Structured Review

Bio-Rad tris glycine precast gel
Pathogenic anti-DNA antibodies bind to <t>HMGB1.</t> (A) HMGB1 was electrophoresed in a 10–20% <t>Tris-Glycine</t> gel, transferred to a PVDF membrane, and immunoblotted with the DNAse pretreated (+) or DNAse untreated (−) monoclonal antibodies indicated
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Images

1) Product Images from "Pathogenic Anti-DNA Antibodies Modulate Gene Expression in Mesangial Cells:"

Article Title: Pathogenic Anti-DNA Antibodies Modulate Gene Expression in Mesangial Cells:

Journal: Immunology letters

doi: 10.1016/j.imlet.2008.08.007

Pathogenic anti-DNA antibodies bind to HMGB1. (A) HMGB1 was electrophoresed in a 10–20% Tris-Glycine gel, transferred to a PVDF membrane, and immunoblotted with the DNAse pretreated (+) or DNAse untreated (−) monoclonal antibodies indicated
Figure Legend Snippet: Pathogenic anti-DNA antibodies bind to HMGB1. (A) HMGB1 was electrophoresed in a 10–20% Tris-Glycine gel, transferred to a PVDF membrane, and immunoblotted with the DNAse pretreated (+) or DNAse untreated (−) monoclonal antibodies indicated

Techniques Used:

Related Articles

SDS Page:

Article Title: Molecular Topology of RNA Polymerase I Upstream Activation Factor
Article Snippet: Protein-bound beads were washed four times with wash buffer (20 mM Tris-HCl [pH 8.0], 20% glycerol, 0.1% Tween 20, and 450 mM KCl) and eluted three times with two bead volumes of elution buffer (wash buffer supplemented with 250 mM imidazole). .. Eluted proteins were separated on 4 to 20% Tris-glycine SDS-PAGE gel (Bio-Rad) and analyzed by Western blotting using the following antibodies: anti-histone H3 (ab46765; Abcam), anti-histone H4 (ab10158; Abcam), anti-Flag (F3165; Sigma) for Uaf30, and rabbit polyclonal antibodies against Rrn10, Rrn5, or Rrn9 (Knutson laboratory via Reeder laboratory). ..

Article Title: Stoichiometry and structure of a lantibiotic maturation complex
Article Snippet: A 50 μL reaction mixture consisting of 20 μM NisB, 160 μM NisC and 200 μM prenisin peptide variant was incubated for 1 h at 25 °C and subsequently applied to SEC analysis. .. After co-elution, the corresponding fractions were analyzed by a 4–20% gradient Tris-Glycine SDS-PAGE (Biorad) gel stained with Page-Blue (Thermo Fisher). .. Immunoblotting and SDS-PAGE analysis All SDS-PAGE and Western blotting experiments were performed with standard laboratory techniques .

Article Title: A Comparative Study of Lectin Affinity Based Plant N-Glycoproteome Profiling Using Tomato Fruit as a Model *
Article Snippet: The recombinant XEGIP was eluted from the beads with acidic buffer (glycine-HCl pH 3.0, 0.1% Triton X-100, and 150 m m NaCl). .. The purified recombinant XEGIP was fractionated on 12% Tris-glycine SDS-PAGE gels (TGXTM gels, Bio-Rad) and stained with Coomassie brilliant blue R-250 (Calbiochem, Darmstadt, Germany). ..

Article Title: Uncovering inherent cellular plasticity of multiciliated ependyma leading to ventricular wall transformation and hydrocephalus
Article Snippet: Biochemistry and immunoprecipitation Cell cultures or tissue samples were lysed and prepared for immunoblotting as described previously , . .. Lysates were resolved on Tris-Glycine SDS-PAGE gels (Bio-Rad) and transferred onto PVDF membranes (Bio-Rad). .. Antibodies were diluted in PBS containing 0.1% Triton-X100 with 2% BSA, followed by overnight incubation at 4 °C.

