tris glycine gel  (Thermo Fisher)


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    Name:
    Novex 12 Tris Glycine Plus Midi Gels
    Description:
    Novex Tris Glycine Plus Midi Protein gels are improved polyacrylamide gels based on traditional Laemmli protein electrophoresis technology allowing the use of Laemmli sample and running buffers The gels offer reproducible separation of a wide range of proteins into well resolved bands Novex Tris Glycine Plus Midi gels are a 1 0 mm thick wider format 8 cm x 13 cm gel for higher throughput electrophoresis of protein samples Features of Novex Tris Glycine Plus gels include Improved shelf life store gels for up to 12 months at 4°C Flexibility use for native and denaturing protein assays Fast run conditions quickly separate your proteins using constant voltage in less than 60 minutesLearn more about all of our Novex Tris Glcyine gels ›View migration charts › Choose the right gel format for your experiments Novex Tris Glycine Plus Midi gels come in fixed concentrations of 10 and 12 as well as gradient concentrations of 4 12 4 20 and 8 16 Select from our many well formats including 12 2 20 and 26 well Run your proteins in native or denatured form Novex Tris Glycine Plus gels do not contain SDS and so can be used to separate proteins in native or denatured form For denatured proteins we recommend using Novex Tris Glycine SDS Sample Buffer and Novex Tris Glycine SDS Running Buffer For native proteins we recommend using Novex Tris Glycine Native Sample Buffer and Novex Tris Glycine Native Running Buffer The gels can be run using our XCell4 SureLock Midi Cell or conveniently with the Bio Rad Criterion Cell using our adapters For transfer of proteins to a membrane we recommend using the Novex Tris Glycine Transfer Buffer Rapid semi dry transfer can be done using the Pierce Power Blotter or rapid dry transfer using the iBlot 2 Gel Transfer Device Alternatively traditional wet transfer can be performed using the Bio Rad Criterion Cell
    Catalog Number:
    wxp01212box
    Price:
    None
    Applications:
    1D Gel Electrophoresis|Protein Biology|Protein Gel Electrophoresis
    Category:
    Gels Fractionation Strips Membranes
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    Structured Review

    Thermo Fisher tris glycine gel
    RNAP containing βG1249D generates holoenzyme with AsiA/σD581BpA, but is defective in generating the crosslink with β’. ( A ) Native <t>Tris-glycine</t> gel. Solutions were assembled with the indicated components. The positions of AsiA, RNAP core, AsiA-RNAP holoenzyme, and σD581BpA are marked. (The bands that migrate faster than AsiA seen in lane 1 are trace contaminants present in the σD581BpA preparation.) ( B ) SDS-PAGE gel showing the products obtained after <t>photocrosslinking.</t> Arrow points to the crosslink between σD581BpA and β’ 80 HRGVICEK 87 identified in Figure 3 .
    Novex Tris Glycine Plus Midi Protein gels are improved polyacrylamide gels based on traditional Laemmli protein electrophoresis technology allowing the use of Laemmli sample and running buffers The gels offer reproducible separation of a wide range of proteins into well resolved bands Novex Tris Glycine Plus Midi gels are a 1 0 mm thick wider format 8 cm x 13 cm gel for higher throughput electrophoresis of protein samples Features of Novex Tris Glycine Plus gels include Improved shelf life store gels for up to 12 months at 4°C Flexibility use for native and denaturing protein assays Fast run conditions quickly separate your proteins using constant voltage in less than 60 minutesLearn more about all of our Novex Tris Glcyine gels ›View migration charts › Choose the right gel format for your experiments Novex Tris Glycine Plus Midi gels come in fixed concentrations of 10 and 12 as well as gradient concentrations of 4 12 4 20 and 8 16 Select from our many well formats including 12 2 20 and 26 well Run your proteins in native or denatured form Novex Tris Glycine Plus gels do not contain SDS and so can be used to separate proteins in native or denatured form For denatured proteins we recommend using Novex Tris Glycine SDS Sample Buffer and Novex Tris Glycine SDS Running Buffer For native proteins we recommend using Novex Tris Glycine Native Sample Buffer and Novex Tris Glycine Native Running Buffer The gels can be run using our XCell4 SureLock Midi Cell or conveniently with the Bio Rad Criterion Cell using our adapters For transfer of proteins to a membrane we recommend using the Novex Tris Glycine Transfer Buffer Rapid semi dry transfer can be done using the Pierce Power Blotter or rapid dry transfer using the iBlot 2 Gel Transfer Device Alternatively traditional wet transfer can be performed using the Bio Rad Criterion Cell
    https://www.bioz.com/result/tris glycine gel/product/Thermo Fisher
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    Images

    1) Product Images from "Visualizing the phage T4 activated transcription complex of DNA and E. coli RNA polymerase"

    Article Title: Visualizing the phage T4 activated transcription complex of DNA and E. coli RNA polymerase

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkw656

    RNAP containing βG1249D generates holoenzyme with AsiA/σD581BpA, but is defective in generating the crosslink with β’. ( A ) Native Tris-glycine gel. Solutions were assembled with the indicated components. The positions of AsiA, RNAP core, AsiA-RNAP holoenzyme, and σD581BpA are marked. (The bands that migrate faster than AsiA seen in lane 1 are trace contaminants present in the σD581BpA preparation.) ( B ) SDS-PAGE gel showing the products obtained after photocrosslinking. Arrow points to the crosslink between σD581BpA and β’ 80 HRGVICEK 87 identified in Figure 3 .
    Figure Legend Snippet: RNAP containing βG1249D generates holoenzyme with AsiA/σD581BpA, but is defective in generating the crosslink with β’. ( A ) Native Tris-glycine gel. Solutions were assembled with the indicated components. The positions of AsiA, RNAP core, AsiA-RNAP holoenzyme, and σD581BpA are marked. (The bands that migrate faster than AsiA seen in lane 1 are trace contaminants present in the σD581BpA preparation.) ( B ) SDS-PAGE gel showing the products obtained after photocrosslinking. Arrow points to the crosslink between σD581BpA and β’ 80 HRGVICEK 87 identified in Figure 3 .

