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Bio-Rad pmsf
Pmsf, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Article Title: Isoprenoids determine Th1/Th2 fate in pathogenic T cells, providing a mechanism of modulation of autoimmunity by atorvastatin
Article Snippet: .. Each protein sample was suspended in 2 vol. of 2× SDS Sample Buffer (Bio-Rad Laboratories) and subjected to SDS-PAGE electrophoresis using precast Tris-HCl Ready-Gels (Bio-Rad Laboratories). .. Proteins were transferred to PVDF membranes (GE Healthcare) and immunoblotting was performed using conventional methods (Santa Cruz Biotechnology, Inc.).

Article Title: Inhibition of PI3K by copanlisib exerts potent antitumor effects on Merkel cell carcinoma cell lines and mouse xenografts
Article Snippet: Xenograft tumor tissues harvested from mice were homogenized in 2% SDS lysis buffer and processed as described previously . .. Briefly, whole cell protein lysates (10–30 µg per lane) were resolved by 8% or 12% SDS-PAGE gel electrophoresis and transferred onto PVDF membranes by a semidry blotting system (Bio-Rad, Hercules, CA). .. Membranes were blocked in 5% fat-free milk/Tris–buffered saline for 1 hour at RT and incubated with specific primary antibodies at 4 °C overnight, followed by one hour RT incubation with secondary antibodies conjugated with horseradish peroxidase.

Article Title: Assembly and Folding Properties of Cytosolic IgG Intrabodies
Article Snippet: After washing the resin, immunoprecipitated proteins were eluted and r esolved by SDS-PAGE, followed by immunoblotting. .. Immunoblot analysis For SDS-PAGE analysis under non-reducing conditions, samples were diluted 1:1 in 2× Laemmli sample buffer (Bio-Rad). ..

Article Title: In vitro pepsin resistance of proteins: Effect of non-reduced SDS-PAGE analysis on fragment observation
Article Snippet: .. 2.4 SDS-PAGE electrophoresis Digest samples and the reagent blank and standard samples were further diluted 1 in 4 in reducing or non-reducing sample buffer (XT sample buffer (Bio-Rad Laboratories Ltd., Hemel Hempstead, UK) ±100 mM dithiothreitol) prior to SDS-PAGE electrophoresis according to the method of Schägger and von Jagow . .. Reduced and non-reduced samples were run on separate gels, however for each gel a standard of the opposite reduction status was run alongside the samples, to allow an on-gel comparison of the migration of the reduced/non-reduced parent protein.

Article Title: Molecular pathogenesis of inherited hypertension with hyperkalemia: The Na-Cl cotransporter is inhibited by wild-type but not mutant WNK4
Article Snippet: .. Lysates and immunoprecipitated proteins were fractionated using 4–15% SDS/PAGE gradient gel electrophoresis (Bio-Rad). .. Proteins were transferred to poly(vinylidene difluoride) (PVDF) membrane (Bio-Rad) at 100 V and 4°C for 2 h. The membrane was blocked in 5% nonfat dried milk in PBS.

Article Title: Engineering of Chimeric Polyketide Synthases Using SYNZIP Docking Domains
Article Snippet: For anion exchange chromatography the HiTrapQ column was from GE Healthcare. .. For all SDS-PAGE analyses, SDS-PAGE Mini Protean TGX precast gels were from Bio Rad (4–20% and 7.5%). .. For protein concentration Amicon Ultracentrifugal filters were from Millipore.

Article Title: Reconstitution of Drosophila and human chromatins by wheat germ cell-free co-expression system
Article Snippet: Then, 1.5 μl each of translation products was mixed with 2x loading buffer (Bio-Rad Laboratories), incubated for 5 min at 95 °C, then analyzed by SDS-PAGE. .. 18.0% SDS-PAGE gel and Coomassie Blue staining were used for Drosophila and human histone proteins, 10% stain-free SDS-PAGE (Bio-Rad Laboratories) was used for chromatin assembly factors and proteins were visualized by the gel documentation system (Bio-Rad Laboratories). .. For DmH1, a sample was run on 18% SDS-PAGE followed by Coomassie Blue staining.

Article Title: The CNS Myelin Proteome: Deep Profile and Persistence After Post-mortem Delay
Article Snippet: .. Briefly, samples were separated on a 12% SDS-PAGE gel (1 h at 200 V) using the Bio-Rad system, fixated overnight in 10% [v/v] acetic acid and 40% [v/v] ethanol and then washed in 30% ethanol (2 × 20 min) and ddH2 O (1 × 20 min). .. For sensitization, gels were incubated 1 min in 0.012% [v/v] Na2 S2 O3 and subsequently washed with ddH2 O (3 × 20 s).