Western Blot:

Article Title: Molecular Topology of RNA Polymerase I Upstream Activation Factor
Article Snippet: Protein-bound beads were washed four times with wash buffer (20 mM Tris-HCl [pH 8.0], 20% glycerol, 0.1% Tween 20, and 450 mM KCl) and eluted three times with two bead volumes of elution buffer (wash buffer supplemented with 250 mM imidazole). .. Eluted proteins were separated on 4 to 20% Tris-glycine SDS-PAGE gel (Bio-Rad) and analyzed by Western blotting using the following antibodies: anti-histone H3 (ab46765; Abcam), anti-histone H4 (ab10158; Abcam), anti-Flag (F3165; Sigma) for Uaf30, and rabbit polyclonal antibodies against Rrn10, Rrn5, or Rrn9 (Knutson laboratory via Reeder laboratory). ..

Article Title: Super elongation complex contains a TFIIF-related subcomplex
Article Snippet: .. Bead-bound proteins were eluted three times with His6 Elution buffer (20 mM Tris-HCl pH 7.5, 200 mM KCl, 10% Glycerol, 0.1 mM EDTA, 250 mM Imidazole, 0.05% Tergitol) and then separated on a 4–20% Tris-Glycine SDS-PAGE gel (Biorad) and analyzed by Western blot using antibodies anti-His6 (Thermo Scientific, His.H8) and anti-Myc (Thermo Scientific, Myc.A7). ..

Co-Elution Assay:

Article Title: Stoichiometry and structure of a lantibiotic maturation complex
Article Snippet: A 50 μL reaction mixture consisting of 20 μM NisB, 160 μM NisC and 200 μM prenisin peptide variant was incubated for 1 h at 25 °C and subsequently applied to SEC analysis. .. After co-elution, the corresponding fractions were analyzed by a 4–20% gradient Tris-Glycine SDS-PAGE (Biorad) gel stained with Page-Blue (Thermo Fisher). .. Immunoblotting and SDS-PAGE analysis All SDS-PAGE and Western blotting experiments were performed with standard laboratory techniques .

Staining:

Article Title: Stoichiometry and structure of a lantibiotic maturation complex
Article Snippet: A 50 μL reaction mixture consisting of 20 μM NisB, 160 μM NisC and 200 μM prenisin peptide variant was incubated for 1 h at 25 °C and subsequently applied to SEC analysis. .. After co-elution, the corresponding fractions were analyzed by a 4–20% gradient Tris-Glycine SDS-PAGE (Biorad) gel stained with Page-Blue (Thermo Fisher). .. Immunoblotting and SDS-PAGE analysis All SDS-PAGE and Western blotting experiments were performed with standard laboratory techniques .

Article Title: A Comparative Study of Lectin Affinity Based Plant N-Glycoproteome Profiling Using Tomato Fruit as a Model *
Article Snippet: The recombinant XEGIP was eluted from the beads with acidic buffer (glycine-HCl pH 3.0, 0.1% Triton X-100, and 150 m m NaCl). .. The purified recombinant XEGIP was fractionated on 12% Tris-glycine SDS-PAGE gels (TGXTM gels, Bio-Rad) and stained with Coomassie brilliant blue R-250 (Calbiochem, Darmstadt, Germany). ..

Polyacrylamide Gel Electrophoresis:

Article Title: Stoichiometry and structure of a lantibiotic maturation complex
Article Snippet: A 50 μL reaction mixture consisting of 20 μM NisB, 160 μM NisC and 200 μM prenisin peptide variant was incubated for 1 h at 25 °C and subsequently applied to SEC analysis. .. After co-elution, the corresponding fractions were analyzed by a 4–20% gradient Tris-Glycine SDS-PAGE (Biorad) gel stained with Page-Blue (Thermo Fisher). .. Immunoblotting and SDS-PAGE analysis All SDS-PAGE and Western blotting experiments were performed with standard laboratory techniques .

Purification:

Article Title: A Comparative Study of Lectin Affinity Based Plant N-Glycoproteome Profiling Using Tomato Fruit as a Model *
Article Snippet: The recombinant XEGIP was eluted from the beads with acidic buffer (glycine-HCl pH 3.0, 0.1% Triton X-100, and 150 m m NaCl). .. The purified recombinant XEGIP was fractionated on 12% Tris-glycine SDS-PAGE gels (TGXTM gels, Bio-Rad) and stained with Coomassie brilliant blue R-250 (Calbiochem, Darmstadt, Germany). ..

