criterion precast polyacrylamide gel  (Bio-Rad)

 
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    Name:
    Acrylamide
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    100 g 99 9 pure acrylamide powder
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    Bio-Rad criterion precast polyacrylamide gel
    Acrylamide
    100 g 99 9 pure acrylamide powder
    https://www.bioz.com/result/criterion precast polyacrylamide gel/product/Bio-Rad
    Average 99 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    criterion precast polyacrylamide gel - by Bioz Stars, 2020-09
    99/100 stars

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    Related Articles

    Nucleic Acid Electrophoresis:

    Article Title: Native Outer Membrane Proteins Protect Mice against Pulmonary Challenge with Virulent Type A Francisella tularensis
    Article Snippet: .. Equal amounts of LPS, iLVS, and OMP preparations were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and either visualized by silver staining (Silver Stain Plus; Bio-Rad) or transferred to nitrocellulose for immunoblot analysis as previously described ( ). .. For comparison of the antigen preparations by immunoblotting, the relative amount of LPS in each antigen preparation was visualized using mouse monoclonal antibody FB11 to F. tularensis LPS (Abcam, Cambridge, MA).

    Article Title: Characterization of the Protocatechuic Acid Catabolic Gene Cluster from Streptomyces sp. Strain 2065
    Article Snippet: .. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed on a Bio-Rad (Mississauga, Ontario, Canada) Miniprotein II apparatus with 13% polyacrylamide gels using the modified procedure of Laemmli ( ). ..

    Article Title: Microaerophilic Induction of the Alpha-Crystallin Chaperone Protein Homologue (hspX) mRNA of Mycobacterium tuberculosis
    Article Snippet: .. Twenty micrograms of protein for each sample was separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using a Tris-tricine 16.5% polyacrylamide gel (Bio-Rad). .. The gel was stained and the protein was transferred to a nitrocellulose paper (Schleicher & Schuell, Keene, N.H.) for Western blotting.

    Article Title: Polyamidoamine Nanoparticles for the Oral Administration of Antimalarial Drugs
    Article Snippet: .. For SDS-polyacrylamide gel electrophoresis (PAGE) analysis, samples were heated at 90 °C for 5 min in an elution buffer, and electrophoresed in 1 mm-thick 12.5% SDS-polyacrylamide gels (Mini Protean II System, Bio-Rad), which were silver-stained as previously described [ ]. .. For the identification of PAA-binding pRBC proteins (see below), a second gel was fixed with acetic acid:ethanol:ddH2 O (1:4:5) and stained with colloidal Coomassie Blue in 20% methanol.

    Silver Staining:

    Article Title: Native Outer Membrane Proteins Protect Mice against Pulmonary Challenge with Virulent Type A Francisella tularensis
    Article Snippet: .. Equal amounts of LPS, iLVS, and OMP preparations were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and either visualized by silver staining (Silver Stain Plus; Bio-Rad) or transferred to nitrocellulose for immunoblot analysis as previously described ( ). .. For comparison of the antigen preparations by immunoblotting, the relative amount of LPS in each antigen preparation was visualized using mouse monoclonal antibody FB11 to F. tularensis LPS (Abcam, Cambridge, MA).

    Purification:

    Article Title: Enhanced-Transient Expression of Hepatitis C Virus Core Protein in Nicotiana tabacum, a Protein With Potential Clinical Applications
    Article Snippet: .. For SDS-PAGE and western blotting analyses, purified HCV core from E. coli and plant and plant crude extracts of the recombinant HCV core protein expressed by P19 co-agroinfiltrated pBI121 and PVX vectors were loaded onto a 12% SDS-polyacrylamide gel; by the end of electrophoresis, the protein bands were either stained with coomassie brilliant blue (Bio-Rad) or transferred to the PVDF membrane. .. Subsequently, the corresponding protein bands on the membrane were identified by biotinylated anti-core polyclonal antibody (Abcam, UK) (1:1000 dilution) and streptavidin HRP conjugate (Sigma, USA) (1:4000 dilution), respectively, and were detected by TMB as substrate.

