Review



standard towbin transfer buffer  (Bio-Rad)


Bioz Verified Symbol Bio-Rad is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 98
      Buy from Supplier

    Structured Review

    Bio-Rad standard towbin transfer buffer
    Fig. 5. Application of the refolding procedure to squalene monooxygenase (SM) fused with three different GFP variants. The SDS-PAGE samples were prepared from HEK293 cells stably expressing SM-FLAG-tGFP or HEK293 cells transiently expressing either SM-FLAG-EGFP or SM-FLAG-msfGFP (sfGFP-V206K). A. In-gel refolding and subsequent Western blotting of SM-GFPs. The SDS-PAGE samples were heated at the indicated temperature for 5 min and resolved on SDS-PAGE (10 % gel). The gel was imaged before and after refolding in the optimized refolding buffer (1 % αCD and 20 % MeOH <t>in</t> <t>Tris-Gly</t> buffer, 30 min at room temperature). The gel after refolding was equilibrated in <t>Towbin</t> transfer buffer supplemented with 0.05 % SDS for 15 min, and proteins were wet-transferred to the PVDF membrane with the same transfer buffer. The membrane was probed with an anti-FLAG antibody and then re-probed with an anti-SM antibody after stripping. The filled and open arrowheads represent the denatured 95 kDa band and the non-denatured 77 kDa band, respectively. B. Quantification of the non-denatured and the denatured bands. The gray solid lines represent the fluorescent intensity of the lower, native band, and the magenta dashed lines represent the fluorescent intensity of the upper, denatured band. In-gel fluorescence was normalized to the sum of the two bands observed for the non-boiled (RT) samples. Data are mean ± SEM (n = 5 independent refolding experiments).
    Standard Towbin Transfer Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 21506 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/standard towbin transfer buffer/product/Bio-Rad
    Average 98 stars, based on 21506 article reviews
    standard towbin transfer buffer - by Bioz Stars, 2026-06
    98/100 stars

    Images

    1) Product Images from "In-gel refolding allows fluorescence detection of fully denatured GFPs after SDS-PAGE."

    Article Title: In-gel refolding allows fluorescence detection of fully denatured GFPs after SDS-PAGE.

    Journal: Analytical biochemistry

    doi: 10.1016/j.ab.2025.115861

    Fig. 5. Application of the refolding procedure to squalene monooxygenase (SM) fused with three different GFP variants. The SDS-PAGE samples were prepared from HEK293 cells stably expressing SM-FLAG-tGFP or HEK293 cells transiently expressing either SM-FLAG-EGFP or SM-FLAG-msfGFP (sfGFP-V206K). A. In-gel refolding and subsequent Western blotting of SM-GFPs. The SDS-PAGE samples were heated at the indicated temperature for 5 min and resolved on SDS-PAGE (10 % gel). The gel was imaged before and after refolding in the optimized refolding buffer (1 % αCD and 20 % MeOH in Tris-Gly buffer, 30 min at room temperature). The gel after refolding was equilibrated in Towbin transfer buffer supplemented with 0.05 % SDS for 15 min, and proteins were wet-transferred to the PVDF membrane with the same transfer buffer. The membrane was probed with an anti-FLAG antibody and then re-probed with an anti-SM antibody after stripping. The filled and open arrowheads represent the denatured 95 kDa band and the non-denatured 77 kDa band, respectively. B. Quantification of the non-denatured and the denatured bands. The gray solid lines represent the fluorescent intensity of the lower, native band, and the magenta dashed lines represent the fluorescent intensity of the upper, denatured band. In-gel fluorescence was normalized to the sum of the two bands observed for the non-boiled (RT) samples. Data are mean ± SEM (n = 5 independent refolding experiments).
    Figure Legend Snippet: Fig. 5. Application of the refolding procedure to squalene monooxygenase (SM) fused with three different GFP variants. The SDS-PAGE samples were prepared from HEK293 cells stably expressing SM-FLAG-tGFP or HEK293 cells transiently expressing either SM-FLAG-EGFP or SM-FLAG-msfGFP (sfGFP-V206K). A. In-gel refolding and subsequent Western blotting of SM-GFPs. The SDS-PAGE samples were heated at the indicated temperature for 5 min and resolved on SDS-PAGE (10 % gel). The gel was imaged before and after refolding in the optimized refolding buffer (1 % αCD and 20 % MeOH in Tris-Gly buffer, 30 min at room temperature). The gel after refolding was equilibrated in Towbin transfer buffer supplemented with 0.05 % SDS for 15 min, and proteins were wet-transferred to the PVDF membrane with the same transfer buffer. The membrane was probed with an anti-FLAG antibody and then re-probed with an anti-SM antibody after stripping. The filled and open arrowheads represent the denatured 95 kDa band and the non-denatured 77 kDa band, respectively. B. Quantification of the non-denatured and the denatured bands. The gray solid lines represent the fluorescent intensity of the lower, native band, and the magenta dashed lines represent the fluorescent intensity of the upper, denatured band. In-gel fluorescence was normalized to the sum of the two bands observed for the non-boiled (RT) samples. Data are mean ± SEM (n = 5 independent refolding experiments).

