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coomassie plustm protein assay kit  (Thermo Fisher)


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    Structured Review

    Thermo Fisher coomassie plustm protein assay kit
    Zymographic analysis of recombinant endoglucanase activity in different cellular fractions of Saccharomyces cerevisiae JARC06. Lane 1 shows the prestained protein molecular weight marker. Lane 2 shows the zymogram of the intracellular (cytoplasmic) enzyme extract. Lane 3 shows the zymogram of the cell wall-associated enzyme fraction released after DTT treatment. Lane 4 shows the zymogram of the enzyme fraction secreted into the culture medium. Lanes 5–7 show SDS–PAGE gel runs parallel with the zymogram and stained with <t>Coomassie</t> Brilliant Blue G-250 to visualize the protein-banding pattern. Lane 5 shows the cytoplasmic protein fraction, lane 6 shows the cell wall-associated proteins, and lane 7 shows the proteins present in the culture supernatant.
    Coomassie Plustm Protein Assay Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/coomassie+plustm+protein+assay+kit/Bovine+Serum+Albumin/pmc13209753-72-15-20
    Average 99 stars, based on 1 article reviews
    coomassie plustm protein assay kit - by Bioz Stars, 2026-10
    99/100 stars

    Images

    1) Product Images from "Differential Processing of a Bacillus subtilis GH5 Endoglucanase During Yeast Surface Display in Saccharomyces cerevisiae"

    Article Title: Differential Processing of a Bacillus subtilis GH5 Endoglucanase During Yeast Surface Display in Saccharomyces cerevisiae

    Journal: Microorganisms

    doi: 10.3390/microorganisms14051061

    Zymographic analysis of recombinant endoglucanase activity in different cellular fractions of Saccharomyces cerevisiae JARC06. Lane 1 shows the prestained protein molecular weight marker. Lane 2 shows the zymogram of the intracellular (cytoplasmic) enzyme extract. Lane 3 shows the zymogram of the cell wall-associated enzyme fraction released after DTT treatment. Lane 4 shows the zymogram of the enzyme fraction secreted into the culture medium. Lanes 5–7 show SDS–PAGE gel runs parallel with the zymogram and stained with Coomassie Brilliant Blue G-250 to visualize the protein-banding pattern. Lane 5 shows the cytoplasmic protein fraction, lane 6 shows the cell wall-associated proteins, and lane 7 shows the proteins present in the culture supernatant.
    Figure Legend Snippet: Zymographic analysis of recombinant endoglucanase activity in different cellular fractions of Saccharomyces cerevisiae JARC06. Lane 1 shows the prestained protein molecular weight marker. Lane 2 shows the zymogram of the intracellular (cytoplasmic) enzyme extract. Lane 3 shows the zymogram of the cell wall-associated enzyme fraction released after DTT treatment. Lane 4 shows the zymogram of the enzyme fraction secreted into the culture medium. Lanes 5–7 show SDS–PAGE gel runs parallel with the zymogram and stained with Coomassie Brilliant Blue G-250 to visualize the protein-banding pattern. Lane 5 shows the cytoplasmic protein fraction, lane 6 shows the cell wall-associated proteins, and lane 7 shows the proteins present in the culture supernatant.

    Techniques Used: Recombinant, Activity Assay, Molecular Weight, Marker, SDS Page, Staining

    Zymographic analysis of endoglucanase activity in cytoplasmic extracts of Saccharomyces cerevisiae. SDS–PAGE gels copolymerized with 0.5% ( w / v ) carboxymethyl cellulose (CMC) were used to evaluate enzymatic activity. Cytoplasmic extracts from the recombinant strain expressing egl S and the control strain ( S. cerevisiae EBY100 harboring the empty pYD1 vector) were analyzed under identical conditions. Lanes: (1) recombinant strain, (2) control strain, (3) molecular weight marker. ( A , B ) Same gel: ( A ) Coomassie Brilliant Blue staining and ( B ) Congo Red staining showing hydrolytic activity as clear zones. ( C , D ) Independent replicate: ( C ) Congo Red staining and ( D ) subsequent Coomassie staining. Hydrolytic activity is detected exclusively in the recombinant strain.
    Figure Legend Snippet: Zymographic analysis of endoglucanase activity in cytoplasmic extracts of Saccharomyces cerevisiae. SDS–PAGE gels copolymerized with 0.5% ( w / v ) carboxymethyl cellulose (CMC) were used to evaluate enzymatic activity. Cytoplasmic extracts from the recombinant strain expressing egl S and the control strain ( S. cerevisiae EBY100 harboring the empty pYD1 vector) were analyzed under identical conditions. Lanes: (1) recombinant strain, (2) control strain, (3) molecular weight marker. ( A , B ) Same gel: ( A ) Coomassie Brilliant Blue staining and ( B ) Congo Red staining showing hydrolytic activity as clear zones. ( C , D ) Independent replicate: ( C ) Congo Red staining and ( D ) subsequent Coomassie staining. Hydrolytic activity is detected exclusively in the recombinant strain.