Recombinant:

Article Title: A Comparative Study of Lectin Affinity Based Plant N-Glycoproteome Profiling Using Tomato Fruit as a Model *
Article Snippet: The recombinant XEGIP was eluted from the beads with acidic buffer (glycine-HCl pH 3.0, 0.1% Triton X-100, and 150 m m NaCl). .. The purified recombinant XEGIP was fractionated on 12% Tris-glycine SDS-PAGE gels (TGXTM gels, Bio-Rad) and stained with Coomassie brilliant blue R-250 (Calbiochem, Darmstadt, Germany). ..

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    Bio-Rad tris tricine precast gels
    The ~55- and the ~15- kDa, 6E10-immunoreactive species contain APP metabolites located N-terminally of Aβ. (A) CSF samples were first immunodepleted using the antibodies noted above each lane, and then subjected to immunoprec ipitation with 6E10, and WB was probed with biotinylated 6E10. Immunodepletion with 6E10 removed both the ~55- (arrowhead) and the ~15- kDa (arrows) proteins as expected. Immunodepletion with the 1G6 antibody fully removed the ~15-kDa species and partially removed the ~55-kDa species, indicating the presence of APP fragments located N-terminally of Aβ in these bands. In contrast, an antibody directed against the C-terminus (CT) of APP and the antibody 4G8 failed to deplete the ~55- and the ~15- kDa, 6E10-immunoreactive proteins. Note that the blot was transferred from a 10–20% <t>Tris-Tricine</t> gel. (B) In different CSF samples, immunodepletion with the antibody 1G6 did not reduce levels of the ~55-kDa band, but almost fully eliminated the ~15-kDa band. Immunodepletion with mouse IgG (msIgG) served as a negative control. Note that the blot was transferred from a 10.5–14% Tris-HCl gel.
    Tris Tricine Precast Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Bio-Rad tris glycine gels
    Aβ species including oAβ are present in both extracellular and intracellular fractions from young TgCRND8 mouse brains. Levels of human Aβ40 ( A , B ), human/rodent Aβ42 ( C , D ), and oAβ ( E , F ) were measured in the <t>Tris-soluble,</t> extracellular enriched fraction and the <t>RIPA-extracted</t> intracellular vesicle fraction from 2-mo-old (preamyloid deposition) TgCRND8 mouse brains ( n = 10). Identically prepared extracts from wild-type (wt) littermates ( n = 5) were included as controls to validate Aβ measurements in transgenic mice. For every assay, the signal in TgCRND8 transgenic mice was significantly higher than in wild-type mice. ** P
    Tris Glycine 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/tris glycine gels/product/Bio-Rad
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tris glycine gels - by Bioz Stars, 2021-04
    97/100 stars
      Buy from Supplier

    Image Search Results


    The ~55- and the ~15- kDa, 6E10-immunoreactive species contain APP metabolites located N-terminally of Aβ. (A) CSF samples were first immunodepleted using the antibodies noted above each lane, and then subjected to immunoprec ipitation with 6E10, and WB was probed with biotinylated 6E10. Immunodepletion with 6E10 removed both the ~55- (arrowhead) and the ~15- kDa (arrows) proteins as expected. Immunodepletion with the 1G6 antibody fully removed the ~15-kDa species and partially removed the ~55-kDa species, indicating the presence of APP fragments located N-terminally of Aβ in these bands. In contrast, an antibody directed against the C-terminus (CT) of APP and the antibody 4G8 failed to deplete the ~55- and the ~15- kDa, 6E10-immunoreactive proteins. Note that the blot was transferred from a 10–20% Tris-Tricine gel. (B) In different CSF samples, immunodepletion with the antibody 1G6 did not reduce levels of the ~55-kDa band, but almost fully eliminated the ~15-kDa band. Immunodepletion with mouse IgG (msIgG) served as a negative control. Note that the blot was transferred from a 10.5–14% Tris-HCl gel.

