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Bio-Rad tris hcl gradient gels
Tris Hcl Gradient Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tris hcl gradient gels - by Bioz Stars, 2021-03
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Related Articles

Purification:

Article Title: Role of the C-terminal domain of PCSK9 in degradation of the LDL receptors [S]
Article Snippet: A rabbit polyclonal anti-β-tubulin antibody (Nordic Biosite AB, Täby, Sweden) was used to detect β-tubulin, which was used as a loading control. .. Purified EC-LDLR or Δ1-7-EC-LDLR (both 400 ng/lane) were run on 4-20% Tris-HCl Criterion Precast Gels (Bio-Rad) and blotted onto Immuno-Blot PVDF membranes as described above. .. The membranes were incubated in phosphate-buffered saline with 2.5% Blotting-Grade Blocker Nonfat Dry Milk (Bio-Rad) at 4°C overnight to reduce nonspecific binding.

Transfection:

Article Title: Role of the C-terminal domain of PCSK9 in degradation of the LDL receptors [S]
Article Snippet: Western blot analyses of cell lysates or culture media of HepG2 cells transfected with PCSK9-containing plasmids were carried out as previously described ( ). .. Briefly, 24 h after transfection, cell lysates were obtained and run on 4-20% Tris-HCl Criterion Precast Gels (Bio-Rad) and blotted onto Immuno-Blot PVDF Membranes (Bio-Rad). .. The membranes were immunostained with a mouse IgG anti-FLAG antibody (Sigma-Aldrich Corp.).

SDS Page:

Article Title: Role of Tuberin in Neuronal Degeneration
Article Snippet: .. A total of 60 μg of protein from each sample was loaded on 4–20% SDS-PAGE Tris–HCl Criterion gradients gels (Bio-Rad) and samples were analyzed by western blot with antibodies as indicated in the figures. ..

Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation
Article Snippet: For mass spectrometry analyses, the number of peptides and coverage were calculated from values obtained using the Uniprot KB database. .. Western blot experiments were performed as previously described using 4–20% Criterion Tris-HCl pre-cast SDS-PAGE gels (Bio-Rad). .. DmLRPPRC2 and DmLRPPRC2-FLAG protein expression in inputs, F.T. and eluate fractions was determined by using the following primary antibodies: FLAG M2 (Sigma, dilution 1:500) and a polyclonal rabbit antiserum raised against DmLRPPRC2 (generated by PSL GmbH, dilution 1:1000).

Article Title: An Engineered Cysteine-Modified Diabody For Imaging Activated Leukocyte Cell Adhesion Molecule (ALCAM)-Positive Tumors
Article Snippet: .. Pre-cast 4–20% Tris-HCl SDS-PAGE gels (Bio-Rad) were loaded with aliquots of fractions and an anti-HER2 CysDb of known molecular weight derived from the sequence of trastuzumab [ , ], electrophoresed, and stained with InstantBlue (Novexin/Expedeon). .. Fractions containing purified anti-ALCAM CysDb were pooled and dialyzed against PBS using a Slide-A-Lyzer Dialysis Cassette (10,000 Da MWCO; Pierce Biotechnology).

Article Title: Fab-based inhibitors reveal ubiquitin independent functions for HIV Vif neutralization of APOBEC3 restriction factors
Article Snippet: Virus-like particles were isolated from culture supernatants by purification through 0.45μm PVDF filters (Millipore) followed by centrifugation (13,000 rpm for 2 hours) through a 20% sucrose, 1x PBS cushion and lysis directly in 2.5x Laemmli Sample Buffer. .. Immunoblotting Samples were run on 4–20% Tris-HCl SDS-PAGE gels (BioRad Criterion) at 150V for 90 minutes. .. Proteins were transferred to PVDF membranes by methanol-based electrotransfer (BioRad Criterion Blotter) at 90V for 2 hours.

Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation
Article Snippet: Note that Laemmli buffer (final concentration: 1% SDS, 5% Glycerol, 30 mM Tris, 0.005% Bromophenol Blue, 350 mM 2-Mercaptoethanol) was added and samples were split: three-fourth for mass-spectrometry and one-fourth for western blot experiments. .. For mass spectrometry analyses, samples were denatured at 95°C for 5 min followed by SDS-PAGE on 4–20% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad). .. The gels were silver stained through the SilverQuest™ Silver Staining (Invitrogen) or Coomassie stained through the Roti®-Blue quick solution (Roth).

Western Blot:

Article Title: Role of Tuberin in Neuronal Degeneration
Article Snippet: .. A total of 60 μg of protein from each sample was loaded on 4–20% SDS-PAGE Tris–HCl Criterion gradients gels (Bio-Rad) and samples were analyzed by western blot with antibodies as indicated in the figures. ..

Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation
Article Snippet: For mass spectrometry analyses, the number of peptides and coverage were calculated from values obtained using the Uniprot KB database. .. Western blot experiments were performed as previously described using 4–20% Criterion Tris-HCl pre-cast SDS-PAGE gels (Bio-Rad). .. DmLRPPRC2 and DmLRPPRC2-FLAG protein expression in inputs, F.T. and eluate fractions was determined by using the following primary antibodies: FLAG M2 (Sigma, dilution 1:500) and a polyclonal rabbit antiserum raised against DmLRPPRC2 (generated by PSL GmbH, dilution 1:1000).

Molecular Weight:

Article Title: An Engineered Cysteine-Modified Diabody For Imaging Activated Leukocyte Cell Adhesion Molecule (ALCAM)-Positive Tumors
Article Snippet: .. Pre-cast 4–20% Tris-HCl SDS-PAGE gels (Bio-Rad) were loaded with aliquots of fractions and an anti-HER2 CysDb of known molecular weight derived from the sequence of trastuzumab [ , ], electrophoresed, and stained with InstantBlue (Novexin/Expedeon). .. Fractions containing purified anti-ALCAM CysDb were pooled and dialyzed against PBS using a Slide-A-Lyzer Dialysis Cassette (10,000 Da MWCO; Pierce Biotechnology).

Derivative Assay:

Article Title: An Engineered Cysteine-Modified Diabody For Imaging Activated Leukocyte Cell Adhesion Molecule (ALCAM)-Positive Tumors
Article Snippet: .. Pre-cast 4–20% Tris-HCl SDS-PAGE gels (Bio-Rad) were loaded with aliquots of fractions and an anti-HER2 CysDb of known molecular weight derived from the sequence of trastuzumab [ , ], electrophoresed, and stained with InstantBlue (Novexin/Expedeon). .. Fractions containing purified anti-ALCAM CysDb were pooled and dialyzed against PBS using a Slide-A-Lyzer Dialysis Cassette (10,000 Da MWCO; Pierce Biotechnology).

Sequencing:

Article Title: An Engineered Cysteine-Modified Diabody For Imaging Activated Leukocyte Cell Adhesion Molecule (ALCAM)-Positive Tumors
Article Snippet: .. Pre-cast 4–20% Tris-HCl SDS-PAGE gels (Bio-Rad) were loaded with aliquots of fractions and an anti-HER2 CysDb of known molecular weight derived from the sequence of trastuzumab [ , ], electrophoresed, and stained with InstantBlue (Novexin/Expedeon). .. Fractions containing purified anti-ALCAM CysDb were pooled and dialyzed against PBS using a Slide-A-Lyzer Dialysis Cassette (10,000 Da MWCO; Pierce Biotechnology).

Staining:

Article Title: An Engineered Cysteine-Modified Diabody For Imaging Activated Leukocyte Cell Adhesion Molecule (ALCAM)-Positive Tumors
Article Snippet: .. Pre-cast 4–20% Tris-HCl SDS-PAGE gels (Bio-Rad) were loaded with aliquots of fractions and an anti-HER2 CysDb of known molecular weight derived from the sequence of trastuzumab [ , ], electrophoresed, and stained with InstantBlue (Novexin/Expedeon). .. Fractions containing purified anti-ALCAM CysDb were pooled and dialyzed against PBS using a Slide-A-Lyzer Dialysis Cassette (10,000 Da MWCO; Pierce Biotechnology).

