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12% novex zymogram blue casein gels  (Thermo Fisher)


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    Structured Review

    Thermo Fisher 12% novex zymogram blue casein gels
    12% Novex Zymogram Blue Casein Gels, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/blue+casein+zymogram+gel/pmc03149281-63-7-12
    Average 90 stars, based on 1 article reviews
    12% novex zymogram blue casein gels - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Staining:

    Article Title: A conjugate of camptothecin and a somatostatin analog against prostate cancer cell invasion via a possible signaling pathway involving PI3K/Akt, alphaVbeta3/alphaVbeta5 and MMP-2/-9.
    Article Snippet: Camptothecin (CPT) was conjugated to the N-terminal of a somatostatin analog (SSA) directly via a carbamate group and a basic N-terminal linking motif, D-Lys-D-Tyr-Lys-D-Tyr-D-Lys.. This new CPT-SSA conjugate termed JF-10-81 was evaluated as a receptor-specific delivery system for its anti-invasive and anti-angiogenic activities.. It was found that, in addition to blocking migration and invasion of highly invasive prostate cancer PC-3 cells, this conjugate also inhibited in vitro capillary-like tube formation of endothelial cells and in vivo angiogenesis in C57B1/6N female mice.

    Activity Assay:

    Article Title: Multifunctional Role of Choline Binding Protein G in Pneumococcal Pathogenesis
    Article Snippet: .. To test for proteolytic activity, equal amounts of either CbpG-293T cell lysate or 293T control lysate were loaded onto a 4 to 16% Blue Casein zymogram gel (Invitrogen). .. The gel was electrophoresed for 110 min at 125 V. After electrophoresis, the gel was renatured for 30 min and developed overnight at 37°C using Novex zymogram renaturing and developing buffers (Invitrogen) according to the manufacturer's protocol.

    Article Title: Multifunctional Role of Choline Binding Protein G in Pneumococcal Pathogenesis
    Article Snippet: .. To test for proteolytic activity, equal amounts of either CbpG-293T cell lysate or 293T control lysate were loaded onto a 4 to 16% Blue Casein zymogram gel (Invitrogen). .. The gel was electrophoresed for 110 min at 125 V. After electrophoresis, the gel was renatured for 30 min and developed overnight at 37°C using Novex zymogram renaturing and developing buffers (Invitrogen) according to the manufacturer’s protocol.

    Control:

    Article Title: Multifunctional Role of Choline Binding Protein G in Pneumococcal Pathogenesis
    Article Snippet: .. To test for proteolytic activity, equal amounts of either CbpG-293T cell lysate or 293T control lysate were loaded onto a 4 to 16% Blue Casein zymogram gel (Invitrogen). .. The gel was electrophoresed for 110 min at 125 V. After electrophoresis, the gel was renatured for 30 min and developed overnight at 37°C using Novex zymogram renaturing and developing buffers (Invitrogen) according to the manufacturer's protocol.

    Article Title: Multifunctional Role of Choline Binding Protein G in Pneumococcal Pathogenesis
    Article Snippet: .. To test for proteolytic activity, equal amounts of either CbpG-293T cell lysate or 293T control lysate were loaded onto a 4 to 16% Blue Casein zymogram gel (Invitrogen). .. The gel was electrophoresed for 110 min at 125 V. After electrophoresis, the gel was renatured for 30 min and developed overnight at 37°C using Novex zymogram renaturing and developing buffers (Invitrogen) according to the manufacturer’s protocol.