    Electrophoresis:

    Article Title: Interaction of local anesthetics with the K+ channel pore domain
    Article Snippet: .. Ten milliliters of each sample was pipetted into wells of precast 12% acrylamide TRIS-HCl ready SDS-PAGE Gels (Bio-Rad) and subjected to electrophoresis at 200V for ~35 min in running buffer (25 mM Tris base, 192 mM glycine, pH 8.3, 0.1% SDS). .. The gel was rinsed in deionized H2 O for 7 min and stained with GelCode Blue Stain Reagent for 1 h, rinsed for 1 h and destained overnight in deionized H2 O.

    Article Title: Time-resolved and steady-state fluorescence quenching of N-acetyl-l-tryptophanamide by acrylamide and iodide
    Article Snippet: .. NATA was from Aldrich and acrylamide ( > 99.9%) electrophoresis purity reagent (lot 32285) was from Bio-Rad. .. Potassium iodide was from Sigma and 1,2-propanediol (propylene glycol) (P.A. grade) was from Janssen Chimica.

    Article Title: Enhanced-Transient Expression of Hepatitis C Virus Core Protein in Nicotiana tabacum, a Protein With Potential Clinical Applications
    Article Snippet: .. For SDS-PAGE and western blotting analyses, purified HCV core from E. coli and plant and plant crude extracts of the recombinant HCV core protein expressed by P19 co-agroinfiltrated pBI121 and PVX vectors were loaded onto a 12% SDS-polyacrylamide gel; by the end of electrophoresis, the protein bands were either stained with coomassie brilliant blue (Bio-Rad) or transferred to the PVDF membrane. .. Subsequently, the corresponding protein bands on the membrane were identified by biotinylated anti-core polyclonal antibody (Abcam, UK) (1:1000 dilution) and streptavidin HRP conjugate (Sigma, USA) (1:4000 dilution), respectively, and were detected by TMB as substrate.

    Polyacrylamide Gel Electrophoresis:

    Article Title: Polyamidoamine Nanoparticles for the Oral Administration of Antimalarial Drugs
    Article Snippet: .. For SDS-polyacrylamide gel electrophoresis (PAGE) analysis, samples were heated at 90 °C for 5 min in an elution buffer, and electrophoresed in 1 mm-thick 12.5% SDS-polyacrylamide gels (Mini Protean II System, Bio-Rad), which were silver-stained as previously described [ ]. .. For the identification of PAA-binding pRBC proteins (see below), a second gel was fixed with acetic acid:ethanol:ddH2 O (1:4:5) and stained with colloidal Coomassie Blue in 20% methanol.

    Staining:

    Article Title: The third helix of the homeodomain of paired class homeodomain proteins acts as a recognition helix both for DNA and protein interactions
    Article Snippet: .. The GST fusion proteins were analyzed on a 10% SDS–polyacrylamide gel and quantified using SYPRO® Ruby protein stain (Bio-Rad) and LumiAnalyst imager and software (Roche Applied Sciences). .. Binding of GST-Pax6-HD and mutants to the 32 P-labeled HDp3 probe (5′-GATCCTCTAGATAATGCGATTAGCGTAG-3′) was performed as described previously , with the exception that 100 mM NaCl was used instead of 30 mM KCl.

    Article Title: Enhanced-Transient Expression of Hepatitis C Virus Core Protein in Nicotiana tabacum, a Protein With Potential Clinical Applications
    Article Snippet: .. For SDS-PAGE and western blotting analyses, purified HCV core from E. coli and plant and plant crude extracts of the recombinant HCV core protein expressed by P19 co-agroinfiltrated pBI121 and PVX vectors were loaded onto a 12% SDS-polyacrylamide gel; by the end of electrophoresis, the protein bands were either stained with coomassie brilliant blue (Bio-Rad) or transferred to the PVDF membrane. .. Subsequently, the corresponding protein bands on the membrane were identified by biotinylated anti-core polyclonal antibody (Abcam, UK) (1:1000 dilution) and streptavidin HRP conjugate (Sigma, USA) (1:4000 dilution), respectively, and were detected by TMB as substrate.