Mass Spectrometry:

Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation
Article Snippet: Note that Laemmli buffer (final concentration: 1% SDS, 5% Glycerol, 30 mM Tris, 0.005% Bromophenol Blue, 350 mM 2-Mercaptoethanol) was added and samples were split: three-fourth for mass-spectrometry and one-fourth for western blot experiments. .. For mass spectrometry analyses, samples were denatured at 95°C for 5 min followed by SDS-PAGE on 4–20% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad). .. The gels were silver stained through the SilverQuest™ Silver Staining (Invitrogen) or Coomassie stained through the Roti®-Blue quick solution (Roth).

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  • 96
    Bio-Rad tris hcl gradient gel
    Western blot analysis of nuclear extracts from macrophages of pIpC-treated PPARγ-MXCre + mice and similarly treated PPARγ-MXCre − mice. A total of 10 μg of protein from nuclear extracts of macrophages and 10 μg of total protein from Hepa-1 cells transfected with an expression vector for PPARγ1 (pSG5-PPARγ cDNA) were subjected to electrophoresis on a 4 to 15% <t>Tris-HCl</t> gradient gel (Bio-Rad), transferred to <t>Immobilon-P</t> membranes (Millipore), and probed as recommended by the manufacturer with anti-PPARγ antibodies (Santa Cruz Biotechnologies) specific for the N terminus (E-8, PPARγ antibody) (A) and the C terminus (H-100, PPARγ antibody) (B) of the PPARγ protein. Detection of immunoreactive proteins was done by using an enhanced chemiluminescence blot detection system (Amersham).
    Tris Hcl Gradient Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tris hcl gradient gel/product/Bio-Rad
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tris hcl gradient gel - by Bioz Stars, 2021-03
    96/100 stars
      Buy from Supplier

    97
    Bio-Rad gradient sds polyacrylamide tris hcl gels
    2-DE separation of proteins extracted from leaves of healthy of Las-infected lemon plants. ( A ) Representative leaf and gel containing extracted proteins separated via 2-DE of a healthy lemon plant. ( B ) Representative leaf and gel containing extracted proteins separated via 2-DE of a Las-infected lemon plant. Two-year old healthy plants were either graft-inoculated with side shoots from PCR-confirmed Las-infected bud sticks or uninoculated and leaf samples were analyzed at six months post-inoculation. A sum of 200 µg of total protein was separated according to charge on a pH 4-7 IpG strip and according to mass on 8-16% gradient <t>SDS-polyacrylamide</t> <t>Tris-HCl</t> gels. Protein spots were visualized by staining with Coomassie Brilliant Blue (CBB). M r , relative molecular mass; pI, isoelectric point.
    Gradient Sds Polyacrylamide Tris Hcl Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gradient sds polyacrylamide tris hcl gels/product/Bio-Rad
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gradient sds polyacrylamide tris hcl gels - by Bioz Stars, 2021-03
    97/100 stars
      Buy from Supplier

    96
    Bio-Rad sds page tris hcl criterion gradients gels
    Tuberin was phosphorylated at threonine 1462 via the Akt–PTEN pathway in the frontal cortex of AD and PD/DLB patients. Total cell lysates were subjected to <t>SDS-PAGE</t> and then immunoblotted with antibodies to p-tuberin, tuberin, p-Akt, Akt, p-PTEN,
    Sds Page Tris Hcl Criterion Gradients Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sds page tris hcl criterion gradients gels/product/Bio-Rad
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sds page tris hcl criterion gradients gels - by Bioz Stars, 2021-03
    96/100 stars
      Buy from Supplier