    Techniques Used: SDS Page

    2) Product Images from "Identification of a Novel Hypocholesterolemic Protein, Major Royal Jelly Protein 1, Derived from Royal Jelly"

    Article Title: Identification of a Novel Hypocholesterolemic Protein, Major Royal Jelly Protein 1, Derived from Royal Jelly

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0105073

    Elution profile of RJ protein using cholic acid-conjugated EAH Sepharose 4B column chromatography and 10% SDS-PAGE patterns of bile acid-binding proteins derived from RJ. (A) Elution profile of RJ protein using cholic acid-conjugated EAH Sepharose 4B column chromatography. Twenty-five milliliters of RJ protein (10-kDa cut-off RJ) solution (118 mg protein) in 0.02% NaN 3 containing 10 mM Tris-HCl (pH 8.0) were applied to the column and washed with (a) 0.5 M NaCl containing 10 mM Tris-HCl buffer (pH 8.0), (b) 0.5% sodium deoxycholate containing 10 mM Tris-HCl buffer (pH 8.0), and (c) 8 M urea containing 10 mM Tris-HCl buffer (pH 8.0). (B) 10% SDS-PAGE patterns of bile acid-binding proteins derived from RJ by cholic acid-conjugated column chromatography. Lane 1, protein standard; lane 2, bile acid-binding proteins eluted with 0.5% sodium deoxycholate from the column. The amount of applied protein in lane 2 was 4.2 µg. The bile acid-binding proteins consist of MRJP1, MRJP2, and MRJP3.
    Figure Legend Snippet: Elution profile of RJ protein using cholic acid-conjugated EAH Sepharose 4B column chromatography and 10% SDS-PAGE patterns of bile acid-binding proteins derived from RJ. (A) Elution profile of RJ protein using cholic acid-conjugated EAH Sepharose 4B column chromatography. Twenty-five milliliters of RJ protein (10-kDa cut-off RJ) solution (118 mg protein) in 0.02% NaN 3 containing 10 mM Tris-HCl (pH 8.0) were applied to the column and washed with (a) 0.5 M NaCl containing 10 mM Tris-HCl buffer (pH 8.0), (b) 0.5% sodium deoxycholate containing 10 mM Tris-HCl buffer (pH 8.0), and (c) 8 M urea containing 10 mM Tris-HCl buffer (pH 8.0). (B) 10% SDS-PAGE patterns of bile acid-binding proteins derived from RJ by cholic acid-conjugated column chromatography. Lane 1, protein standard; lane 2, bile acid-binding proteins eluted with 0.5% sodium deoxycholate from the column. The amount of applied protein in lane 2 was 4.2 µg. The bile acid-binding proteins consist of MRJP1, MRJP2, and MRJP3.

    Techniques Used: Column Chromatography, SDS Page, Binding Assay, Derivative Assay

    Typical elution profiles of RJ proteins by HPLC and 15% SDS-PAGE patterns of the isolated RJ proteins. (A) Typical elution profile of RJ protein by HPLC. Elution profile of RJ protein (10-kDa cut-off RJ) by size-exclusion chromatography using a HiLoad 26/60 Superdex 200 p.g. column. Thirteen milliliters of 10-kDa cut-off RJ solution (182 mg protein) in 150 mM NaCl containing 20 mM phosphate (Na 2 HPO 4 /NaH 2 PO 4 ) buffer (pH 7.5) were applied to the column. The molecular weights of the eluted proteins were calibrated using standard proteins, as follows. Peak A, 515 kDa; peak B, 290 kDa; peak C, 157 kDa; peak D, 79 kDa; peak E, 55 kDa; peak F, 5 kDa. (B) 15% SDS-PAGE patterns of peak B and peak E. Lane 1, molecular weight standards; lane 2, protein containing peak B from Fig. 2(A) ; lane 3, protein containing peak E from Fig. 2(A) . The amount of applied protein in lanes 2 and 3 was 5 µg each. The protein contained in peak B from Fig. 2(A) was detected as a 55-kDa protein. The protein contained in peak E of Fig. 2(A) was detected as 2 major protein bands (55 kDa and 49 kDa)respectively. (C) Elution profile of peak E by anion exchange chromatography using a HiPrep QFF 16/10 column. Five millilters of peak E protein solution (125 mg protein) in 20 mM Tris-HCl (pH 8.0) was applied to the column. (D) 15% SDS-PAGE pattern of proteins derived from anion exchange chromatography. Lane 1, molecular weight standards; lane 2, protein containing the peak E1 and E2 of Fig. 2(C) . The amount of applied protein in lane 2 was 8 µg.
    Figure Legend Snippet: Typical elution profiles of RJ proteins by HPLC and 15% SDS-PAGE patterns of the isolated RJ proteins. (A) Typical elution profile of RJ protein by HPLC. Elution profile of RJ protein (10-kDa cut-off RJ) by size-exclusion chromatography using a HiLoad 26/60 Superdex 200 p.g. column. Thirteen milliliters of 10-kDa cut-off RJ solution (182 mg protein) in 150 mM NaCl containing 20 mM phosphate (Na 2 HPO 4 /NaH 2 PO 4 ) buffer (pH 7.5) were applied to the column. The molecular weights of the eluted proteins were calibrated using standard proteins, as follows. Peak A, 515 kDa; peak B, 290 kDa; peak C, 157 kDa; peak D, 79 kDa; peak E, 55 kDa; peak F, 5 kDa. (B) 15% SDS-PAGE patterns of peak B and peak E. Lane 1, molecular weight standards; lane 2, protein containing peak B from Fig. 2(A) ; lane 3, protein containing peak E from Fig. 2(A) . The amount of applied protein in lanes 2 and 3 was 5 µg each. The protein contained in peak B from Fig. 2(A) was detected as a 55-kDa protein. The protein contained in peak E of Fig. 2(A) was detected as 2 major protein bands (55 kDa and 49 kDa)respectively. (C) Elution profile of peak E by anion exchange chromatography using a HiPrep QFF 16/10 column. Five millilters of peak E protein solution (125 mg protein) in 20 mM Tris-HCl (pH 8.0) was applied to the column. (D) 15% SDS-PAGE pattern of proteins derived from anion exchange chromatography. Lane 1, molecular weight standards; lane 2, protein containing the peak E1 and E2 of Fig. 2(C) . The amount of applied protein in lane 2 was 8 µg.