    Techniques Used: Activity Assay, SDS Page, Recombinant, Expressing, Control, Plasmid Preparation, Molecular Weight, Marker, Staining

    Related Articles

    Concentration Assay:

    Article Title: At2-MMP is required for attenuation of cell proliferation during wound healing in incised Arabidopsis inflorescence stems.
    Article Snippet: 1Graduate School of Science and Technology, University of Tsukuba, Tsukuba, Ibaraki, 305,8572 Japan 2Faculty of Advanced Science and Technology, Kumamoto University, Kurokami, Chuo-ku, Kumamoto, 860, 8555 Japan 3Institute of Health and Sport Sciences, University of Tsukuba, Tsukuba, Ibaraki, 305,8572 Japan 4Advanced Instrumental Analysis Center, Teikyo University, Utsunomiya, Tochigi, 320,8551 Japan 5Department of Biosciences, Teikyo University, Utsunomiya, Tochigi, 320,8551 Japan 6Institute of Life and Environmental Sciences, University of Tsukuba, Tsukuba, Ibaraki, 305,8572 Japan

    other:

    Article Title: Differential Processing of a Bacillus subtilis GH5 Endoglucanase During Yeast Surface Display in Saccharomyces cerevisiae
    Article Snippet: Protein concentrations in the different enzyme extracts were determined using the Bradford method with the Coomassie Plus Protein Assay Kit (Thermo Scientific, Carlsbad, CA, USA) [ ], using bovine serum albumin (BSA) as the standard.

    Article Title: Identification of protein related to dietary vitamin B 3 deficiency in Mediterranean fruit fly larvae
    Article Snippet: The lysates were then homogenized on ice using an Ultraturrax homogenizer (Cole Parmer, Verman Hills, IL) for 3 min at an interval of 30 s, after which the homogenate was centrifuged at 17 555 g for 30 min.

    Protein Concentration:

    Article Title: PACAP38 Differentially Effects Genes and CRMP2 Protein Expression in Ischemic Core and Penumbra Regions of Permanent Middle Cerebral Artery Occlusion Model Mice Brain
    Article Snippet: .. Protein concentration was determined with a Coomassie PlusTM Protein Assay kit (PIERCE, Rockford, IL, USA) using bovine serum albumin (BSA) as a standard and a NanoDrop 2000 spectrophotometer (Thermo Scientific, Wilmington, DE, USA). .. The separated proteins after SDS-PAGE (mini-gel) were transferred onto a polyvinyldifluoride (PVDF) (Trans-Blot Turbo Midi PVDF, 0.2 μM, Transfer Packs kit; Cat. no. 170-4157, Bio-Rad, Hercules, CA, USA).

    Article Title: Identification of protein related to dietary vitamin B 3 deficiency in Mediterranean fruit fly larvae
    Article Snippet: The lysates were then homogenized on ice using an Ultraturrax homogenizer (Cole Parmer, Verman Hills, IL) for 3 min at an interval of 30 s, after which the homogenate was centrifuged at 17 555 g for 30 min. .. The supernatant fractions were saved for protein identification by nano LC/IT/MS, while the protein concentration was determined using a Coomassie PlusTM Protein Assay Kit (Pierce). ..