    Zymography:

    Article Title: Helicobacter pylori upregulates matrilysin (MMP-7) in epithelial cells in vivo and in vitro in a Cag dependent manner.
    Article Snippet: For blotting, SDS-PAGE gels were blotted for one hour onto PVDF membranes at 150 mA, blocked in phosphate buffered saline-0.5% Tween with 5% skimmed milk powder (Oxoid) for one hour, and then incubated with primary antibody (monoclonal anti-MMP-7; Oncogene Research Products, Nottingham, UK) overnight, washed and incubated with peroxidase conjugated goat antimouse IgG antibodies(Sigma-Aldrich), washed, and then developed using ECL system (Amersham Pharmacia-Biotech). .. For casein zymography, samples were mixed with SDS sample buffer (Novex; Invitrogen, Paisley, UK), applied to a 4–16% blue casein zymogram gel (Invitrogen) and run using the manufacturer’s recommended buffers. .. After running, the gels were placed in renaturing buffer and incubated overnight in developing buffer (both buffers from Invitrogen).



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    Seed proteins from wild-type and mutant lines from the TI1 C77Y family were separated by cation-exchange chromatography. Absorbance profiles at 280 nm are shown ( a, b : red and <t>blue</t> lines without symbols; mAbs, left-hand scale). Using BAPNA and BTEE as specific substrates, the trypsin ( a ) and chymotrypsin inhibitory ( b ) activities of wild-type (red triangle) and mutant (blue triangl) protein fractions are shown, relative to assays where trypsin activity is 100% (control; right-hand scale). Numbers in peaks in each chromatogram correspond to the different forms of TI1 and TI2 (peak 1: TI2 processed; Peak 2: TI2 unprocessed; Peak 3: TI1 processed; Peak 4: TI1 unprocessed. ( c ) in-gel protease inhibitory activity of inhibitor isoforms from wild-type (i, iii) and C77Y mutant (ii, iv) lines. <t>Zymogram</t> blue <t>casein</t> <t>gels</t> were treated with the digestive enzymes, trypsin (i, ii) or chymotrypsin (iii, iv); dark areas indicate where the enzyme has been inhibited. The direction of electrophoresis on non-denaturing gels is indicated (-, +). The arrow indicates the position of the isoform that is missing from the mutant lines (tracks ii and iv).
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    Seed proteins from wild-type and mutant lines from the TI1 C77Y family were separated by cation-exchange chromatography. Absorbance profiles at 280 nm are shown ( a, b : red and <t>blue</t> lines without symbols; mAbs, left-hand scale). Using BAPNA and BTEE as specific substrates, the trypsin ( a ) and chymotrypsin inhibitory ( b ) activities of wild-type (red triangle) and mutant (blue triangl) protein fractions are shown, relative to assays where trypsin activity is 100% (control; right-hand scale). Numbers in peaks in each chromatogram correspond to the different forms of TI1 and TI2 (peak 1: TI2 processed; Peak 2: TI2 unprocessed; Peak 3: TI1 processed; Peak 4: TI1 unprocessed. ( c ) in-gel protease inhibitory activity of inhibitor isoforms from wild-type (i, iii) and C77Y mutant (ii, iv) lines. <t>Zymogram</t> blue <t>casein</t> <t>gels</t> were treated with the digestive enzymes, trypsin (i, ii) or chymotrypsin (iii, iv); dark areas indicate where the enzyme has been inhibited. The direction of electrophoresis on non-denaturing gels is indicated (-, +). The arrow indicates the position of the isoform that is missing from the mutant lines (tracks ii and iv).
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    Image Search Results


    Seed proteins from wild-type and mutant lines from the TI1 C77Y family were separated by cation-exchange chromatography. Absorbance profiles at 280 nm are shown ( a, b : red and blue lines without symbols; mAbs, left-hand scale). Using BAPNA and BTEE as specific substrates, the trypsin ( a ) and chymotrypsin inhibitory ( b ) activities of wild-type (red triangle) and mutant (blue triangl) protein fractions are shown, relative to assays where trypsin activity is 100% (control; right-hand scale). Numbers in peaks in each chromatogram correspond to the different forms of TI1 and TI2 (peak 1: TI2 processed; Peak 2: TI2 unprocessed; Peak 3: TI1 processed; Peak 4: TI1 unprocessed. ( c ) in-gel protease inhibitory activity of inhibitor isoforms from wild-type (i, iii) and C77Y mutant (ii, iv) lines. Zymogram blue casein gels were treated with the digestive enzymes, trypsin (i, ii) or chymotrypsin (iii, iv); dark areas indicate where the enzyme has been inhibited. The direction of electrophoresis on non-denaturing gels is indicated (-, +). The arrow indicates the position of the isoform that is missing from the mutant lines (tracks ii and iv).

