nupage reducing agent  (Thermo Fisher)


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    Thermo Fisher nupage reducing agent
    General profiles of Aβ 1–42 oligomers injected in vivo and oligomerization of Aβ 1–42 over time. A , Representative <t>immunoblot</t> of the Aβ 1–42 solution used in our mouse model. The Aβ 1–42 preparation is kept at 25°C for 1 h before administration and is almost exclusively composed of low-molecular-weight Aβ 1–42 oligomers as revealed by electrophoresis on an <t>SDS-NuPAGE</t> Novex 4–12% Bis-Tris gel system using the Aβ antibodies 6E10 and 3D6. B , Representative 6E10-immunoblots of Aβ 1–42 oligomerization. Soluble Aβ 1–42 forms higher molecular weight (MW) oligomers over time and its concentration decreases in favor of insoluble Aβ 1–42 species, which were recovered from the side of low-adhesion tubes with formic acid treatment. Scrambled Aβ 1–42 (Aβscr) is not recognized by the 6E10 antibody ( n = 3 for each gel in 3 independent experiments). C , The Aβ 1–42 solution was verified in nondenaturing condition by TEM 1 h (i–iii) and 24 h (iv–vi) after preparation (i and iv, ×30000, scale bars 0, 5 μm; ii and v, ×85000, scale bars 0, 1 μm; iii and vi, ×140000, scale bars 0, 1 μm).
    Nupage Reducing Agent, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nupage reducing agent/product/Thermo Fisher
    Average 99 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    nupage reducing agent - by Bioz Stars, 2020-05
    99/100 stars

    Images

    1) Product Images from "Neurotoxicity and Memory Deficits Induced by Soluble Low-Molecular-Weight Amyloid-β1–42 Oligomers Are Revealed In Vivo by Using a Novel Animal Model"

    Article Title: Neurotoxicity and Memory Deficits Induced by Soluble Low-Molecular-Weight Amyloid-β1–42 Oligomers Are Revealed In Vivo by Using a Novel Animal Model

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.5901-11.2012

    General profiles of Aβ 1–42 oligomers injected in vivo and oligomerization of Aβ 1–42 over time. A , Representative immunoblot of the Aβ 1–42 solution used in our mouse model. The Aβ 1–42 preparation is kept at 25°C for 1 h before administration and is almost exclusively composed of low-molecular-weight Aβ 1–42 oligomers as revealed by electrophoresis on an SDS-NuPAGE Novex 4–12% Bis-Tris gel system using the Aβ antibodies 6E10 and 3D6. B , Representative 6E10-immunoblots of Aβ 1–42 oligomerization. Soluble Aβ 1–42 forms higher molecular weight (MW) oligomers over time and its concentration decreases in favor of insoluble Aβ 1–42 species, which were recovered from the side of low-adhesion tubes with formic acid treatment. Scrambled Aβ 1–42 (Aβscr) is not recognized by the 6E10 antibody ( n = 3 for each gel in 3 independent experiments). C , The Aβ 1–42 solution was verified in nondenaturing condition by TEM 1 h (i–iii) and 24 h (iv–vi) after preparation (i and iv, ×30000, scale bars 0, 5 μm; ii and v, ×85000, scale bars 0, 1 μm; iii and vi, ×140000, scale bars 0, 1 μm).
    Figure Legend Snippet: General profiles of Aβ 1–42 oligomers injected in vivo and oligomerization of Aβ 1–42 over time. A , Representative immunoblot of the Aβ 1–42 solution used in our mouse model. The Aβ 1–42 preparation is kept at 25°C for 1 h before administration and is almost exclusively composed of low-molecular-weight Aβ 1–42 oligomers as revealed by electrophoresis on an SDS-NuPAGE Novex 4–12% Bis-Tris gel system using the Aβ antibodies 6E10 and 3D6. B , Representative 6E10-immunoblots of Aβ 1–42 oligomerization. Soluble Aβ 1–42 forms higher molecular weight (MW) oligomers over time and its concentration decreases in favor of insoluble Aβ 1–42 species, which were recovered from the side of low-adhesion tubes with formic acid treatment. Scrambled Aβ 1–42 (Aβscr) is not recognized by the 6E10 antibody ( n = 3 for each gel in 3 independent experiments). C , The Aβ 1–42 solution was verified in nondenaturing condition by TEM 1 h (i–iii) and 24 h (iv–vi) after preparation (i and iv, ×30000, scale bars 0, 5 μm; ii and v, ×85000, scale bars 0, 1 μm; iii and vi, ×140000, scale bars 0, 1 μm).