Electrophoresis:

Article Title: Isoprenoids determine Th1/Th2 fate in pathogenic T cells, providing a mechanism of modulation of autoimmunity by atorvastatin
Article Snippet: .. Each protein sample was suspended in 2 vol. of 2× SDS Sample Buffer (Bio-Rad Laboratories) and subjected to SDS-PAGE electrophoresis using precast Tris-HCl Ready-Gels (Bio-Rad Laboratories). .. Proteins were transferred to PVDF membranes (GE Healthcare) and immunoblotting was performed using conventional methods (Santa Cruz Biotechnology, Inc.).

Article Title: In vitro pepsin resistance of proteins: Effect of non-reduced SDS-PAGE analysis on fragment observation
Article Snippet: .. 2.4 SDS-PAGE electrophoresis Digest samples and the reagent blank and standard samples were further diluted 1 in 4 in reducing or non-reducing sample buffer (XT sample buffer (Bio-Rad Laboratories Ltd., Hemel Hempstead, UK) ±100 mM dithiothreitol) prior to SDS-PAGE electrophoresis according to the method of Schägger and von Jagow . .. Reduced and non-reduced samples were run on separate gels, however for each gel a standard of the opposite reduction status was run alongside the samples, to allow an on-gel comparison of the migration of the reduced/non-reduced parent protein.

Nucleic Acid Electrophoresis:

Article Title: Inhibition of PI3K by copanlisib exerts potent antitumor effects on Merkel cell carcinoma cell lines and mouse xenografts
Article Snippet: Xenograft tumor tissues harvested from mice were homogenized in 2% SDS lysis buffer and processed as described previously . .. Briefly, whole cell protein lysates (10–30 µg per lane) were resolved by 8% or 12% SDS-PAGE gel electrophoresis and transferred onto PVDF membranes by a semidry blotting system (Bio-Rad, Hercules, CA). .. Membranes were blocked in 5% fat-free milk/Tris–buffered saline for 1 hour at RT and incubated with specific primary antibodies at 4 °C overnight, followed by one hour RT incubation with secondary antibodies conjugated with horseradish peroxidase.

Article Title: Molecular pathogenesis of inherited hypertension with hyperkalemia: The Na-Cl cotransporter is inhibited by wild-type but not mutant WNK4
Article Snippet: .. Lysates and immunoprecipitated proteins were fractionated using 4–15% SDS/PAGE gradient gel electrophoresis (Bio-Rad). .. Proteins were transferred to poly(vinylidene difluoride) (PVDF) membrane (Bio-Rad) at 100 V and 4°C for 2 h. The membrane was blocked in 5% nonfat dried milk in PBS.

Immunoprecipitation:

Article Title: Molecular pathogenesis of inherited hypertension with hyperkalemia: The Na-Cl cotransporter is inhibited by wild-type but not mutant WNK4
Article Snippet: .. Lysates and immunoprecipitated proteins were fractionated using 4–15% SDS/PAGE gradient gel electrophoresis (Bio-Rad). .. Proteins were transferred to poly(vinylidene difluoride) (PVDF) membrane (Bio-Rad) at 100 V and 4°C for 2 h. The membrane was blocked in 5% nonfat dried milk in PBS.

Staining:

Article Title: Reconstitution of Drosophila and human chromatins by wheat germ cell-free co-expression system
Article Snippet: Then, 1.5 μl each of translation products was mixed with 2x loading buffer (Bio-Rad Laboratories), incubated for 5 min at 95 °C, then analyzed by SDS-PAGE. .. 18.0% SDS-PAGE gel and Coomassie Blue staining were used for Drosophila and human histone proteins, 10% stain-free SDS-PAGE (Bio-Rad Laboratories) was used for chromatin assembly factors and proteins were visualized by the gel documentation system (Bio-Rad Laboratories). .. For DmH1, a sample was run on 18% SDS-PAGE followed by Coomassie Blue staining.

