recombinant proteins resolved by reducing SDS-PAGE. Each protein has a C-terminal BAP and 6HIS and was purified from whole HEK293E cell supernatant by HisTrap Excel Ni-Sepharose column prior to visualization. B , Western blotting detection of hexahistidine tag affinity-purified proteins, which were resolved by reducing SDS-page, blotted, and probed with monoclonal anti-pentahistidine antibody. Each protein is shown with and without treatment by PNGaseF, an amidase which cleaves N -linked glycan residues. C , Western blotting detection of affinity-purified Pfs25 by 4B7 monoclonal antibody after SDS-PAGE under reducing and non-reducing conditions and nitrocellulose transfer.

    Article Snippet: Recombinant proteins were resolved by 4–20% Tris-Glycine gradient sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions and visualized by Coomassie brilliant blue R-250 (Bio-Rad, UK).

    Techniques: Expressing, Staining, Recombinant, SDS Page, Purification, Western Blot, Affinity Purification

    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

    Expression of fusion protein in E. coli . The figure shows a glycine-SDS-PAGE gel stained with Coomassie blue R-250 (A) and the results of an ELISA (B) for total cell proteins obtained from the E. coli Origami strain carrying plasmid pCR04 before induction

    Journal:

    Article Title: Heterologous Expression and Purification of Active Divercin V41, a Class IIa Bacteriocin Encoded by a Synthetic Gene in Escherichia coli

    doi: 10.1128/JB.186.13.4276-4284.2004

    Figure Lengend Snippet: Expression of fusion protein in E. coli . The figure shows a glycine-SDS-PAGE gel stained with Coomassie blue R-250 (A) and the results of an ELISA (B) for total cell proteins obtained from the E. coli Origami strain carrying plasmid pCR04 before induction

    Article Snippet: Proteins in glycine-SDS-PAGE gels were stained with Coomassie blue R-250 (Sigma).

    Techniques: Expressing, SDS Page, Staining, Enzyme-linked Immunosorbent Assay, Plasmid Preparation

    SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with Coomassie blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).

    Journal: Plant Physiology

    Article Title: Actin Depolymerization Affects Stress-Induced Translational Activity of Potato Tuber Tissue 1

    doi:

    Figure Lengend Snippet: SDS-PAGE and immunoblot analysis of the 4000 g pellet and supernatant (Supt) fractions from 2-h-wounded aerobic tuber extract. A, Polypeptides present in 20 μg of each fraction were resolved in a 15% gel stained with Coomassie blue R-250. Mobility of molecular size standards (Bio-Rad) and identification of major species are shown. Immunoblots of duplicate lanes on the same gel were electroblotted to a Hybond C nylon membrane and probed with either anti-actin monoclonal antibody (B) or anti-β-tubulin monoclonal antibody (C).

    Article Snippet: Twenty micrograms of protein was loaded per lane and either stained with Coomassie blue R-250 or electroblotted to Hybond C membranes (Amersham), as described by .

    Techniques: SDS Page, Staining, Western Blot

    Proteomic and bioinformatic analysis of LGR5 knockdown in SH-SY5Y cells. (A) Coomassie brilliant blue R-350 stained gels after 2D-PAGE. Protein spots in SH-SY5Y cells after treatment with control siRNA or LGR5 siRNA. Common landmarks of protein spots in the SH-SY5Y cells after treatment with control siRNA and LGR5 siRNA are indicated. (B) Identification of protein spots. Protein spots exhibiting a change greater than twofold in the expression in SH-SY5Y cells treated with LGR5 siRNA compared to control cells. (C) Detailed information of the 12 selected protein spots. (D) Proteins with increased and decreased expression after LGR5 inhibition compared to control-treated cells. (E) Identification of different expression levels of hnRNPA2B1 and hnRNPH3 in SH-SY5Y cells after treatment with LGR5 siRNA or control siRNA by western blotting. (F) LGR5-associated protein-protein interaction network. An LGR5-associated protein-protein interaction network was constructed using a bioinformatics approach. Circles indicate LGR5 and the 12 proteins found to be associated with LGR5 in neuroblastoma cells by a proteomics approach. The thickness of the line between any two proteins represents the degree of confidence in the interaction between the two proteins, with thicker lines indicating higher confidence (left upper). The types of interactions between proteins are represented by action types and effects (right lower).

    Journal: Experimental Neurobiology

    Article Title: LGR5 and Downstream Intracellular Signaling Proteins Play Critical Roles in the Cell Proliferation of Neuroblastoma, Meningioma and Pituitary Adenoma

    doi: 10.5607/en.2019.28.5.628

    Figure Lengend Snippet: Proteomic and bioinformatic analysis of LGR5 knockdown in SH-SY5Y cells. (A) Coomassie brilliant blue R-350 stained gels after 2D-PAGE. Protein spots in SH-SY5Y cells after treatment with control siRNA or LGR5 siRNA. Common landmarks of protein spots in the SH-SY5Y cells after treatment with control siRNA and LGR5 siRNA are indicated. (B) Identification of protein spots. Protein spots exhibiting a change greater than twofold in the expression in SH-SY5Y cells treated with LGR5 siRNA compared to control cells. (C) Detailed information of the 12 selected protein spots. (D) Proteins with increased and decreased expression after LGR5 inhibition compared to control-treated cells. (E) Identification of different expression levels of hnRNPA2B1 and hnRNPH3 in SH-SY5Y cells after treatment with LGR5 siRNA or control siRNA by western blotting. (F) LGR5-associated protein-protein interaction network. An LGR5-associated protein-protein interaction network was constructed using a bioinformatics approach. Circles indicate LGR5 and the 12 proteins found to be associated with LGR5 in neuroblastoma cells by a proteomics approach. The thickness of the line between any two proteins represents the degree of confidence in the interaction between the two proteins, with thicker lines indicating higher confidence (left upper). The types of interactions between proteins are represented by action types and effects (right lower).

    Article Snippet: Image analysis Completed 2D-PAGE gels were stained using Coomassie brilliant blue R-350 (CBB; GE Healthcare) and scanned as computer images.

    Techniques: Staining, Polyacrylamide Gel Electrophoresis, Expressing, Inhibition, Western Blot, Construct

    Solubilized MSC and SB623-derived ECM analyzed by SDS-PAGE. SDS/urea-soluble SB623-derived ECM (SB) and corresponding MSC. M: molecular weight markers. SDS/urea samples were precipitated, re-suspended in 2X loading buffer, loaded on a 1.5-mm 4–20% Tris-acetate gel, electrophoresed and stained with Coomassie Blue R-250.

    Journal: PLoS ONE

    Article Title: Proteomic Analysis of the Extracellular Matrix Produced by Mesenchymal Stromal Cells: Implications for Cell Therapy Mechanism

    doi: 10.1371/journal.pone.0079283

    Figure Lengend Snippet: Solubilized MSC and SB623-derived ECM analyzed by SDS-PAGE. SDS/urea-soluble SB623-derived ECM (SB) and corresponding MSC. M: molecular weight markers. SDS/urea samples were precipitated, re-suspended in 2X loading buffer, loaded on a 1.5-mm 4–20% Tris-acetate gel, electrophoresed and stained with Coomassie Blue R-250.

    Article Snippet: The gel was stained with Coomassie Brilliant Blue R-250 (MP Biomedicals) for 1 hour and destained overnight in methanol, acetic acid (Sigma-Aldrich) and deionized water at 4°C.

    Techniques: Derivative Assay, SDS Page, Molecular Weight, Staining