    Modification:

    Article Title: Characterization of the Protocatechuic Acid Catabolic Gene Cluster from Streptomyces sp. Strain 2065
    Article Snippet: .. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed on a Bio-Rad (Mississauga, Ontario, Canada) Miniprotein II apparatus with 13% polyacrylamide gels using the modified procedure of Laemmli ( ). ..

    Western Blot:

    Article Title: Enhanced-Transient Expression of Hepatitis C Virus Core Protein in Nicotiana tabacum, a Protein With Potential Clinical Applications
    Article Snippet: .. For SDS-PAGE and western blotting analyses, purified HCV core from E. coli and plant and plant crude extracts of the recombinant HCV core protein expressed by P19 co-agroinfiltrated pBI121 and PVX vectors were loaded onto a 12% SDS-polyacrylamide gel; by the end of electrophoresis, the protein bands were either stained with coomassie brilliant blue (Bio-Rad) or transferred to the PVDF membrane. .. Subsequently, the corresponding protein bands on the membrane were identified by biotinylated anti-core polyclonal antibody (Abcam, UK) (1:1000 dilution) and streptavidin HRP conjugate (Sigma, USA) (1:4000 dilution), respectively, and were detected by TMB as substrate.

    Recombinant:

    Article Title: Enhanced-Transient Expression of Hepatitis C Virus Core Protein in Nicotiana tabacum, a Protein With Potential Clinical Applications
    Article Snippet: .. For SDS-PAGE and western blotting analyses, purified HCV core from E. coli and plant and plant crude extracts of the recombinant HCV core protein expressed by P19 co-agroinfiltrated pBI121 and PVX vectors were loaded onto a 12% SDS-polyacrylamide gel; by the end of electrophoresis, the protein bands were either stained with coomassie brilliant blue (Bio-Rad) or transferred to the PVDF membrane. .. Subsequently, the corresponding protein bands on the membrane were identified by biotinylated anti-core polyclonal antibody (Abcam, UK) (1:1000 dilution) and streptavidin HRP conjugate (Sigma, USA) (1:4000 dilution), respectively, and were detected by TMB as substrate.

    SDS Page:

    Article Title: Interaction of local anesthetics with the K+ channel pore domain
    Article Snippet: .. Ten milliliters of each sample was pipetted into wells of precast 12% acrylamide TRIS-HCl ready SDS-PAGE Gels (Bio-Rad) and subjected to electrophoresis at 200V for ~35 min in running buffer (25 mM Tris base, 192 mM glycine, pH 8.3, 0.1% SDS). .. The gel was rinsed in deionized H2 O for 7 min and stained with GelCode Blue Stain Reagent for 1 h, rinsed for 1 h and destained overnight in deionized H2 O.

    Article Title: Native Outer Membrane Proteins Protect Mice against Pulmonary Challenge with Virulent Type A Francisella tularensis
    Article Snippet: .. Equal amounts of LPS, iLVS, and OMP preparations were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and either visualized by silver staining (Silver Stain Plus; Bio-Rad) or transferred to nitrocellulose for immunoblot analysis as previously described ( ). .. For comparison of the antigen preparations by immunoblotting, the relative amount of LPS in each antigen preparation was visualized using mouse monoclonal antibody FB11 to F. tularensis LPS (Abcam, Cambridge, MA).