    Techniques Used: High Performance Liquid Chromatography, SDS Page, Isolation, Size-exclusion Chromatography, Molecular Weight, Chromatography, Derivative Assay

    3) Product Images from "Expression and characterization of an epoxide hydrolase from Anopheles gambiae with high activity on epoxy fatty acids"

    Article Title: Expression and characterization of an epoxide hydrolase from Anopheles gambiae with high activity on epoxy fatty acids

    Journal: Insect biochemistry and molecular biology

    doi: 10.1016/j.ibmb.2014.08.004

    pH gradient and specific activity of Rotofor fractions. pH of fractions were measured, and 100 l of each fraction was diluted with 900 l 50 mM Tris-HCl, pH 8 buffer before activity was measured. Specific activity ( mol diols/ (min × mg protein)) was measured with t -DPPO as the substrate. The pI determined was 6.3.
    Figure Legend Snippet: pH gradient and specific activity of Rotofor fractions. pH of fractions were measured, and 100 l of each fraction was diluted with 900 l 50 mM Tris-HCl, pH 8 buffer before activity was measured. Specific activity ( mol diols/ (min × mg protein)) was measured with t -DPPO as the substrate. The pI determined was 6.3.

    Techniques Used: Activity Assay

    4) Product Images from "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains"

    Article Title: Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains

    Journal: The EMBO Journal

    doi: 10.1093/emboj/cdf691

    Fig. 4. Auto-ubiquitylation of BRCA1/BARD1 complex involves addition of multiple polyubiquitin chains. ( A ) BRCA1/BARD1-dependent ubiquitylation of H2A requires all the key reaction components. Reactions were carried out as described in Materials and methods, but omitting the indicated component from the reaction. The complete reaction is shown in lane a. Ubiquitylated BRCA1/BARD1 com plex (Ub-BRCA1/BARD1) and ubiquitylated H2A are indicated. ( B ) Ubiquitylation of the BRCA1/BARD1 complex in the presence of unmodified ubiquitin (lanes a–d) or methyl ubiquitin (lanes e–h). Reactions were carried out as outlined in Materials and methods using 0, 0.1, 0.3 or 1 µg (lanes a and e, b and f, c and g, and d and h) of ubiquitin or methyl ubiquitin as indicated. Reactions were performed for 60 min. Products were analysed by SDS–PAGE on a 4–20% Tris–glycine gel. Ubiquitylated H2A (Ub-H2A) and auto-ubiquitylated BRCA1/BARD1 products (Ub-BRCA1/BARD1) are indicated.
    Figure Legend Snippet: Fig. 4. Auto-ubiquitylation of BRCA1/BARD1 complex involves addition of multiple polyubiquitin chains. ( A ) BRCA1/BARD1-dependent ubiquitylation of H2A requires all the key reaction components. Reactions were carried out as described in Materials and methods, but omitting the indicated component from the reaction. The complete reaction is shown in lane a. Ubiquitylated BRCA1/BARD1 com plex (Ub-BRCA1/BARD1) and ubiquitylated H2A are indicated. ( B ) Ubiquitylation of the BRCA1/BARD1 complex in the presence of unmodified ubiquitin (lanes a–d) or methyl ubiquitin (lanes e–h). Reactions were carried out as outlined in Materials and methods using 0, 0.1, 0.3 or 1 µg (lanes a and e, b and f, c and g, and d and h) of ubiquitin or methyl ubiquitin as indicated. Reactions were performed for 60 min. Products were analysed by SDS–PAGE on a 4–20% Tris–glycine gel. Ubiquitylated H2A (Ub-H2A) and auto-ubiquitylated BRCA1/BARD1 products (Ub-BRCA1/BARD1) are indicated.

    Techniques Used: SDS Page

    Fig. 1. BRCA1/BARD1 has E3 monoubiquitin ligase activity in vitro . ( A ) A Coomassie-stained gel of the full-length BRCA1/BARD1 complex. His-tagged BRCA1 and BARD1 proteins were co-expressed and co-purified as a complex from Sf9 insect cells as described in Materials and methods. A 20 µl aliquot of the purified complex was analysed by SDS–PAGE using a 6% Tris–glycine gel and visualized by staining with Simply Blue Safe Stain (Invitrogen). Molecular weight markers (M) and the BRCA1 and BARD1 proteins are indicated. ( B ) BRCA1/BARD1 complex exhibits ubiquitin ligase activity in the presence of the E2 enzyme, UbcH5a. Ubiquitin E3 ligase activity was investigated by incubating histone H2A substrate with BRCA1/BARD1 complex in the presence of E1 enzyme and a variety of E2 enzymes (as indicated). Reactions were carried out with a 30–60 min pre-incubation step as described in Materials and methods. 125 I-Labelled products were analysed by SDS–PAGE and visualized using a PhosphorImager. [ 125 I]ubiquitin substrate and 125 I-ubiquitylated H2A products (Ub-H2A) are indicated.
    Figure Legend Snippet: Fig. 1. BRCA1/BARD1 has E3 monoubiquitin ligase activity in vitro . ( A ) A Coomassie-stained gel of the full-length BRCA1/BARD1 complex. His-tagged BRCA1 and BARD1 proteins were co-expressed and co-purified as a complex from Sf9 insect cells as described in Materials and methods. A 20 µl aliquot of the purified complex was analysed by SDS–PAGE using a 6% Tris–glycine gel and visualized by staining with Simply Blue Safe Stain (Invitrogen). Molecular weight markers (M) and the BRCA1 and BARD1 proteins are indicated. ( B ) BRCA1/BARD1 complex exhibits ubiquitin ligase activity in the presence of the E2 enzyme, UbcH5a. Ubiquitin E3 ligase activity was investigated by incubating histone H2A substrate with BRCA1/BARD1 complex in the presence of E1 enzyme and a variety of E2 enzymes (as indicated). Reactions were carried out with a 30–60 min pre-incubation step as described in Materials and methods. 125 I-Labelled products were analysed by SDS–PAGE and visualized using a PhosphorImager. [ 125 I]ubiquitin substrate and 125 I-ubiquitylated H2A products (Ub-H2A) are indicated.