    Journal: PLoS ONE

    Article Title: Eliminating Anti-Nutritional Plant Food Proteins: The Case of Seed Protease Inhibitors in Pea

    doi: 10.1371/journal.pone.0134634

    Figure Lengend Snippet: Seed proteins from wild-type and mutant lines from the TI1 C77Y family were separated by cation-exchange chromatography. Absorbance profiles at 280 nm are shown ( a, b : red and blue lines without symbols; mAbs, left-hand scale). Using BAPNA and BTEE as specific substrates, the trypsin ( a ) and chymotrypsin inhibitory ( b ) activities of wild-type (red triangle) and mutant (blue triangl) protein fractions are shown, relative to assays where trypsin activity is 100% (control; right-hand scale). Numbers in peaks in each chromatogram correspond to the different forms of TI1 and TI2 (peak 1: TI2 processed; Peak 2: TI2 unprocessed; Peak 3: TI1 processed; Peak 4: TI1 unprocessed. ( c ) in-gel protease inhibitory activity of inhibitor isoforms from wild-type (i, iii) and C77Y mutant (ii, iv) lines. Zymogram blue casein gels were treated with the digestive enzymes, trypsin (i, ii) or chymotrypsin (iii, iv); dark areas indicate where the enzyme has been inhibited. The direction of electrophoresis on non-denaturing gels is indicated (-, +). The arrow indicates the position of the isoform that is missing from the mutant lines (tracks ii and iv).

    Article Snippet: Non-denaturing gel separation of active protease inhibitor isoforms was carried out on 4–16% zymogram blue casein gels (Invitrogen) [ ].

    Techniques: Mutagenesis, Chromatography, Activity Assay, Control, Electrophoresis

    Seed proteins from wild-type and mutant lines from the TI1 E109K family were separated by cation-exchange chromatography. Absorbance profiles at 280 nm are shown (a, b: red and blue lines without symbols; mAbs, left-hand scale). Using BAPNA and BTEE as specific substrates, the trypsin ( a ) and chymotrypsin inhibitory ( b ) activities of wild-type (red triangle) and mutant (blue triangle) protein fractions are shown, relative to assays where trypsin activity is 100% (control; right-hand scale). Numbers in peaks in each chromatogram correspond to the different forms of TI1 and TI2 (peak 1: TI2 processed; Peak 2: TI2 unprocessed; Peak 3: TI1 processed; Peak 4: TI1 unprocessed. ( c ) in-gel protease inhibitory activity of inhibitor isoforms from wild-type (i, iii) and E109K mutant (ii, iv) lines. Zymogram blue casein gels were treated with the digestive enzymes, trypsin (i, ii) or chymotrypsin (iii, iv); dark areas indicate where the enzyme has been inhibited. The direction of electrophoresis on non-denaturing gels is indicated (-, +). The arrow indicates the position of the isoform that is missing from the mutant lines (tracks ii and iv).

    Journal: PLoS ONE

    Article Title: Eliminating Anti-Nutritional Plant Food Proteins: The Case of Seed Protease Inhibitors in Pea