    Spectrophotometry:

    Article Title: PACAP38 Differentially Effects Genes and CRMP2 Protein Expression in Ischemic Core and Penumbra Regions of Permanent Middle Cerebral Artery Occlusion Model Mice Brain
    Article Snippet: .. Protein concentration was determined with a Coomassie PlusTM Protein Assay kit (PIERCE, Rockford, IL, USA) using bovine serum albumin (BSA) as a standard and a NanoDrop 2000 spectrophotometer (Thermo Scientific, Wilmington, DE, USA). .. The separated proteins after SDS-PAGE (mini-gel) were transferred onto a polyvinyldifluoride (PVDF) (Trans-Blot Turbo Midi PVDF, 0.2 μM, Transfer Packs kit; Cat. no. 170-4157, Bio-Rad, Hercules, CA, USA).

    Modification:

    Article Title: Improved biomass and protein production in solid-state cultures of an Aspergillus sojae strain harboring the Vitreoscilla hemoglobin
    Article Snippet: .. Total soluble protein was measured in SSF-supernatant samples according to the modified Bradford method (Bradford ) from the commercial Coomassie PlusTM Protein Assay Kit (Thermo Scientific, Illinois, USA). ..

    Article Title: Exploitation of Agricultural Wastes and By-Products for Production of Aureobasidium pullulans Y-2311-1 Xylanase: Screening, Bioprocess Optimization and Scale Up
    Article Snippet: .. Total protein was estimated according to the modified Bradford method, using a Coomassie PlusTM Protein Assay Kit (Pierce, Fischer Scientific, Schwerte, Germany). ..



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    Zymographic analysis of recombinant endoglucanase activity in different cellular fractions of Saccharomyces cerevisiae JARC06. Lane 1 shows the prestained protein molecular weight marker. Lane 2 shows the zymogram of the intracellular (cytoplasmic) enzyme extract. Lane 3 shows the zymogram of the cell wall-associated enzyme fraction released after DTT treatment. Lane 4 shows the zymogram of the enzyme fraction secreted into the culture medium. Lanes 5–7 show SDS–PAGE gel runs parallel with the zymogram and stained with <t>Coomassie</t> Brilliant Blue G-250 to visualize the protein-banding pattern. Lane 5 shows the cytoplasmic protein fraction, lane 6 shows the cell wall-associated proteins, and lane 7 shows the proteins present in the culture supernatant.
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    Zymographic analysis of recombinant endoglucanase activity in different cellular fractions of Saccharomyces cerevisiae JARC06. Lane 1 shows the prestained protein molecular weight marker. Lane 2 shows the zymogram of the intracellular (cytoplasmic) enzyme extract. Lane 3 shows the zymogram of the cell wall-associated enzyme fraction released after DTT treatment. Lane 4 shows the zymogram of the enzyme fraction secreted into the culture medium. Lanes 5–7 show SDS–PAGE gel runs parallel with the zymogram and stained with <t>Coomassie</t> Brilliant Blue G-250 to visualize the protein-banding pattern. Lane 5 shows the cytoplasmic protein fraction, lane 6 shows the cell wall-associated proteins, and lane 7 shows the proteins present in the culture supernatant.
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    Zymographic analysis of recombinant endoglucanase activity in different cellular fractions of Saccharomyces cerevisiae JARC06. Lane 1 shows the prestained protein molecular weight marker. Lane 2 shows the zymogram of the intracellular (cytoplasmic) enzyme extract. Lane 3 shows the zymogram of the cell wall-associated enzyme fraction released after DTT treatment. Lane 4 shows the zymogram of the enzyme fraction secreted into the culture medium. Lanes 5–7 show SDS–PAGE gel runs parallel with the zymogram and stained with <t>Coomassie</t> Brilliant Blue G-250 to visualize the protein-banding pattern. Lane 5 shows the cytoplasmic protein fraction, lane 6 shows the cell wall-associated proteins, and lane 7 shows the proteins present in the culture supernatant.
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    Image Search Results


    Zymographic analysis of recombinant endoglucanase activity in different cellular fractions of Saccharomyces cerevisiae JARC06. Lane 1 shows the prestained protein molecular weight marker. Lane 2 shows the zymogram of the intracellular (cytoplasmic) enzyme extract. Lane 3 shows the zymogram of the cell wall-associated enzyme fraction released after DTT treatment. Lane 4 shows the zymogram of the enzyme fraction secreted into the culture medium. Lanes 5–7 show SDS–PAGE gel runs parallel with the zymogram and stained with Coomassie Brilliant Blue G-250 to visualize the protein-banding pattern. Lane 5 shows the cytoplasmic protein fraction, lane 6 shows the cell wall-associated proteins, and lane 7 shows the proteins present in the culture supernatant.