    Techniques Used: Activity Assay, In Vitro, Staining, Purification, SDS Page, Molecular Weight, Incubation

    5) Product Images from "Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-?B activation in muramyl dipeptide recognition"

    Article Title: Membrane recruitment of NOD2 in intestinal epithelial cells is essential for nuclear factor-?B activation in muramyl dipeptide recognition

    Journal: The Journal of Cell Biology

    doi: 10.1083/jcb.200502153

    Expression and cellular localization of endogenous NOD2. (A) Western blot analysis using rabbit NOD2 antiserum HM2559 and anti–β-actin. 10 μg of total protein from different intestinal epithelial cells (IEC), COS7, and HEK293 cell lines were loaded onto 4–12% Tris-glycine gel. (B) NF-κB activation in HT29 and Caco-2 cells after stimulation with 1 μg/ml MDP-LD or MDP-LL using NF-κB luciferase reporter assay and normalization with renilla after 18 h of transfection. Error bars represent SEM of at least four separate experiments. *, P
    Figure Legend Snippet: Expression and cellular localization of endogenous NOD2. (A) Western blot analysis using rabbit NOD2 antiserum HM2559 and anti–β-actin. 10 μg of total protein from different intestinal epithelial cells (IEC), COS7, and HEK293 cell lines were loaded onto 4–12% Tris-glycine gel. (B) NF-κB activation in HT29 and Caco-2 cells after stimulation with 1 μg/ml MDP-LD or MDP-LL using NF-κB luciferase reporter assay and normalization with renilla after 18 h of transfection. Error bars represent SEM of at least four separate experiments. *, P

    Techniques Used: Expressing, Western Blot, Activation Assay, Luciferase, Reporter Assay, Transfection

    Membrane association of expressed NOD2. (A) Amino acid sequences of the COOH-terminal domain of NOD2 and the NOD2 3020insC mutant, which is associated with CD. (B) Confocal microscopy examination of Caco-2 cells that are transfected with Flag-NOD2, Flag-NOD2 3020insC mutant, and empty vector (pCMVtag2C) shows the membrane association of NOD2 (arrows) but not of the NOD2 mutant. NOD2 and 3020insC mutant were detected by using monoclonal anti-Flag antibody followed by fluorescein-conjugated anti–mouse IgG. (C) Western blot analysis using anti-Flag, anti–E-cadherin, or anti–lactate dehydrogenase antibodies. Caco-2 cells were transfected with Flag-NOD2 (WT) or Flag-NOD2 3020insC (mutant). Cytosolic (C) and membrane (M) fractions were separated as described in Materials and methods. Proteins were fractionated through 4–12% Tris-glycine SDS-PAGE and were subjected to Western blot analysis by using anti-Flag antibody to detect NOD2 expression. The ratio in the membrane and cytosolic fractions that were determined after the quantification of NOD2 3020insC mutant was compared with NOD2 wild type. The result is the mean of four separate experiments. Error bar represents SEM. *, P
    Figure Legend Snippet: Membrane association of expressed NOD2. (A) Amino acid sequences of the COOH-terminal domain of NOD2 and the NOD2 3020insC mutant, which is associated with CD. (B) Confocal microscopy examination of Caco-2 cells that are transfected with Flag-NOD2, Flag-NOD2 3020insC mutant, and empty vector (pCMVtag2C) shows the membrane association of NOD2 (arrows) but not of the NOD2 mutant. NOD2 and 3020insC mutant were detected by using monoclonal anti-Flag antibody followed by fluorescein-conjugated anti–mouse IgG. (C) Western blot analysis using anti-Flag, anti–E-cadherin, or anti–lactate dehydrogenase antibodies. Caco-2 cells were transfected with Flag-NOD2 (WT) or Flag-NOD2 3020insC (mutant). Cytosolic (C) and membrane (M) fractions were separated as described in Materials and methods. Proteins were fractionated through 4–12% Tris-glycine SDS-PAGE and were subjected to Western blot analysis by using anti-Flag antibody to detect NOD2 expression. The ratio in the membrane and cytosolic fractions that were determined after the quantification of NOD2 3020insC mutant was compared with NOD2 wild type. The result is the mean of four separate experiments. Error bar represents SEM. *, P

    Techniques Used: Mutagenesis, Confocal Microscopy, Transfection, Plasmid Preparation, Western Blot, SDS Page, Expressing

    6) Product Images from "A Defined Tuberculosis Vaccine Candidate Boosts BCG and Protects Against Multidrug Resistant Mycobacterium tuberculosis"

    Article Title: A Defined Tuberculosis Vaccine Candidate Boosts BCG and Protects Against Multidrug Resistant Mycobacterium tuberculosis

    Journal: Science translational medicine

    doi: 10.1126/scitranslmed.3001094

    ID93 protein construct and characterization. (A) Schematic of the ID93 fusion protein. (B – D) SDS-PAGE and immunoblot of three lots of ID93. (B) 2 μg per lane of ID93 (lanes 1 – 3) were run in reducing and non-reducing conditions on a 4 – 20 % Tris glycine gel. (C) Immunoblot of ID93 with mouse antibody to ID93 and rabbit anti-sera to E. coli (50 ng and 1 μg of ID93, respectively). (D) Immunoblot of ID93 with mouse antibody to Rv3619, Rv1813, Rv3620, and Rv2608 (50 ng of ID93). EC, E. coli protein standards; ID93, lanes 1 – 3; lane 4, Rv3619; lane 5, Rv1813; lane 6, Rv3620; lane 7, Rv2608.
    Figure Legend Snippet: ID93 protein construct and characterization. (A) Schematic of the ID93 fusion protein. (B – D) SDS-PAGE and immunoblot of three lots of ID93. (B) 2 μg per lane of ID93 (lanes 1 – 3) were run in reducing and non-reducing conditions on a 4 – 20 % Tris glycine gel. (C) Immunoblot of ID93 with mouse antibody to ID93 and rabbit anti-sera to E. coli (50 ng and 1 μg of ID93, respectively). (D) Immunoblot of ID93 with mouse antibody to Rv3619, Rv1813, Rv3620, and Rv2608 (50 ng of ID93). EC, E. coli protein standards; ID93, lanes 1 – 3; lane 4, Rv3619; lane 5, Rv1813; lane 6, Rv3620; lane 7, Rv2608.