    Image Search Results


    Western blot analysis of nuclear extracts from macrophages of pIpC-treated PPARγ-MXCre + mice and similarly treated PPARγ-MXCre − mice. A total of 10 μg of protein from nuclear extracts of macrophages and 10 μg of total protein from Hepa-1 cells transfected with an expression vector for PPARγ1 (pSG5-PPARγ cDNA) were subjected to electrophoresis on a 4 to 15% Tris-HCl gradient gel (Bio-Rad), transferred to Immobilon-P membranes (Millipore), and probed as recommended by the manufacturer with anti-PPARγ antibodies (Santa Cruz Biotechnologies) specific for the N terminus (E-8, PPARγ antibody) (A) and the C terminus (H-100, PPARγ antibody) (B) of the PPARγ protein. Detection of immunoreactive proteins was done by using an enhanced chemiluminescence blot detection system (Amersham).

    Journal: Molecular and Cellular Biology

    Article Title: Conditional Disruption of the Peroxisome Proliferator-Activated Receptor ? Gene in Mice Results in Lowered Expression of ABCA1, ABCG1, and apoE in Macrophages and Reduced Cholesterol Efflux

    doi: 10.1128/MCB.22.8.2607-2619.2002

    Figure Lengend Snippet: Western blot analysis of nuclear extracts from macrophages of pIpC-treated PPARγ-MXCre + mice and similarly treated PPARγ-MXCre − mice. A total of 10 μg of protein from nuclear extracts of macrophages and 10 μg of total protein from Hepa-1 cells transfected with an expression vector for PPARγ1 (pSG5-PPARγ cDNA) were subjected to electrophoresis on a 4 to 15% Tris-HCl gradient gel (Bio-Rad), transferred to Immobilon-P membranes (Millipore), and probed as recommended by the manufacturer with anti-PPARγ antibodies (Santa Cruz Biotechnologies) specific for the N terminus (E-8, PPARγ antibody) (A) and the C terminus (H-100, PPARγ antibody) (B) of the PPARγ protein. Detection of immunoreactive proteins was done by using an enhanced chemiluminescence blot detection system (Amersham).

    Article Snippet: Then, 10 μg of total protein from Hepa-1 cells and 10 μg of protein from nuclear extracts of macrophages were subjected to electrophoresis on a 4 to 15% Tris-HCl gradient gel (Bio-Rad, Hercules, Calif.), transferred to Immobilon-P membranes (Millipore, Bedford, Mass.), and probed according to the manufacturer's recommendations with anti-PPARγ antibodies (E-8 and H-100; Santa Cruz Biotechnology, Inc., Santa Cruz, Calif.) as indicated.

    Techniques: Western Blot, Mouse Assay, Transfection, Expressing, Plasmid Preparation, Electrophoresis

    2-DE separation of proteins extracted from leaves of healthy of Las-infected lemon plants. ( A ) Representative leaf and gel containing extracted proteins separated via 2-DE of a healthy lemon plant. ( B ) Representative leaf and gel containing extracted proteins separated via 2-DE of a Las-infected lemon plant. Two-year old healthy plants were either graft-inoculated with side shoots from PCR-confirmed Las-infected bud sticks or uninoculated and leaf samples were analyzed at six months post-inoculation. A sum of 200 µg of total protein was separated according to charge on a pH 4-7 IpG strip and according to mass on 8-16% gradient SDS-polyacrylamide Tris-HCl gels. Protein spots were visualized by staining with Coomassie Brilliant Blue (CBB). M r , relative molecular mass; pI, isoelectric point.