    Journal: Microorganisms

    Article Title: Differential Processing of a Bacillus subtilis GH5 Endoglucanase During Yeast Surface Display in Saccharomyces cerevisiae

    doi: 10.3390/microorganisms14051061

    Figure Lengend Snippet: Zymographic analysis of recombinant endoglucanase activity in different cellular fractions of Saccharomyces cerevisiae JARC06. Lane 1 shows the prestained protein molecular weight marker. Lane 2 shows the zymogram of the intracellular (cytoplasmic) enzyme extract. Lane 3 shows the zymogram of the cell wall-associated enzyme fraction released after DTT treatment. Lane 4 shows the zymogram of the enzyme fraction secreted into the culture medium. Lanes 5–7 show SDS–PAGE gel runs parallel with the zymogram and stained with Coomassie Brilliant Blue G-250 to visualize the protein-banding pattern. Lane 5 shows the cytoplasmic protein fraction, lane 6 shows the cell wall-associated proteins, and lane 7 shows the proteins present in the culture supernatant.

    Article Snippet: Protein concentrations in the different enzyme extracts were determined using the Bradford method with the Coomassie PlusTM Protein Assay Kit (Thermo Scientific, Carlsbad, CA, USA) [ ], using bovine serum albumin (BSA) as the standard.

    Techniques: Recombinant, Activity Assay, Molecular Weight, Marker, SDS Page, Staining

    Zymographic analysis of endoglucanase activity in cytoplasmic extracts of Saccharomyces cerevisiae. SDS–PAGE gels copolymerized with 0.5% ( w / v ) carboxymethyl cellulose (CMC) were used to evaluate enzymatic activity. Cytoplasmic extracts from the recombinant strain expressing egl S and the control strain ( S. cerevisiae EBY100 harboring the empty pYD1 vector) were analyzed under identical conditions. Lanes: (1) recombinant strain, (2) control strain, (3) molecular weight marker. ( A , B ) Same gel: ( A ) Coomassie Brilliant Blue staining and ( B ) Congo Red staining showing hydrolytic activity as clear zones. ( C , D ) Independent replicate: ( C ) Congo Red staining and ( D ) subsequent Coomassie staining. Hydrolytic activity is detected exclusively in the recombinant strain.

    Journal: Microorganisms

    Article Title: Differential Processing of a Bacillus subtilis GH5 Endoglucanase During Yeast Surface Display in Saccharomyces cerevisiae

    doi: 10.3390/microorganisms14051061

    Figure Lengend Snippet: Zymographic analysis of endoglucanase activity in cytoplasmic extracts of Saccharomyces cerevisiae. SDS–PAGE gels copolymerized with 0.5% ( w / v ) carboxymethyl cellulose (CMC) were used to evaluate enzymatic activity. Cytoplasmic extracts from the recombinant strain expressing egl S and the control strain ( S. cerevisiae EBY100 harboring the empty pYD1 vector) were analyzed under identical conditions. Lanes: (1) recombinant strain, (2) control strain, (3) molecular weight marker. ( A , B ) Same gel: ( A ) Coomassie Brilliant Blue staining and ( B ) Congo Red staining showing hydrolytic activity as clear zones. ( C , D ) Independent replicate: ( C ) Congo Red staining and ( D ) subsequent Coomassie staining. Hydrolytic activity is detected exclusively in the recombinant strain.

    Article Snippet: Protein concentrations in the different enzyme extracts were determined using the Bradford method with the Coomassie PlusTM Protein Assay Kit (Thermo Scientific, Carlsbad, CA, USA) [ ], using bovine serum albumin (BSA) as the standard.

    Techniques: Activity Assay, SDS Page, Recombinant, Expressing, Control, Plasmid Preparation, Molecular Weight, Marker, Staining