    Journal: PLoS ONE

    Article Title: Human cerebrospinal fluid 6E10-immunoreactive protein species contain amyloid precursor protein fragments

    doi: 10.1371/journal.pone.0212815

    Figure Lengend Snippet: The ~55- and the ~15- kDa, 6E10-immunoreactive species contain APP metabolites located N-terminally of Aβ. (A) CSF samples were first immunodepleted using the antibodies noted above each lane, and then subjected to immunoprec ipitation with 6E10, and WB was probed with biotinylated 6E10. Immunodepletion with 6E10 removed both the ~55- (arrowhead) and the ~15- kDa (arrows) proteins as expected. Immunodepletion with the 1G6 antibody fully removed the ~15-kDa species and partially removed the ~55-kDa species, indicating the presence of APP fragments located N-terminally of Aβ in these bands. In contrast, an antibody directed against the C-terminus (CT) of APP and the antibody 4G8 failed to deplete the ~55- and the ~15- kDa, 6E10-immunoreactive proteins. Note that the blot was transferred from a 10–20% Tris-Tricine gel. (B) In different CSF samples, immunodepletion with the antibody 1G6 did not reduce levels of the ~55-kDa band, but almost fully eliminated the ~15-kDa band. Immunodepletion with mouse IgG (msIgG) served as a negative control. Note that the blot was transferred from a 10.5–14% Tris-HCl gel.

    Article Snippet: Proteins were eluted by boiling the magnetic beads at 95°C in 30 μL of sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) loading buffer (500 mM Tris-HCl, 24% (v/v) glycerol, 8% (w/v) SDS, 0.01% (w/v) Coomassie brilliant blue, 0.1% (v/v) phenol red, 710 mM β-mercaptoethanol, pH 8.0); elutates were size-fractionated on 10.5–14% Tris-HCl or 10–20% Tris-Tricine precast gels (Bio-Rad, Hercules, CA), and electrophoretically transferred onto 0.2-μm nitrocellulose membranes at a constant current of 0.4 A for 3 hr at 4°C.

    Techniques: Western Blot, Negative Control

    Heterologous expression of spider dragline silk proteins in the recombinant marine photosynthetic bacterium Rhodovulum sulfidophilum under photoheterotrophic conditions. a A recombinant R. sulfidophilum harboring the broad-host-range vector pBBR1MCS-2 with a MaSp1 repetitive domain from Nephila clavipes was developed to express spider dragline silk protein. b A gene cassette containing the trc promoter (P trc ) and MaSp1 -(1-mer, 2-mer, 3-mer, and 6-mer) was inserted into pBBR1MCS-2, and a histidine tag was present at the N -terminus of MaSp1 (pink-color box). c Tris-Tricine SDS-PAGE (16.5%) of soluble proteins from four days of recombinant R. sulfidophilum cultures. d Western blot using monoclonal anti-His•Tag antibody, which targets histidine-tagged MaSp1-(1-mer, 2-mer, 3-mer, or 6-mer) proteins.

    Journal: Communications Biology

    Article Title: A marine photosynthetic microbial cell factory as a platform for spider silk production

    doi: 10.1038/s42003-020-1099-6

    Figure Lengend Snippet: Heterologous expression of spider dragline silk proteins in the recombinant marine photosynthetic bacterium Rhodovulum sulfidophilum under photoheterotrophic conditions. a A recombinant R. sulfidophilum harboring the broad-host-range vector pBBR1MCS-2 with a MaSp1 repetitive domain from Nephila clavipes was developed to express spider dragline silk protein. b A gene cassette containing the trc promoter (P trc ) and MaSp1 -(1-mer, 2-mer, 3-mer, and 6-mer) was inserted into pBBR1MCS-2, and a histidine tag was present at the N -terminus of MaSp1 (pink-color box). c Tris-Tricine SDS-PAGE (16.5%) of soluble proteins from four days of recombinant R. sulfidophilum cultures. d Western blot using monoclonal anti-His•Tag antibody, which targets histidine-tagged MaSp1-(1-mer, 2-mer, 3-mer, or 6-mer) proteins.

    Article Snippet: Soluble proteins were resolved via SDS-PAGE by using a 16.5% Mini-PROTEAN® Tris-Tricine precast gel (Bio-Rad).