    Article Title: Enhanced-Transient Expression of Hepatitis C Virus Core Protein in Nicotiana tabacum, a Protein With Potential Clinical Applications
    Article Snippet: .. For SDS-PAGE and western blotting analyses, purified HCV core from E. coli and plant and plant crude extracts of the recombinant HCV core protein expressed by P19 co-agroinfiltrated pBI121 and PVX vectors were loaded onto a 12% SDS-polyacrylamide gel; by the end of electrophoresis, the protein bands were either stained with coomassie brilliant blue (Bio-Rad) or transferred to the PVDF membrane. .. Subsequently, the corresponding protein bands on the membrane were identified by biotinylated anti-core polyclonal antibody (Abcam, UK) (1:1000 dilution) and streptavidin HRP conjugate (Sigma, USA) (1:4000 dilution), respectively, and were detected by TMB as substrate.

    Article Title: Characterization of the Protocatechuic Acid Catabolic Gene Cluster from Streptomyces sp. Strain 2065
    Article Snippet: .. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed on a Bio-Rad (Mississauga, Ontario, Canada) Miniprotein II apparatus with 13% polyacrylamide gels using the modified procedure of Laemmli ( ). ..

    Article Title: Microaerophilic Induction of the Alpha-Crystallin Chaperone Protein Homologue (hspX) mRNA of Mycobacterium tuberculosis
    Article Snippet: .. Twenty micrograms of protein for each sample was separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) using a Tris-tricine 16.5% polyacrylamide gel (Bio-Rad). .. The gel was stained and the protein was transferred to a nitrocellulose paper (Schleicher & Schuell, Keene, N.H.) for Western blotting.

    Software:

    Article Title: The third helix of the homeodomain of paired class homeodomain proteins acts as a recognition helix both for DNA and protein interactions
    Article Snippet: .. The GST fusion proteins were analyzed on a 10% SDS–polyacrylamide gel and quantified using SYPRO® Ruby protein stain (Bio-Rad) and LumiAnalyst imager and software (Roche Applied Sciences). .. Binding of GST-Pax6-HD and mutants to the 32 P-labeled HDp3 probe (5′-GATCCTCTAGATAATGCGATTAGCGTAG-3′) was performed as described previously , with the exception that 100 mM NaCl was used instead of 30 mM KCl.

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    Bio-Rad criterion precast tris tricine
    (a) Representative pictures from <t>Tris-Tricine-sodium</t> dodecyl sulfate-polyacrylamide gel electrophoresis of peptides after proteolysis. The proteases used were human neutrophil elastase (HNE), Pseudomonas aeruginosa elastase (PE), aureolysin (Aur), and
    Criterion Precast Tris Tricine, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Bio-Rad criterion tris hcl precast sds page gels
    Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by <t>SDS-PAGE</t> followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.
    Criterion Tris Hcl Precast Sds Page Gels, 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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    99
    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: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad criterion tgx precast sds page gels
    Binding specificity for EGFRvIII antigen . (A) Scheme of the extracellular domains (ECD) of EGFR, EGFRvIII, and a further truncated EGFRvIII variant EGFRvIII trunc (recombinant, not naturally occurring). (B) Binding of different EGFRvIII- or EGFR-targeting antibodies or antibody fragments to recombinant Fc-fusions of these ECD variants after non-reducing <t>SDS-PAGE</t> and Western Blot. EGFRvIII ECD due to the 267 amino acid deletion has an ~25 kDa smaller molecular size than EGFR ECD , resulting in an ~50 kDa size difference in the dimeric form of the Fc-fusion proteins under non-reducing conditions. (C) Binding of the anti-EGFRvIII A3 diabody to immobilized EGFRvIII antigen is efficiently outcompeted with increasing concentrations of EGFRvIII-specific peptide PEPvIII (aa-sequence: LEEKKGNYVVTDH). (D) Normalized ELISA signals for binding of anti-EGFRvIII A3 diabody to EGFRvIII N-terminal epitope spanning 15-mer peptides containing single amino acid substitutions in each position of the native sequence. Filled circles indicate strong binding to the native sequence or correspondingly substituted sequences, open circles indicate positions in which substitutions completely disrupted binding.
    Criterion Tgx Precast Sds Page Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (a) Representative pictures from Tris-Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis of peptides after proteolysis. The proteases used were human neutrophil elastase (HNE), Pseudomonas aeruginosa elastase (PE), aureolysin (Aur), and