    Techniques Used: Injection, In Vivo, Molecular Weight, Electrophoresis, Western Blot, Concentration Assay, Transmission Electron Microscopy

    Sequestration of soluble Aβ 1–42 oligomers with TTR. A , Representative 6E10-immunoblot of soluble Aβ 1–42 oligomers 1 or 24 h following Aβ 1–42 preparation with TTR (TTR-Aβ, molar (M) ratio of 2:1) or Aβ 1–42 alone (Aβ) at the temperature indicated. B , Increasing doses of TTR mixed with Aβ 1–42 at 37°C during 24 h promoted the sequestration and retrieval of soluble Aβ 1–42 oligomers on an SDS-NuPAGE gel system using the 6E10 antibody. Lower levels of insoluble Aβ 1–42 stuck to the side of low-adhesion tubes were recovered with formic acid treatment while increasing the TTR concentration in Aβ 1–42 solutions (right blot) ( n = 3 for each gel, 3 independent experiments).
    Figure Legend Snippet: Sequestration of soluble Aβ 1–42 oligomers with TTR. A , Representative 6E10-immunoblot of soluble Aβ 1–42 oligomers 1 or 24 h following Aβ 1–42 preparation with TTR (TTR-Aβ, molar (M) ratio of 2:1) or Aβ 1–42 alone (Aβ) at the temperature indicated. B , Increasing doses of TTR mixed with Aβ 1–42 at 37°C during 24 h promoted the sequestration and retrieval of soluble Aβ 1–42 oligomers on an SDS-NuPAGE gel system using the 6E10 antibody. Lower levels of insoluble Aβ 1–42 stuck to the side of low-adhesion tubes were recovered with formic acid treatment while increasing the TTR concentration in Aβ 1–42 solutions (right blot) ( n = 3 for each gel, 3 independent experiments).

    Techniques Used: Concentration Assay

    2) Product Images from "Generation of monoclonal antibodies against native viral proteins using antigen-expressing mammalian cells for mouse immunization"

    Article Title: Generation of monoclonal antibodies against native viral proteins using antigen-expressing mammalian cells for mouse immunization

    Journal: BMC Biotechnology

    doi: 10.1186/s12896-016-0314-5

    Expression of D1NS1 and D4NS1 by transfected HEK cells. HEK cell lysates were analyzed by aqua-staining and Western blot analysis after separation on NuPAGE Novex 4–12 % Bis-Tris Gels under reducing conditions (addition of reducing agent and heating of the samples). While aqua-staining of lysates prepared from HEK-derived cell lines expressing D1NS1 (D1) and D4NS1 (D4) showed no additional band of the predicted size of the NS1 proteins, as compared to the lysates of untransfected HEK cells (−) ( a ), Western blot analysis using anti-hexa-His tag antibodies confirmed the expression of D1NS1 and D4NS1 by the HEK cells ( b ). Western blotting using anti-tubulin antibodies was performed as a control for the amount of cellular proteins of the untransfected and transfected HEK cell lysates loaded on the gels ( c ). M = molecular weight marker in kDa
    Figure Legend Snippet: Expression of D1NS1 and D4NS1 by transfected HEK cells. HEK cell lysates were analyzed by aqua-staining and Western blot analysis after separation on NuPAGE Novex 4–12 % Bis-Tris Gels under reducing conditions (addition of reducing agent and heating of the samples). While aqua-staining of lysates prepared from HEK-derived cell lines expressing D1NS1 (D1) and D4NS1 (D4) showed no additional band of the predicted size of the NS1 proteins, as compared to the lysates of untransfected HEK cells (−) ( a ), Western blot analysis using anti-hexa-His tag antibodies confirmed the expression of D1NS1 and D4NS1 by the HEK cells ( b ). Western blotting using anti-tubulin antibodies was performed as a control for the amount of cellular proteins of the untransfected and transfected HEK cell lysates loaded on the gels ( c ). M = molecular weight marker in kDa