    Journal: PLoS ONE

    Article Title: Study on Citrus Response to Huanglongbing Highlights a Down-Regulation of Defense-Related Proteins in Lemon Plants Upon 'Ca. Liberibacter asiaticus' Infection

    doi: 10.1371/journal.pone.0067442

    Figure Lengend Snippet: 2-DE separation of proteins extracted from leaves of healthy of Las-infected lemon plants. ( A ) Representative leaf and gel containing extracted proteins separated via 2-DE of a healthy lemon plant. ( B ) Representative leaf and gel containing extracted proteins separated via 2-DE of a Las-infected lemon plant. Two-year old healthy plants were either graft-inoculated with side shoots from PCR-confirmed Las-infected bud sticks or uninoculated and leaf samples were analyzed at six months post-inoculation. A sum of 200 µg of total protein was separated according to charge on a pH 4-7 IpG strip and according to mass on 8-16% gradient SDS-polyacrylamide Tris-HCl gels. Protein spots were visualized by staining with Coomassie Brilliant Blue (CBB). M r , relative molecular mass; pI, isoelectric point.

    Article Snippet: Second dimension electrophoresis was performed in 8-16% gradient SDS-polyacrylamide Tris-HCl gels (Criterion precast gels, Bio-Rad) in a twelve-gel cell system (Criterion Dodeca Cell, Bio-Rad).

    Techniques: Infection, Polymerase Chain Reaction, Stripping Membranes, Staining

    PDQuest-generated master gel image showing the general spot pattern of matched protein spots from the total leaf proteome of healthy or Las-infected lemon plants. Labeled spots were differentially produced in response to Las-infection and described in Table 1 . A sum of 200 µg of total protein was separated according to charge on a pH 4-7 IpG strip and according to mass on 8-16% gradient SDS-polyacrylamide Tris-HCl gels. Protein spots were visualized by staining with Coomassie Brilliant Blue (CBB). M r , relative molecular mass; pI, isoelectric point.

    Journal: PLoS ONE

    Article Title: Study on Citrus Response to Huanglongbing Highlights a Down-Regulation of Defense-Related Proteins in Lemon Plants Upon 'Ca. Liberibacter asiaticus' Infection

    doi: 10.1371/journal.pone.0067442

    Figure Lengend Snippet: PDQuest-generated master gel image showing the general spot pattern of matched protein spots from the total leaf proteome of healthy or Las-infected lemon plants. Labeled spots were differentially produced in response to Las-infection and described in Table 1 . A sum of 200 µg of total protein was separated according to charge on a pH 4-7 IpG strip and according to mass on 8-16% gradient SDS-polyacrylamide Tris-HCl gels. Protein spots were visualized by staining with Coomassie Brilliant Blue (CBB). M r , relative molecular mass; pI, isoelectric point.

    Article Snippet: Second dimension electrophoresis was performed in 8-16% gradient SDS-polyacrylamide Tris-HCl gels (Criterion precast gels, Bio-Rad) in a twelve-gel cell system (Criterion Dodeca Cell, Bio-Rad).

    Techniques: Generated, Infection, Labeling, Produced, Stripping Membranes, Staining

    Differentially produced protein spots from 2-DE analysis of total leaf proteins from healthy or Las-infected lemon plants. Panels A-M show magnified views of protein spots in representative 2-DE gels containing separated total proteins from leaves of healthy or Las-infected lemon plants. Labeled spots showed significant changes and correspond to the spots presented in in Figure 2 and Tables 2 and 3 . Two-year old healthy plants were either graft-inoculated with side shoots from PCR-confirmed Las-infected bud sticks or uninoculated and leaf samples were analyzed at six months post-inoculation. A sum of 200 µg of total protein was separated according to charge on a pH 4-7 IpG strip and according to mass on 8-16% gradient SDS-polyacrylamide Tris-HCl gels. Protein spots were visualized by staining with Coomassie Brilliant Blue (CBB). M r , relative molecular mass; pI, isoelectric point.