    Journal:

    Article Title: Evaluation of Strategies for Improving Proteolytic Resistance of Antimicrobial Peptides by Using Variants of EFK17, an Internal Segment of LL-37 ▿Evaluation of Strategies for Improving Proteolytic Resistance of Antimicrobial Peptides by Using Variants of EFK17, an Internal Segment of LL-37 ▿ †

    doi: 10.1128/AAC.00477-08

    Figure Lengend Snippet: (a) Representative pictures from Tris-Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis of peptides after proteolysis. The proteases used were human neutrophil elastase (HNE), Pseudomonas aeruginosa elastase (PE), aureolysin (Aur), and

    Article Snippet: Gel electrophoresis was done using Criterion precast Tris-Tricine 16.5% polyacrylamide gels and Tris-Tricine-sodium dodecyl sulfate running buffer from Bio-Rad (Hercules, CA) at 150 V for 35 min, submerged in ice.

    Techniques: Polyacrylamide Gel Electrophoresis

    Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by SDS-PAGE followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.

    Journal: Nucleic Acids Research

    Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation

    doi: 10.1093/nar/gku1132

    Figure Lengend Snippet: Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by SDS-PAGE followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.

    Article Snippet: All isolated fractions were separated in 4–15% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad) and tested by a standard western blotting procedure.

    Techniques: Fluorescence, Confocal Microscopy, Expressing, Marker, Fractionation, SDS Page, Western Blot

    Steady-state levels and activities of the OXPHOS complexes. (A) Western blot analysis of the Lrpprc2 RNAi#1 line (left side) and the Lrpprc2 RNAi#2 line (right side) performed on 20–40 μg whole-body protein extracts from controls and DmLrpprc2 KD third-instar larvae and 6-day-old adults. Protein extracts were separated by standard SDS-PAGE followed by western blot analysis with antibodies against the nuclear-encoded subunit NDUFS3 of complex I, the α-subunit of complex V and VDAC, the latter used as reference for loading. (B) BN-PAGE combined with complex I, complex IV and complex V in-gel activity analyses on the Lrpprc2 RNAi#1 line and the Lrpprc2 RNAi#2 line. BN-PAGE was performed on 75 μg for complex I, 100 μg for complex IV and 150 μg for complex V of mitochondrial protein extracts from control and DmLrpprc2 KD third-instar larvae. The assembly status of complex V (right panel) is black because of color inversion. Loading controls are provided by Coomassie staining to assess the total mitochondrial protein content per sample (only for complex V, left panel) and western blot analysis of VDAC protein levels in mitochondrial protein lysates collected prior to BN-PAGE gel loading. The position of complex I (CI), complex IV (CIV), complex V dimers (CV 2 ), complex V monomers (CV 1 ) and complex V subassembled components ( sub CV a and sub CV b ) are indicated by arrows.

    Journal: Nucleic Acids Research

    Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation

    doi: 10.1093/nar/gku1132

    Figure Lengend Snippet: Steady-state levels and activities of the OXPHOS complexes. (A) Western blot analysis of the Lrpprc2 RNAi#1 line (left side) and the Lrpprc2 RNAi#2 line (right side) performed on 20–40 μg whole-body protein extracts from controls and DmLrpprc2 KD third-instar larvae and 6-day-old adults. Protein extracts were separated by standard SDS-PAGE followed by western blot analysis with antibodies against the nuclear-encoded subunit NDUFS3 of complex I, the α-subunit of complex V and VDAC, the latter used as reference for loading. (B) BN-PAGE combined with complex I, complex IV and complex V in-gel activity analyses on the Lrpprc2 RNAi#1 line and the Lrpprc2 RNAi#2 line. BN-PAGE was performed on 75 μg for complex I, 100 μg for complex IV and 150 μg for complex V of mitochondrial protein extracts from control and DmLrpprc2 KD third-instar larvae. The assembly status of complex V (right panel) is black because of color inversion. Loading controls are provided by Coomassie staining to assess the total mitochondrial protein content per sample (only for complex V, left panel) and western blot analysis of VDAC protein levels in mitochondrial protein lysates collected prior to BN-PAGE gel loading. The position of complex I (CI), complex IV (CIV), complex V dimers (CV 2 ), complex V monomers (CV 1 ) and complex V subassembled components ( sub CV a and sub CV b ) are indicated by arrows.