    Techniques Used: Construct, SDS Page

    7) Product Images from "Oligomeric structure and chaperone-like activity of Drosophila melanogaster mitochondrial small heat shock protein Hsp22 and arginine mutants in the alpha-crystallin domain"

    Article Title: Oligomeric structure and chaperone-like activity of Drosophila melanogaster mitochondrial small heat shock protein Hsp22 and arginine mutants in the alpha-crystallin domain

    Journal: Cell Stress & Chaperones

    doi: 10.1007/s12192-017-0784-y

    Novex™ 4–12% Tris-glycine native gel analysis. a Twenty-five micrograms of DmHsp22WT and its arginine mutants after Bradford protein assay were loaded on 4–12% Tris-glycine native gel at 4 °C to compare the oligomeric profiles of proteins. b Native gel analysis of the human R140G-HspB1 versus HspB1WT. Twenty-five micrograms of each purified protein were loaded on 4–12% Tris-glycine native gel and separated either at 4 °C. Proteins were visualized by using Coomassie brilliant blue staining G250
    Figure Legend Snippet: Novex™ 4–12% Tris-glycine native gel analysis. a Twenty-five micrograms of DmHsp22WT and its arginine mutants after Bradford protein assay were loaded on 4–12% Tris-glycine native gel at 4 °C to compare the oligomeric profiles of proteins. b Native gel analysis of the human R140G-HspB1 versus HspB1WT. Twenty-five micrograms of each purified protein were loaded on 4–12% Tris-glycine native gel and separated either at 4 °C. Proteins were visualized by using Coomassie brilliant blue staining G250

    Techniques Used: Bradford Protein Assay, Purification, Staining

    8) Product Images from "Interaction of the Trans-Frame Potyvirus Protein P3N-PIPO with Host Protein PCaP1 Facilitates Potyvirus Movement"

    Article Title: Interaction of the Trans-Frame Potyvirus Protein P3N-PIPO with Host Protein PCaP1 Facilitates Potyvirus Movement

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.1002639

    Co-immunoprecipitation of P3N-PIPO and PCaP1 expressed in planta . Proteins from crude extracts of N. benthamiana leaves (2 days post agroinfiltration) that co-expressed HA-P3N-PIPO and c-myc-PCaP1, or expressed HA-P3N-PIPO or c-myc-PCaP1 only were pulled-down using anti-HA (top panels) or anti-c-myc (bottom panels) antibodies, separated by 4–12% Novex Tris-Glycine PAGE, electroblotted onto PVDF membrane and probed with anti-HA or anti-c-myc antibody as indicated. Recognition of HA-P3N-PIPO and c-myc-PCAP1 are shown at right. Immunoblotting (IB).
    Figure Legend Snippet: Co-immunoprecipitation of P3N-PIPO and PCaP1 expressed in planta . Proteins from crude extracts of N. benthamiana leaves (2 days post agroinfiltration) that co-expressed HA-P3N-PIPO and c-myc-PCaP1, or expressed HA-P3N-PIPO or c-myc-PCaP1 only were pulled-down using anti-HA (top panels) or anti-c-myc (bottom panels) antibodies, separated by 4–12% Novex Tris-Glycine PAGE, electroblotted onto PVDF membrane and probed with anti-HA or anti-c-myc antibody as indicated. Recognition of HA-P3N-PIPO and c-myc-PCAP1 are shown at right. Immunoblotting (IB).

    Techniques Used: Immunoprecipitation, Polyacrylamide Gel Electrophoresis

    Genome map of TuMV-GFP and expression of P3N-PIPO in planta . (A) Genome map of TuMV-GFP. Mature proteins processed from the proteolytic cleavage of the large polyprotein are indicated in boxes. pipo ORF is indicated above the polyprotein ORF with putative frameshift sequence indicated and bars showing codons in the polyprotein ORF (below) and pipo ORF (above). Sizes of P3N-PIPO and P3 proteins are indicated below the regions that code for them. P3-derived portion is shaded gray; PIPO-derived portion is in black. Position of inserted GFP coding insertion is indicated by dashed lines. Solid circle indicates VPg at 5′ end; (A)n indicates poly(A) tail. (B) Immunodetection of P3N-PIPO and P3 in TuMV-GFP-infected Arabidopsis . Total protein was extracted from the infected leaves at 14 days post inoculation (dpi), separated in either 4–12% NuPAGE Bis-Tris gel (Life Technologies) (for P3-N-PIPO and P3 detections) or in 4–12% Novex Tris-glycine gel (for GFP detection), blotted onto PVDF membrane and probed with anti-PIPO, anti-P3 or anti-GFP antibody and detected by ECL-plus Western reagents. Positions of protein mobility markers in kilodaltons (kDa) are indicated at right. Lanes indicate total protein from plants inoculated with wild-type (WT) TuMV-GFP, or pipo knockout mutants of TuMV-GFP (p41 and p68). These mutants differ from WT TuMV-GFP by single point mutations that introduce stop codons into the pipo ORF: CGA→ UGA and GGA → UGA at bases 3103 and 3130 in mutants p41 and p68, respectively ( pipo -frame codons shown). These mutations do not alter the amino acid sequence of the overlapping P3 region of the polyprotein. Note that putative P3N-PIPO migrates more slowly (∼28 kDa) than its predicted molecular weight (∼25 kDa).
    Figure Legend Snippet: Genome map of TuMV-GFP and expression of P3N-PIPO in planta . (A) Genome map of TuMV-GFP. Mature proteins processed from the proteolytic cleavage of the large polyprotein are indicated in boxes. pipo ORF is indicated above the polyprotein ORF with putative frameshift sequence indicated and bars showing codons in the polyprotein ORF (below) and pipo ORF (above). Sizes of P3N-PIPO and P3 proteins are indicated below the regions that code for them. P3-derived portion is shaded gray; PIPO-derived portion is in black. Position of inserted GFP coding insertion is indicated by dashed lines. Solid circle indicates VPg at 5′ end; (A)n indicates poly(A) tail. (B) Immunodetection of P3N-PIPO and P3 in TuMV-GFP-infected Arabidopsis . Total protein was extracted from the infected leaves at 14 days post inoculation (dpi), separated in either 4–12% NuPAGE Bis-Tris gel (Life Technologies) (for P3-N-PIPO and P3 detections) or in 4–12% Novex Tris-glycine gel (for GFP detection), blotted onto PVDF membrane and probed with anti-PIPO, anti-P3 or anti-GFP antibody and detected by ECL-plus Western reagents. Positions of protein mobility markers in kilodaltons (kDa) are indicated at right. Lanes indicate total protein from plants inoculated with wild-type (WT) TuMV-GFP, or pipo knockout mutants of TuMV-GFP (p41 and p68). These mutants differ from WT TuMV-GFP by single point mutations that introduce stop codons into the pipo ORF: CGA→ UGA and GGA → UGA at bases 3103 and 3130 in mutants p41 and p68, respectively ( pipo -frame codons shown). These mutations do not alter the amino acid sequence of the overlapping P3 region of the polyprotein. Note that putative P3N-PIPO migrates more slowly (∼28 kDa) than its predicted molecular weight (∼25 kDa).