    Techniques: Expressing, Recombinant, Plasmid Preparation, SDS Page, Western Blot

    Aβ species including oAβ are present in both extracellular and intracellular fractions from young TgCRND8 mouse brains. Levels of human Aβ40 ( A , B ), human/rodent Aβ42 ( C , D ), and oAβ ( E , F ) were measured in the Tris-soluble, extracellular enriched fraction and the RIPA-extracted intracellular vesicle fraction from 2-mo-old (preamyloid deposition) TgCRND8 mouse brains ( n = 10). Identically prepared extracts from wild-type (wt) littermates ( n = 5) were included as controls to validate Aβ measurements in transgenic mice. For every assay, the signal in TgCRND8 transgenic mice was significantly higher than in wild-type mice. ** P

    Journal: The FASEB Journal

    Article Title: Intracellular metalloprotease activity controls intraneuronal Aβ aggregation and limits secretion of Aβ via exosomes

    doi: 10.1096/fj.201801319R

    Figure Lengend Snippet: Aβ species including oAβ are present in both extracellular and intracellular fractions from young TgCRND8 mouse brains. Levels of human Aβ40 ( A , B ), human/rodent Aβ42 ( C , D ), and oAβ ( E , F ) were measured in the Tris-soluble, extracellular enriched fraction and the RIPA-extracted intracellular vesicle fraction from 2-mo-old (preamyloid deposition) TgCRND8 mouse brains ( n = 10). Identically prepared extracts from wild-type (wt) littermates ( n = 5) were included as controls to validate Aβ measurements in transgenic mice. For every assay, the signal in TgCRND8 transgenic mice was significantly higher than in wild-type mice. ** P

    Article Snippet: Extracellular vesicle proteins were extracted in RIPA buffer, electrophoresed on 4–20% Tris-glycine gels (Criterion Precast Gel; Bio-Rad, Hercules, CA, USA), and transferred to PVDF membranes (Immobilon; MilliporeSigma).

    Techniques: Transgenic Assay, Mouse Assay

    Intracerebroventricular administration of PA to TgCRND8 and wild-type mice increases extracellular and intracellular Aβ. Aβ species were measured 16 h after icv administration of PA to TgCRND8 mice ( A , B ) and wild-type mice ( C , D ). A , B ) Levels of Tris-soluble extracellular ( A ) and RIPA-soluble intracellular ( B ) Aβ40 and Aβ42 were increased in transgenic mouse brains after PA injection. C , D ) Levels of endogenous rodent Aβ40 and Aβ42 were also increased in extracellular ( C ) and intracellular ( D ) fractions of wild-type mouse brains after PA injection. Intracellular Aβ from wild-type mice was purified and concentrated by solid-phase extraction before measurement by ELISA (for TgCRND8 mice, n = 8 for Aβ40 and n = 10 for Aβ42; for wild-type mice, n = 6 for all groups). **** P

    Journal: The FASEB Journal

    Article Title: Intracellular metalloprotease activity controls intraneuronal Aβ aggregation and limits secretion of Aβ via exosomes

    doi: 10.1096/fj.201801319R

    Figure Lengend Snippet: Intracerebroventricular administration of PA to TgCRND8 and wild-type mice increases extracellular and intracellular Aβ. Aβ species were measured 16 h after icv administration of PA to TgCRND8 mice ( A , B ) and wild-type mice ( C , D ). A , B ) Levels of Tris-soluble extracellular ( A ) and RIPA-soluble intracellular ( B ) Aβ40 and Aβ42 were increased in transgenic mouse brains after PA injection. C , D ) Levels of endogenous rodent Aβ40 and Aβ42 were also increased in extracellular ( C ) and intracellular ( D ) fractions of wild-type mouse brains after PA injection. Intracellular Aβ from wild-type mice was purified and concentrated by solid-phase extraction before measurement by ELISA (for TgCRND8 mice, n = 8 for Aβ40 and n = 10 for Aβ42; for wild-type mice, n = 6 for all groups). **** P

    Article Snippet: Extracellular vesicle proteins were extracted in RIPA buffer, electrophoresed on 4–20% Tris-glycine gels (Criterion Precast Gel; Bio-Rad, Hercules, CA, USA), and transferred to PVDF membranes (Immobilon; MilliporeSigma).

    Techniques: Mouse Assay, Transgenic Assay, Injection, Purification, Enzyme-linked Immunosorbent Assay