    doi: 10.1371/journal.pone.0134634

    Figure Lengend Snippet: Seed proteins from wild-type and mutant lines from the TI1 E109K family were separated by cation-exchange chromatography. Absorbance profiles at 280 nm are shown (a, b: red and blue lines without symbols; mAbs, left-hand scale). Using BAPNA and BTEE as specific substrates, the trypsin ( a ) and chymotrypsin inhibitory ( b ) activities of wild-type (red triangle) and mutant (blue triangle) protein fractions are shown, relative to assays where trypsin activity is 100% (control; right-hand scale). Numbers in peaks in each chromatogram correspond to the different forms of TI1 and TI2 (peak 1: TI2 processed; Peak 2: TI2 unprocessed; Peak 3: TI1 processed; Peak 4: TI1 unprocessed. ( c ) in-gel protease inhibitory activity of inhibitor isoforms from wild-type (i, iii) and E109K mutant (ii, iv) lines. Zymogram blue casein gels were treated with the digestive enzymes, trypsin (i, ii) or chymotrypsin (iii, iv); dark areas indicate where the enzyme has been inhibited. The direction of electrophoresis on non-denaturing gels is indicated (-, +). The arrow indicates the position of the isoform that is missing from the mutant lines (tracks ii and iv).

    Article Snippet: Non-denaturing gel separation of active protease inhibitor isoforms was carried out on 4–16% zymogram blue casein gels (Invitrogen) [ ].

    Techniques: Mutagenesis, Chromatography, Activity Assay, Control, Electrophoresis

    Seed proteins from wild-type and mutant lines from the TI1 S85F family were separated by cation-exchange chromatography. Absorbance profiles at 280 nm are shown ( a, b : red and blue lines without symbols; mAbs, left-hand scale). Using BAPNA and BTEE as specific substrates, the trypsin ( a ) and chymotrypsin inhibitory ( b ) activities of wild-type (red triangle) and mutant (blue triangle) protein fractions are shown, relative to assays where trypsin activity is 100% (control; right-hand scale). Numbers in peaks in each chromatogram correspond to the different forms of TI1 and TI2 (peak 1: TI2 processed; Peak 2: TI2 unprocessed; Peak 3: TI1 processed; Peak 4: TI1 unprocessed. ( c ) in-gel protease inhibitory activity of inhibitor isoforms from wild-type (i, iii) and S85F mutant (ii, iv) lines. Zymogram blue casein gels were treated with the digestive enzymes, trypsin (i, ii) or chymotrypsin (iii, iv); dark areas indicate where the enzyme has been inhibited. The direction of electrophoresis on non-denaturing gels is indicated (-, +). The arrow indicates the position of the isoform that is missing from the mutant lines (track iv).

    Journal: PLoS ONE

    Article Title: Eliminating Anti-Nutritional Plant Food Proteins: The Case of Seed Protease Inhibitors in Pea

    doi: 10.1371/journal.pone.0134634

    Figure Lengend Snippet: Seed proteins from wild-type and mutant lines from the TI1 S85F family were separated by cation-exchange chromatography. Absorbance profiles at 280 nm are shown ( a, b : red and blue lines without symbols; mAbs, left-hand scale). Using BAPNA and BTEE as specific substrates, the trypsin ( a ) and chymotrypsin inhibitory ( b ) activities of wild-type (red triangle) and mutant (blue triangle) protein fractions are shown, relative to assays where trypsin activity is 100% (control; right-hand scale). Numbers in peaks in each chromatogram correspond to the different forms of TI1 and TI2 (peak 1: TI2 processed; Peak 2: TI2 unprocessed; Peak 3: TI1 processed; Peak 4: TI1 unprocessed. ( c ) in-gel protease inhibitory activity of inhibitor isoforms from wild-type (i, iii) and S85F mutant (ii, iv) lines. Zymogram blue casein gels were treated with the digestive enzymes, trypsin (i, ii) or chymotrypsin (iii, iv); dark areas indicate where the enzyme has been inhibited. The direction of electrophoresis on non-denaturing gels is indicated (-, +). The arrow indicates the position of the isoform that is missing from the mutant lines (track iv).

    Article Snippet: Non-denaturing gel separation of active protease inhibitor isoforms was carried out on 4–16% zymogram blue casein gels (Invitrogen) [ ].

    Techniques: Mutagenesis, Chromatography, Activity Assay, Control, Electrophoresis