    Techniques Used: SDS Page, Stable Transfection, Expressing, Western Blot, Membrane, Stripping Membranes, Fluorescence



    Similar Products

    standard towbin transfer buffer  (Bio-Rad)
    98
    Bio-Rad standard towbin transfer buffer
    Fig. 5. Application of the refolding procedure to squalene monooxygenase (SM) fused with three different GFP variants. The SDS-PAGE samples were prepared from HEK293 cells stably expressing SM-FLAG-tGFP or HEK293 cells transiently expressing either SM-FLAG-EGFP or SM-FLAG-msfGFP (sfGFP-V206K). A. In-gel refolding and subsequent Western blotting of SM-GFPs. The SDS-PAGE samples were heated at the indicated temperature for 5 min and resolved on SDS-PAGE (10 % gel). The gel was imaged before and after refolding in the optimized refolding buffer (1 % αCD and 20 % MeOH <t>in</t> <t>Tris-Gly</t> buffer, 30 min at room temperature). The gel after refolding was equilibrated in <t>Towbin</t> transfer buffer supplemented with 0.05 % SDS for 15 min, and proteins were wet-transferred to the PVDF membrane with the same transfer buffer. The membrane was probed with an anti-FLAG antibody and then re-probed with an anti-SM antibody after stripping. The filled and open arrowheads represent the denatured 95 kDa band and the non-denatured 77 kDa band, respectively. B. Quantification of the non-denatured and the denatured bands. The gray solid lines represent the fluorescent intensity of the lower, native band, and the magenta dashed lines represent the fluorescent intensity of the upper, denatured band. In-gel fluorescence was normalized to the sum of the two bands observed for the non-boiled (RT) samples. Data are mean ± SEM (n = 5 independent refolding experiments).
    Standard Towbin Transfer Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/standard towbin transfer buffer/product/Bio-Rad
    Average 98 stars, based on 1 article reviews
    standard towbin transfer buffer - by Bioz Stars, 2026-06
    98/100 stars
    		  Buy from Supplier

    Image Search Results


    Fig. 5. Application of the refolding procedure to squalene monooxygenase (SM) fused with three different GFP variants. The SDS-PAGE samples were prepared from HEK293 cells stably expressing SM-FLAG-tGFP or HEK293 cells transiently expressing either SM-FLAG-EGFP or SM-FLAG-msfGFP (sfGFP-V206K). A. In-gel refolding and subsequent Western blotting of SM-GFPs. The SDS-PAGE samples were heated at the indicated temperature for 5 min and resolved on SDS-PAGE (10 % gel). The gel was imaged before and after refolding in the optimized refolding buffer (1 % αCD and 20 % MeOH in Tris-Gly buffer, 30 min at room temperature). The gel after refolding was equilibrated in Towbin transfer buffer supplemented with 0.05 % SDS for 15 min, and proteins were wet-transferred to the PVDF membrane with the same transfer buffer. The membrane was probed with an anti-FLAG antibody and then re-probed with an anti-SM antibody after stripping. The filled and open arrowheads represent the denatured 95 kDa band and the non-denatured 77 kDa band, respectively. B. Quantification of the non-denatured and the denatured bands. The gray solid lines represent the fluorescent intensity of the lower, native band, and the magenta dashed lines represent the fluorescent intensity of the upper, denatured band. In-gel fluorescence was normalized to the sum of the two bands observed for the non-boiled (RT) samples. Data are mean ± SEM (n = 5 independent refolding experiments).

    Journal: Analytical biochemistry

    Article Title: In-gel refolding allows fluorescence detection of fully denatured GFPs after SDS-PAGE.

    doi: 10.1016/j.ab.2025.115861

    Figure Lengend Snippet: Fig. 5. Application of the refolding procedure to squalene monooxygenase (SM) fused with three different GFP variants. The SDS-PAGE samples were prepared from HEK293 cells stably expressing SM-FLAG-tGFP or HEK293 cells transiently expressing either SM-FLAG-EGFP or SM-FLAG-msfGFP (sfGFP-V206K). A. In-gel refolding and subsequent Western blotting of SM-GFPs. The SDS-PAGE samples were heated at the indicated temperature for 5 min and resolved on SDS-PAGE (10 % gel). The gel was imaged before and after refolding in the optimized refolding buffer (1 % αCD and 20 % MeOH in Tris-Gly buffer, 30 min at room temperature). The gel after refolding was equilibrated in Towbin transfer buffer supplemented with 0.05 % SDS for 15 min, and proteins were wet-transferred to the PVDF membrane with the same transfer buffer. The membrane was probed with an anti-FLAG antibody and then re-probed with an anti-SM antibody after stripping. The filled and open arrowheads represent the denatured 95 kDa band and the non-denatured 77 kDa band, respectively. B. Quantification of the non-denatured and the denatured bands. The gray solid lines represent the fluorescent intensity of the lower, native band, and the magenta dashed lines represent the fluorescent intensity of the upper, denatured band. In-gel fluorescence was normalized to the sum of the two bands observed for the non-boiled (RT) samples. Data are mean ± SEM (n = 5 independent refolding experiments).

    Article Snippet: Proteins were transferred from the gel after in-gel renaturation, which was equilibrated with a standard Towbin transfer buffer (25 mM Tris, 192 mM Gly, 20 % (v/v) MeOH) supplemented with 0.05 % SDS for 10 min, to a PVDF membrane equilibrated with the standard Towbin transfer buffer in a Mini-protean tetra wet transfer system (Bio-Rad) with myPowerII 500 power supply (AE-8155, ATTO).

    Techniques: SDS Page, Stable Transfection, Expressing, Western Blot, Membrane, Stripping Membranes, Fluorescence