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    Bio-Rad pmsf
    Detection of CheA1 in different subcellular fractions of A. brasilense wild-type strain Sp7 and its Δ cheA1 mutant derivative by Western blotting. (A) Whole-cell lysates of the wild type and the Δ cheA1 mutant were probed with affinity-purified polyclonal antibodies raised against a recombinantly produced soluble CheA1ΔTMX from A. brasilense Sp7, as described in Materials and Methods. (B) Different subcellular fractions collected from the wild-type strain Sp7 were probed with affinity-purified polyclonal antibodies raised against a recombinantly produced soluble CheA1ΔTMX from A. brasilense Sp7. Note that different protocols were used for sample preparation and SDS-PAGE for the Western blots shown in panels A and B (see Materials and Methods). In panel A, an anti-CheAΔTMX antibody, which was further purified against whole proteins extracted from the Δ che1 mutant, was used. These samples were run on a 7.5% gel and transferred to a 0.45-μm hydrophobic PVDF transfer membrane. In panel B, an anti-CheAΔTMX antibody which had not been further purified against whole proteins extracted from the Δ che1 mutant was used. The membrane fraction was <t>resuspended</t> in a solubilizing buffer (1× PBS with 2% Triton X-100 and 1 mM <t>PMSF)</t> and run on an 8 to 16% gradient gel before being transferred to a nitrocellulose membrane. For the cytosolic fraction, these samples were concentrated via acetone precipitation before being loaded in a 10% gel and transferred to a nitrocellulose membrane. The numbers on the left indicate the positions of the molecular mass markers run on the same gels. The arrows point to the soluble, faint band corresponding to CheA1ΔTMX.
    Pmsf, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pmsf/product/Bio-Rad
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pmsf - by Bioz Stars, 2021-04
    86/100 stars
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    Detection of CheA1 in different subcellular fractions of A. brasilense wild-type strain Sp7 and its Δ cheA1 mutant derivative by Western blotting. (A) Whole-cell lysates of the wild type and the Δ cheA1 mutant were probed with affinity-purified polyclonal antibodies raised against a recombinantly produced soluble CheA1ΔTMX from A. brasilense Sp7, as described in Materials and Methods. (B) Different subcellular fractions collected from the wild-type strain Sp7 were probed with affinity-purified polyclonal antibodies raised against a recombinantly produced soluble CheA1ΔTMX from A. brasilense Sp7. Note that different protocols were used for sample preparation and SDS-PAGE for the Western blots shown in panels A and B (see Materials and Methods). In panel A, an anti-CheAΔTMX antibody, which was further purified against whole proteins extracted from the Δ che1 mutant, was used. These samples were run on a 7.5% gel and transferred to a 0.45-μm hydrophobic PVDF transfer membrane. In panel B, an anti-CheAΔTMX antibody which had not been further purified against whole proteins extracted from the Δ che1 mutant was used. The membrane fraction was resuspended in a solubilizing buffer (1× PBS with 2% Triton X-100 and 1 mM PMSF) and run on an 8 to 16% gradient gel before being transferred to a nitrocellulose membrane. For the cytosolic fraction, these samples were concentrated via acetone precipitation before being loaded in a 10% gel and transferred to a nitrocellulose membrane. The numbers on the left indicate the positions of the molecular mass markers run on the same gels. The arrows point to the soluble, faint band corresponding to CheA1ΔTMX.

    Journal: Journal of Bacteriology

    Article Title: Distinct Domains of CheA Confer Unique Functions in Chemotaxis and Cell Length in Azospirillum brasilense Sp7

    doi: 10.1128/JB.00189-17

    Figure Lengend Snippet: Detection of CheA1 in different subcellular fractions of A. brasilense wild-type strain Sp7 and its Δ cheA1 mutant derivative by Western blotting. (A) Whole-cell lysates of the wild type and the Δ cheA1 mutant were probed with affinity-purified polyclonal antibodies raised against a recombinantly produced soluble CheA1ΔTMX from A. brasilense Sp7, as described in Materials and Methods. (B) Different subcellular fractions collected from the wild-type strain Sp7 were probed with affinity-purified polyclonal antibodies raised against a recombinantly produced soluble CheA1ΔTMX from A. brasilense Sp7. Note that different protocols were used for sample preparation and SDS-PAGE for the Western blots shown in panels A and B (see Materials and Methods). In panel A, an anti-CheAΔTMX antibody, which was further purified against whole proteins extracted from the Δ che1 mutant, was used. These samples were run on a 7.5% gel and transferred to a 0.45-μm hydrophobic PVDF transfer membrane. In panel B, an anti-CheAΔTMX antibody which had not been further purified against whole proteins extracted from the Δ che1 mutant was used. The membrane fraction was resuspended in a solubilizing buffer (1× PBS with 2% Triton X-100 and 1 mM PMSF) and run on an 8 to 16% gradient gel before being transferred to a nitrocellulose membrane. For the cytosolic fraction, these samples were concentrated via acetone precipitation before being loaded in a 10% gel and transferred to a nitrocellulose membrane. The numbers on the left indicate the positions of the molecular mass markers run on the same gels. The arrows point to the soluble, faint band corresponding to CheA1ΔTMX.

    Article Snippet: Equal volumes of the membrane pellet, which was resuspended in 1× PBS with 2% Triton X-100, 1 mM PMSF, and 2× Laemmli buffer with reducing agent, were boiled for 5 min prior to being loaded, at an amount of 31 μg, into an 8 to 16% Mini-Protean precast gradient gel (Bio-Rad).

    Techniques: Mutagenesis, Western Blot, Affinity Purification, Produced, Sample Prep, SDS Page, Purification