    Techniques Used: Expressing, Transfection, Staining, Western Blot, Derivative Assay, Molecular Weight, Marker

    Related Articles

    Enzyme-linked Immunosorbent Assay:

    Article Title: Development and comparison of enzyme-linked immunosorbent assays based on recombinant trimeric full-length and truncated spike proteins for detecting antibodies against porcine epidemic diarrhea virus
    Article Snippet: .. To determine the purity and quality of the truncated S protein used for ELISA, the truncated S protein was first denatured in NuPAGE® LDS sample buffer (Thermo Fisher Scientific) containing the NuPAGE® reducing agent (Thermo Fisher Scientific), and boiled at 95 °C for 5 min. .. The denatured protein was separated by 10% SDS-PAGE and detected by the Coomassie blue (Bio-rad) protein dye.

    Electrophoresis:

    Article Title: Cysteine Cross-linking Defines the Extracellular Gate for the Leishmania donovani Nucleoside Transporter 1.1 (LdNT1.1) *
    Article Snippet: .. Samples were resolved by electrophoresis on 10% gradient NuPAGE® Novex Bis-Tris gels (Invitrogen) without NuPAGE® reducing agent using the XCell SureLock ™ Mini-Cell system (Invitrogen). .. Subsequently, proteins were electrotransferred under denaturing conditions onto nitrocellulose membranes (Protran, Whatman, GmbH, Germany) using the XCell II™ Blot Module (Invitrogen).

    Immunoprecipitation:

    Article Title: Nucleolin Interacts with the Dengue Virus Capsid Protein and Plays a Role in Formation of Infectious Virus Particles
    Article Snippet: .. The immunoprecipitated sample was then resuspended in Novex SDS sample buffer containing NuPAGE sample-reducing agent (Life Technologies) and incubated at 95°C for 10 min. .. Samples were then run on 10 to 20% Tris-glycine gels and transferred to nitrocellulose membranes.

    Incubation:

    Article Title: Nucleolin Interacts with the Dengue Virus Capsid Protein and Plays a Role in Formation of Infectious Virus Particles
    Article Snippet: .. The immunoprecipitated sample was then resuspended in Novex SDS sample buffer containing NuPAGE sample-reducing agent (Life Technologies) and incubated at 95°C for 10 min. .. Samples were then run on 10 to 20% Tris-glycine gels and transferred to nitrocellulose membranes.

    Staining:

    Article Title: The Escherichia coli β-Barrel Assembly Machinery Is Sensitized to Perturbations under High Membrane Fluidity
    Article Snippet: .. The beads were resuspended in 50 µl 1× NuPAGE LDS sample buffer supplemented with 1× NuPAGE sample reducing agent (Thermo Fisher Scientific) and heated to 95°C for 10 min. Twenty microliters of supernatant was loaded on a 12% bis-Tris SDS-PAGE gel, and proteins were stained with InstantBlue protein stain (Expedeon). ..

    SDS Page:

    Article Title: The Escherichia coli β-Barrel Assembly Machinery Is Sensitized to Perturbations under High Membrane Fluidity
    Article Snippet: .. The beads were resuspended in 50 µl 1× NuPAGE LDS sample buffer supplemented with 1× NuPAGE sample reducing agent (Thermo Fisher Scientific) and heated to 95°C for 10 min. Twenty microliters of supernatant was loaded on a 12% bis-Tris SDS-PAGE gel, and proteins were stained with InstantBlue protein stain (Expedeon). ..

    Derivative Assay:

    Article Title: Pichia pastoris is a Suitable Host for the Heterologous Expression of Predicted Class I and Class II Hydrophobins for Discovery, Study, and Application in Biotechnology
    Article Snippet: .. Nu-PAGE Bis-Tris Mini Gels (4–12% gradient) and NuPAGE LDS sample buffer with NuPAGE reducing agent (Life Technologies, Carlsbad, CA, USA) were used for the analysis of samples derived from the 500 mL cultures and bioreactor productions. .. Furthermore, the accompanying NuPAGE MES SDS running buffer (Life Technologies) was used.