    Techniques Used: Expressing, Sequencing, Derivative Assay, Immunodetection, Infection, Western Blot, Knock-Out, Introduce, Molecular Weight

    Immunodetection of PCaP1 in wild-type and PCaP1 knockout Arabidopsis plants. Total soluble proteins from leaves collected at 14 dpi were separated by 4–12% Novex Tris-glycine PAGE, blotted onto PVDF membrane, probed with anti-PCaP1 antibody or anti-GFP antibody and detected by ECL-Plus Western reagents. Samples were from mock inoculated or TuMV-GFP infected wild-type (WT) or PCaP1 knockout ( pcap1 ) plants. Equal loading of proteins was verified by similar levels of Coomassie staining of Rubisco protein (bottom panel).
    Figure Legend Snippet: Immunodetection of PCaP1 in wild-type and PCaP1 knockout Arabidopsis plants. Total soluble proteins from leaves collected at 14 dpi were separated by 4–12% Novex Tris-glycine PAGE, blotted onto PVDF membrane, probed with anti-PCaP1 antibody or anti-GFP antibody and detected by ECL-Plus Western reagents. Samples were from mock inoculated or TuMV-GFP infected wild-type (WT) or PCaP1 knockout ( pcap1 ) plants. Equal loading of proteins was verified by similar levels of Coomassie staining of Rubisco protein (bottom panel).

    Techniques Used: Immunodetection, Knock-Out, Polyacrylamide Gel Electrophoresis, Western Blot, Infection, Staining

    9) Product Images from "Mass spectrometric analysis reveals O-methylation of pyruvate kinase from pancreatic cancer cells"

    Article Title: Mass spectrometric analysis reveals O-methylation of pyruvate kinase from pancreatic cancer cells

    Journal: Analytical and bioanalytical chemistry

    doi: 10.1007/s00216-013-6880-7

    SDS-PAGE of cell lysates from CFPAC-1 and normal duct cells. A total of 50 μg proteins from each sample was dispensed into the wells of the Novex 4–20 % Tris-Glycine Gel to separate the proteins by SDS-PAGE. Protein bands corresponding
    Figure Legend Snippet: SDS-PAGE of cell lysates from CFPAC-1 and normal duct cells. A total of 50 μg proteins from each sample was dispensed into the wells of the Novex 4–20 % Tris-Glycine Gel to separate the proteins by SDS-PAGE. Protein bands corresponding

    Techniques Used: SDS Page

    10) Product Images from "Human T-lymphotropic Virus Type 1-infected Cells Secrete Exosomes That Contain Tax Protein *"

    Article Title: Human T-lymphotropic Virus Type 1-infected Cells Secrete Exosomes That Contain Tax Protein *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M114.549659

    Characterization of unfiltered exosomes derived from HTLV-infected cells. A , exosome fractions were collected from cell culture supernatants 1, 2, and 5 days post-seeding in exosome-free medium. Equivalent amounts of exosomes isolated from uninfected CEM and HTLV-1-positive C81, MT2, and ED(−) cells were resolved on 4–20% Tris/glycine gels and analyzed by Coomassie Blue staining. B , CEM, C81, MT2, and ED(−)-derived exosomes (10 μg) and corresponding WCE collected 5 days postseeding were analyzed via Western blot using antibodies against HSP70, Alix, CD63, cytochrome c , and β-actin. C , transmission electron microscopy image analysis of CEM-, C81-, and MT2-derived exosomes are shown at ×75,000 magnification.
    Figure Legend Snippet: Characterization of unfiltered exosomes derived from HTLV-infected cells. A , exosome fractions were collected from cell culture supernatants 1, 2, and 5 days post-seeding in exosome-free medium. Equivalent amounts of exosomes isolated from uninfected CEM and HTLV-1-positive C81, MT2, and ED(−) cells were resolved on 4–20% Tris/glycine gels and analyzed by Coomassie Blue staining. B , CEM, C81, MT2, and ED(−)-derived exosomes (10 μg) and corresponding WCE collected 5 days postseeding were analyzed via Western blot using antibodies against HSP70, Alix, CD63, cytochrome c , and β-actin. C , transmission electron microscopy image analysis of CEM-, C81-, and MT2-derived exosomes are shown at ×75,000 magnification.

    Techniques Used: Derivative Assay, Infection, Cell Culture, Isolation, Staining, Western Blot, Transmission Assay, Electron Microscopy

    Exosomes derived from HTLV-1-infected cells contain viral mRNA transcripts. A , total RNA was isolated from exosomes derived from CEM, C81, MT2, and ED(−) cells and subjected to quantitative RT-PCR in triplicate using primers specific for HTLV-1 Tax, HBZ, 5′-LTR, and Env. Results presented are mean ± S.D. ( error bars ) after normalization to β-globin. B , both cell culture supernatants and exosomes (undiluted and 10 −1 ) derived from CEM, C81, MT2, and ED(−) cells were analyzed for RT activity. C , 293T cells (1 × 10 6 cells) were seeded for 12 h, exposed to CEM- or C81-derived exosomes (10 μg) for 2 h, and then labeled with 35 S label for 4 h. After lysis, cellular extracts were subjected to co-immunoprecipitation using IgG, α-Tax, α-HBZ, or α-Env antibody (3 μg each) overnight at 4 ºC. The next day, Protein A + G was added, and samples were washed with radioimmune precipitation assay buffer and then TNE50 + 0.1% Nonidet P-40. Washed immunoprecipitated complexes were resolved on 4–20% Tris/glycine gels, dried, and imaged using a PhosphorImager. D , raw densitometry counts of images from the PhosphorImager were obtained using ImageJ, and results were normalized to IgG counts before plotting.
    Figure Legend Snippet: Exosomes derived from HTLV-1-infected cells contain viral mRNA transcripts. A , total RNA was isolated from exosomes derived from CEM, C81, MT2, and ED(−) cells and subjected to quantitative RT-PCR in triplicate using primers specific for HTLV-1 Tax, HBZ, 5′-LTR, and Env. Results presented are mean ± S.D. ( error bars ) after normalization to β-globin. B , both cell culture supernatants and exosomes (undiluted and 10 −1 ) derived from CEM, C81, MT2, and ED(−) cells were analyzed for RT activity. C , 293T cells (1 × 10 6 cells) were seeded for 12 h, exposed to CEM- or C81-derived exosomes (10 μg) for 2 h, and then labeled with 35 S label for 4 h. After lysis, cellular extracts were subjected to co-immunoprecipitation using IgG, α-Tax, α-HBZ, or α-Env antibody (3 μg each) overnight at 4 ºC. The next day, Protein A + G was added, and samples were washed with radioimmune precipitation assay buffer and then TNE50 + 0.1% Nonidet P-40. Washed immunoprecipitated complexes were resolved on 4–20% Tris/glycine gels, dried, and imaged using a PhosphorImager. D , raw densitometry counts of images from the PhosphorImager were obtained using ImageJ, and results were normalized to IgG counts before plotting.