    Article Snippet: All isolated fractions were separated in 4–15% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad) and tested by a standard western blotting procedure.

    Techniques: Western Blot, SDS Page, Polyacrylamide Gel Electrophoresis, Activity Assay, Staining

    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

    Binding specificity for EGFRvIII antigen . (A) Scheme of the extracellular domains (ECD) of EGFR, EGFRvIII, and a further truncated EGFRvIII variant EGFRvIII trunc (recombinant, not naturally occurring). (B) Binding of different EGFRvIII- or EGFR-targeting antibodies or antibody fragments to recombinant Fc-fusions of these ECD variants after non-reducing SDS-PAGE and Western Blot. EGFRvIII ECD due to the 267 amino acid deletion has an ~25 kDa smaller molecular size than EGFR ECD , resulting in an ~50 kDa size difference in the dimeric form of the Fc-fusion proteins under non-reducing conditions. (C) Binding of the anti-EGFRvIII A3 diabody to immobilized EGFRvIII antigen is efficiently outcompeted with increasing concentrations of EGFRvIII-specific peptide PEPvIII (aa-sequence: LEEKKGNYVVTDH). (D) Normalized ELISA signals for binding of anti-EGFRvIII A3 diabody to EGFRvIII N-terminal epitope spanning 15-mer peptides containing single amino acid substitutions in each position of the native sequence. Filled circles indicate strong binding to the native sequence or correspondingly substituted sequences, open circles indicate positions in which substitutions completely disrupted binding.

    Journal: Frontiers in Oncology

    Article Title: Highly Specific and Effective Targeting of EGFRvIII-Positive Tumors with TandAb Antibodies

    doi: 10.3389/fonc.2017.00100

    Figure Lengend Snippet: Binding specificity for EGFRvIII antigen . (A) Scheme of the extracellular domains (ECD) of EGFR, EGFRvIII, and a further truncated EGFRvIII variant EGFRvIII trunc (recombinant, not naturally occurring). (B) Binding of different EGFRvIII- or EGFR-targeting antibodies or antibody fragments to recombinant Fc-fusions of these ECD variants after non-reducing SDS-PAGE and Western Blot. EGFRvIII ECD due to the 267 amino acid deletion has an ~25 kDa smaller molecular size than EGFR ECD , resulting in an ~50 kDa size difference in the dimeric form of the Fc-fusion proteins under non-reducing conditions. (C) Binding of the anti-EGFRvIII A3 diabody to immobilized EGFRvIII antigen is efficiently outcompeted with increasing concentrations of EGFRvIII-specific peptide PEPvIII (aa-sequence: LEEKKGNYVVTDH). (D) Normalized ELISA signals for binding of anti-EGFRvIII A3 diabody to EGFRvIII N-terminal epitope spanning 15-mer peptides containing single amino acid substitutions in each position of the native sequence. Filled circles indicate strong binding to the native sequence or correspondingly substituted sequences, open circles indicate positions in which substitutions completely disrupted binding.

    Article Snippet: Samples with DTT were heated at 95°C for 5 min prior to loading on 4–20% Criterion TGX Precast SDS-PAGE Gels (Bio-Rad).

    Techniques: Binding Assay, Variant Assay, Recombinant, SDS Page, Western Blot, Sequencing, Enzyme-linked Immunosorbent Assay