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    Thermo Fisher nupage reducing agent
    Expression and characterization of G1b PEDV S protein by ICC staining and western blotting. a ICC staining of G1b PEDV S-expressing HEK cells using anti-V5 tag antibody. The cells were fixed on the plates using acetone, probed using 1000-fold diluted anti-V5 tag antibody, and detected using anti-mouse IgG antibody conjugated with HRP. The coloration procedure was carried out using the DAB system. b The negative control of the ICC staining of non-transfected HEK cells. The cells were probed with anti-V5 tag antibody following by the anti-mouse IgG antibody conjugated with HRP to distinguish the non-specific signals. c The molecular weight of the purified G1b PEDV S protein (Lane 1) was estimated by western blotting. The purified G1b PEDV S protein was denatured in <t>NuPAGE®</t> <t>LDS</t> sample buffer containing the NuPAGE® reducing agent and boiled at 95 °C for 5 min, then, separated by SDS-PAGE, transferred onto the PVDF membrane, and stained with anti-V5 tag antibody. The HEK cell lysate was used as the negative control (Lane 2). The ladder is shown in kilodalton (kDa)
    Nupage Reducing Agent, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nupage reducing agent/product/Thermo Fisher
    Average 99 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    nupage reducing agent - by Bioz Stars, 2020-05
    99/100 stars
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    Expression and characterization of G1b PEDV S protein by ICC staining and western blotting. a ICC staining of G1b PEDV S-expressing HEK cells using anti-V5 tag antibody. The cells were fixed on the plates using acetone, probed using 1000-fold diluted anti-V5 tag antibody, and detected using anti-mouse IgG antibody conjugated with HRP. The coloration procedure was carried out using the DAB system. b The negative control of the ICC staining of non-transfected HEK cells. The cells were probed with anti-V5 tag antibody following by the anti-mouse IgG antibody conjugated with HRP to distinguish the non-specific signals. c The molecular weight of the purified G1b PEDV S protein (Lane 1) was estimated by western blotting. The purified G1b PEDV S protein was denatured in NuPAGE® LDS sample buffer containing the NuPAGE® reducing agent and boiled at 95 °C for 5 min, then, separated by SDS-PAGE, transferred onto the PVDF membrane, and stained with anti-V5 tag antibody. The HEK cell lysate was used as the negative control (Lane 2). The ladder is shown in kilodalton (kDa)

    Journal: BMC Veterinary Research

    Article Title: Development and comparison of enzyme-linked immunosorbent assays based on recombinant trimeric full-length and truncated spike proteins for detecting antibodies against porcine epidemic diarrhea virus

    doi: 10.1186/s12917-019-2171-7

    Figure Lengend Snippet: Expression and characterization of G1b PEDV S protein by ICC staining and western blotting. a ICC staining of G1b PEDV S-expressing HEK cells using anti-V5 tag antibody. The cells were fixed on the plates using acetone, probed using 1000-fold diluted anti-V5 tag antibody, and detected using anti-mouse IgG antibody conjugated with HRP. The coloration procedure was carried out using the DAB system. b The negative control of the ICC staining of non-transfected HEK cells. The cells were probed with anti-V5 tag antibody following by the anti-mouse IgG antibody conjugated with HRP to distinguish the non-specific signals. c The molecular weight of the purified G1b PEDV S protein (Lane 1) was estimated by western blotting. The purified G1b PEDV S protein was denatured in NuPAGE® LDS sample buffer containing the NuPAGE® reducing agent and boiled at 95 °C for 5 min, then, separated by SDS-PAGE, transferred onto the PVDF membrane, and stained with anti-V5 tag antibody. The HEK cell lysate was used as the negative control (Lane 2). The ladder is shown in kilodalton (kDa)

    Article Snippet: To determine the purity and quality of the truncated S protein used for ELISA, the truncated S protein was first denatured in NuPAGE® LDS sample buffer (Thermo Fisher Scientific) containing the NuPAGE® reducing agent (Thermo Fisher Scientific), and boiled at 95 °C for 5 min.

    Techniques: Expressing, Immunocytochemistry, Staining, Western Blot, Negative Control, Transfection, Molecular Weight, Purification, SDS Page