    Techniques Used: Derivative Assay, Infection, Isolation, Quantitative RT-PCR, Cell Culture, Activity Assay, Labeling, Lysis, Immunoprecipitation

    Specific enrichment of exosomes. A , aliquots of 50 ml (5-day-old cultures) of CEM, C81, MT2, and ED(−) cell culture supernatants were clarified by filtration (0.22 μm), whereas 50 ml of each supernatant were left unfiltered. Exosomes (1 μg) isolated from both filtered and unfiltered supernatants were resolved on 4–20% Tris/glycine gels and analyzed by silver staining. B , C81 exosomes from both filtered (9 μg) and unfiltered (7 μg) supernatants and corresponding WCE (10 μg) were evaluated for the incorporation of common exosome markers by Western blot using HSP70, CD63, cytochrome c , and actin antibodies. C , cells were treated with brefeldin A or manumycin A, and the resulting supernatant was collected after 48 h for exosomal preparation ( lanes 1 and 2 ), or exosomes obtained from C81 cells were trypsin-treated or freeze/thawed ( F/T ) and then trypsin-treated ( lanes 3 and 4 ). Lanes 5 and 6 , input exosome controls from C81 or CEM cells, respectively. Resulting exosomes were assayed for the presence of Tax by Western blotting. D , exosomes from MT2 cells were enriched by trapping with nanotrap particles NT080 ( lane 3 ) or NT086 ( lane 4 ) to enrich for virions. Lanes 1 and 2 , are exosomal controls from CEM or MT2 cells, respectively. The trapped exosomes were assayed for the presence of Tax by Western blotting.
    Figure Legend Snippet: Specific enrichment of exosomes. A , aliquots of 50 ml (5-day-old cultures) of CEM, C81, MT2, and ED(−) cell culture supernatants were clarified by filtration (0.22 μm), whereas 50 ml of each supernatant were left unfiltered. Exosomes (1 μg) isolated from both filtered and unfiltered supernatants were resolved on 4–20% Tris/glycine gels and analyzed by silver staining. B , C81 exosomes from both filtered (9 μg) and unfiltered (7 μg) supernatants and corresponding WCE (10 μg) were evaluated for the incorporation of common exosome markers by Western blot using HSP70, CD63, cytochrome c , and actin antibodies. C , cells were treated with brefeldin A or manumycin A, and the resulting supernatant was collected after 48 h for exosomal preparation ( lanes 1 and 2 ), or exosomes obtained from C81 cells were trypsin-treated or freeze/thawed ( F/T ) and then trypsin-treated ( lanes 3 and 4 ). Lanes 5 and 6 , input exosome controls from C81 or CEM cells, respectively. Resulting exosomes were assayed for the presence of Tax by Western blotting. D , exosomes from MT2 cells were enriched by trapping with nanotrap particles NT080 ( lane 3 ) or NT086 ( lane 4 ) to enrich for virions. Lanes 1 and 2 , are exosomal controls from CEM or MT2 cells, respectively. The trapped exosomes were assayed for the presence of Tax by Western blotting.

    Techniques Used: Cell Culture, Filtration, Isolation, Silver Staining, Western Blot

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    SDS Page:

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    Polyacrylamide Gel Electrophoresis:

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    Thermo Fisher bis tris glycine gel
    Analysis of MSNP protein coronas by <t>SDS-PAGE.</t> Notes: MSNPs of different sizes were incubated with cell-culture medium with 5% or 10% serum at 37°C for 24 hours. After centrifugation to remove unbound serum proteins, pellets were washed three times and then resuspended in 30 µL water and analyzed by SDS-PAGE on a 12% <t>bis-Tris-glycine</t> gel (Thermo Fisher Scientific), followed by EZ blue staining. Representative gels are shown. ( A ) Protein coronas of MSNPs after incubation in cell-culture medium with 5% serum. Lane 1, aliquot of medium; lane 2, protein coronas of 30 nm MSNPs; lane 3, protein coronas of 250 nm MSNPs; lane 4, medium alone submitted to centrifugation as negative control; lane 5, molecular weight marker. ( B ) Protein coronas of MSNPs after incubation in cell-culture medium with 10% serum. Lane 1, medium alone submitted to centrifugation as negative control; lane 2, protein coronas of 30 nm MSNPs; lane 3, protein coronas of 250 nm MSNPs; lane 4, an aliquot of medium; lane 5, molecular weight marker. Abbreviations: MSNP, mesoporous silica nanoparticle; SDS-PAGE, sodium dodecyl sulfate polyacrylamide-gel electrophoresis.
    Bis Tris Glycine Gel, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher tris glycine sds page
    Electrophoretic analysis of U 1 -SCRTX-Lg1a. Silver-stained 12% <t>SDS-PAGE</t> gel of the crude venom of L. gaucho (CV) (5 µg) and purified antimicrobial U 1 -SCRTX-Lg1a (2.5 µg) under non-reducing conditions. On the left are numbers that correspond to the positions of molecular weight markers (MW) expressed in kDa.
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    Thermo Fisher sds page sds polyacrylamide gels
    Stability test on released toxoid. <t>SDS-PAGE</t> analysis of protein released from the various MSNPs after ( A ) 0 months ( B ) 3 months ( C ) 6 months. The samples were kept under the following conditions A1: In suspension, kept at 4 °C, A2: In suspension, kept at RT, A3: Lyophilised, kept at 4 °C, A4: Lyophilised, kept at RT. Lanes are loaded as follows: (M) Marker, (−ve) Negative control, (+ve) Positive control, (1) LP2@A1, (2) LP3@A1, (3) SBA-15@A1, (4) LP2@A2, (5) LP3@A2, (6) SBA-15@A2, (7) LP2@A3, (8) LP3@A3, (9) SBA-15@A3, (10) LP2@A4, (11) LP3@A4, (12) SBA-15@A4.
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    Analysis of MSNP protein coronas by SDS-PAGE. Notes: MSNPs of different sizes were incubated with cell-culture medium with 5% or 10% serum at 37°C for 24 hours. After centrifugation to remove unbound serum proteins, pellets were washed three times and then resuspended in 30 µL water and analyzed by SDS-PAGE on a 12% bis-Tris-glycine gel (Thermo Fisher Scientific), followed by EZ blue staining. Representative gels are shown. ( A ) Protein coronas of MSNPs after incubation in cell-culture medium with 5% serum. Lane 1, aliquot of medium; lane 2, protein coronas of 30 nm MSNPs; lane 3, protein coronas of 250 nm MSNPs; lane 4, medium alone submitted to centrifugation as negative control; lane 5, molecular weight marker. ( B ) Protein coronas of MSNPs after incubation in cell-culture medium with 10% serum. Lane 1, medium alone submitted to centrifugation as negative control; lane 2, protein coronas of 30 nm MSNPs; lane 3, protein coronas of 250 nm MSNPs; lane 4, an aliquot of medium; lane 5, molecular weight marker. Abbreviations: MSNP, mesoporous silica nanoparticle; SDS-PAGE, sodium dodecyl sulfate polyacrylamide-gel electrophoresis.