    Journal: PLoS ONE

    Article Title: Study on Citrus Response to Huanglongbing Highlights a Down-Regulation of Defense-Related Proteins in Lemon Plants Upon 'Ca. Liberibacter asiaticus' Infection

    doi: 10.1371/journal.pone.0067442

    Figure Lengend Snippet: Differentially produced protein spots from 2-DE analysis of total leaf proteins from healthy or Las-infected lemon plants. Panels A-M show magnified views of protein spots in representative 2-DE gels containing separated total proteins from leaves of healthy or Las-infected lemon plants. Labeled spots showed significant changes and correspond to the spots presented in in Figure 2 and Tables 2 and 3 . Two-year old healthy plants were either graft-inoculated with side shoots from PCR-confirmed Las-infected bud sticks or uninoculated and leaf samples were analyzed at six months post-inoculation. A sum of 200 µg of total protein was separated according to charge on a pH 4-7 IpG strip and according to mass on 8-16% gradient SDS-polyacrylamide Tris-HCl gels. Protein spots were visualized by staining with Coomassie Brilliant Blue (CBB). M r , relative molecular mass; pI, isoelectric point.

    Article Snippet: Second dimension electrophoresis was performed in 8-16% gradient SDS-polyacrylamide Tris-HCl gels (Criterion precast gels, Bio-Rad) in a twelve-gel cell system (Criterion Dodeca Cell, Bio-Rad).

    Techniques: Produced, Infection, Labeling, Polymerase Chain Reaction, Stripping Membranes, Staining

    Experimental strategy for comparing peptide- vs protein-level enrichments. (A) Experimental design applying on-resin iTRAQ-labeling. (B) Silver-staining image of SDS–PAGE of enriched Cys-peptides. For each lane of the 4–20% Tris–HCl precast gel, 5 of 30 μl of DTT-eluted Cys-peptides was loaded. The higher protein bands in protein-level enrichment samples indicate incomplete on-resin digestion. (C) An MS/MS spectrum of the Cys-peptide GVLECQVSR from obscurin protein and its zoom-in spectrum of reporter-ion region showing the SNO abundance increased in response to GSNO treatment.

    Journal: Free radical biology & medicine

    Article Title: Quantitative site-specific reactivity profiling of S-nitrosylation in mouse skeletal muscle using cysteinyl peptide enrichment coupled with mass spectrometry

    doi: 10.1016/j.freeradbiomed.2012.12.010

    Figure Lengend Snippet: Experimental strategy for comparing peptide- vs protein-level enrichments. (A) Experimental design applying on-resin iTRAQ-labeling. (B) Silver-staining image of SDS–PAGE of enriched Cys-peptides. For each lane of the 4–20% Tris–HCl precast gel, 5 of 30 μl of DTT-eluted Cys-peptides was loaded. The higher protein bands in protein-level enrichment samples indicate incomplete on-resin digestion. (C) An MS/MS spectrum of the Cys-peptide GVLECQVSR from obscurin protein and its zoom-in spectrum of reporter-ion region showing the SNO abundance increased in response to GSNO treatment.

    Article Snippet: SDS–PAGE was carried out with a 4–20% precast linear gradient Tris–HCl polyacrylamide gel (Bio-Rad) to assess enrichment efficiency and total SNO levels.

    Techniques: Labeling, Silver Staining, SDS Page, Mass Spectrometry

    Tuberin was phosphorylated at threonine 1462 via the Akt–PTEN pathway in the frontal cortex of AD and PD/DLB patients. Total cell lysates were subjected to SDS-PAGE and then immunoblotted with antibodies to p-tuberin, tuberin, p-Akt, Akt, p-PTEN,

    Journal:

    Article Title: Role of Tuberin in Neuronal Degeneration

    doi: 10.1007/s11064-007-9558-8

    Figure Lengend Snippet: Tuberin was phosphorylated at threonine 1462 via the Akt–PTEN pathway in the frontal cortex of AD and PD/DLB patients. Total cell lysates were subjected to SDS-PAGE and then immunoblotted with antibodies to p-tuberin, tuberin, p-Akt, Akt, p-PTEN,

    Article Snippet: A total of 60 μg of protein from each sample was loaded on 4–20% SDS-PAGE Tris–HCl Criterion gradients gels (Bio-Rad) and samples were analyzed by western blot with antibodies as indicated in the figures.

    Techniques: SDS Page