    Journal: International Journal of Nanomedicine

    Article Title: Mesoporous silica nanoparticles trigger mitophagy in endothelial cells and perturb neuronal network activity in a size- and time-dependent manner

    doi: 10.2147/IJN.S127663

    Figure Lengend Snippet: Analysis of MSNP protein coronas by SDS-PAGE. Notes: MSNPs of different sizes were incubated with cell-culture medium with 5% or 10% serum at 37°C for 24 hours. After centrifugation to remove unbound serum proteins, pellets were washed three times and then resuspended in 30 µL water and analyzed by SDS-PAGE on a 12% bis-Tris-glycine gel (Thermo Fisher Scientific), followed by EZ blue staining. Representative gels are shown. ( A ) Protein coronas of MSNPs after incubation in cell-culture medium with 5% serum. Lane 1, aliquot of medium; lane 2, protein coronas of 30 nm MSNPs; lane 3, protein coronas of 250 nm MSNPs; lane 4, medium alone submitted to centrifugation as negative control; lane 5, molecular weight marker. ( B ) Protein coronas of MSNPs after incubation in cell-culture medium with 10% serum. Lane 1, medium alone submitted to centrifugation as negative control; lane 2, protein coronas of 30 nm MSNPs; lane 3, protein coronas of 250 nm MSNPs; lane 4, an aliquot of medium; lane 5, molecular weight marker. Abbreviations: MSNP, mesoporous silica nanoparticle; SDS-PAGE, sodium dodecyl sulfate polyacrylamide-gel electrophoresis.

    Article Snippet: After the last step of washing, pellets were resuspended in 30 µL of water and analyzed by SDS-PAGE on a 12% bis-Tris-glycine gel (Thermo Fisher Scientific), followed by EZ blue staining.

    Techniques: SDS Page, Incubation, Cell Culture, Centrifugation, Staining, Negative Control, Molecular Weight, Marker, Polyacrylamide Gel Electrophoresis

    Electrophoretic analysis of U 1 -SCRTX-Lg1a. Silver-stained 12% SDS-PAGE gel of the crude venom of L. gaucho (CV) (5 µg) and purified antimicrobial U 1 -SCRTX-Lg1a (2.5 µg) under non-reducing conditions. On the left are numbers that correspond to the positions of molecular weight markers (MW) expressed in kDa.

    Journal: Toxins

    Article Title: Loxosceles gaucho Spider Venom: An Untapped Source of Antimicrobial Agents

    doi: 10.3390/toxins10120522

    Figure Lengend Snippet: Electrophoretic analysis of U 1 -SCRTX-Lg1a. Silver-stained 12% SDS-PAGE gel of the crude venom of L. gaucho (CV) (5 µg) and purified antimicrobial U 1 -SCRTX-Lg1a (2.5 µg) under non-reducing conditions. On the left are numbers that correspond to the positions of molecular weight markers (MW) expressed in kDa.

    Article Snippet: SDS-PAGE Analysis Samples of L. gaucho crude venom (5 µg) and U1 -SCRTX-Lg1a (2.5 µg) were analyzed by 12% tris-glycine SDS-PAGE under non-reducing conditions [ ], using a Spectra Multicolor Broad Range Protein Ladder (Thermo Fisher Scientific, Waltham, MA, USA) to estimate the molecular mass.

    Techniques: Staining, SDS Page, Purification, Molecular Weight

    Stability test on released toxoid. SDS-PAGE analysis of protein released from the various MSNPs after ( A ) 0 months ( B ) 3 months ( C ) 6 months. The samples were kept under the following conditions A1: In suspension, kept at 4 °C, A2: In suspension, kept at RT, A3: Lyophilised, kept at 4 °C, A4: Lyophilised, kept at RT. Lanes are loaded as follows: (M) Marker, (−ve) Negative control, (+ve) Positive control, (1) LP2@A1, (2) LP3@A1, (3) SBA-15@A1, (4) LP2@A2, (5) LP3@A2, (6) SBA-15@A2, (7) LP2@A3, (8) LP3@A3, (9) SBA-15@A3, (10) LP2@A4, (11) LP3@A4, (12) SBA-15@A4.

    Journal: Pharmaceutics

    Article Title: An Assessment of Mesoporous Silica Nanoparticle Architectures as Antigen Carriers

    doi: 10.3390/pharmaceutics12030294

    Figure Lengend Snippet: Stability test on released toxoid. SDS-PAGE analysis of protein released from the various MSNPs after ( A ) 0 months ( B ) 3 months ( C ) 6 months. The samples were kept under the following conditions A1: In suspension, kept at 4 °C, A2: In suspension, kept at RT, A3: Lyophilised, kept at 4 °C, A4: Lyophilised, kept at RT. Lanes are loaded as follows: (M) Marker, (−ve) Negative control, (+ve) Positive control, (1) LP2@A1, (2) LP3@A1, (3) SBA-15@A1, (4) LP2@A2, (5) LP3@A2, (6) SBA-15@A2, (7) LP2@A3, (8) LP3@A3, (9) SBA-15@A3, (10) LP2@A4, (11) LP3@A4, (12) SBA-15@A4.

    Article Snippet: SDS-PAGE SDS-polyacrylamide gels from Thermo Scientific (Novex 8–16% Tris-glycine mini gels) were assembled in a Bio-Rad Mini Protean II system and 1× Novex Tris-Glycine SDS running buffer was added to the top and bottom reservoirs.

    Techniques: SDS Page, Marker, Negative Control, Positive Control