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Sds 4 to 12 bis tris protein gels

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SDS–4 to 12% bis-Tris protein gels are pre-cast polyacrylamide gels used for the separation and analysis of proteins. The gels feature a bis-Tris buffer system and a gradient of 4 to 12% acrylamide concentration, which allows for the effective resolution of a wide range of protein molecular weights.

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Chemidoc mp imaging system, by Bio-Rad (3 mentions) Anti spike s2, by Thermo Fisher Scientific (3 mentions)

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Bis-Tris gels (1248 citations) Bis-Tris protein gels (111 citations) 4 to 12% bis-tris gels (10 citations) SDS Bis-Tris gel (7 citations) Bis-Tris gels 4-12% (2 citations)

4 protocols using sds 4 to 12 bis tris protein gels

1

SARS-CoV-2 Spike Protein Characterization

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Forty-eight hours after transfection of cells with plasmid preparations, the culture supernatant was harvested and passed through a 0.45-μm-pore-size filter to remove cellular debris. The filtrate was centrifuged at 15,000 rpm for 120 min to pellet virions. The pelleted virions were lysed in Laemmli reducing buffer (1 M Tris-HCl [pH 6.8], SDS, 100% glycerol, β-mercaptoethanol, and bromophenol blue). Pelleted virions were subjected to electrophoresis on SDS–4 to 12% bis-Tris protein gels (Thermo Fisher Scientific) under reducing conditions. This was followed by electroblotting onto polyvinylidene difluoride (PVDF) membranes. The SARS-CoV-2 Spike proteins were visualized by a ChemiDoc> MP imaging system (Biorad) using anti-Spike S2 (Invitrogen at 1:1000 dilution) and anti-p24 Gag antibodies (NIH AIDS Reagents 1:1000 dilution).
Kemp S.A., Collier D.A., Datir R.P., Ferreira I.A., Gayed S., Jahun A., Hosmillo M., Rees-Spear C., Mlcochova P., Lumb I.U., Roberts D.J., Chandra A., Temperton N., Sharrocks K., Blane E., Modis Y., Leigh K., Briggs J., van Gils M., Smith K.G., Bradley J.R., Smith C., Doffinger R., Ceron-Gutierrez L., Barcenas-Morales G., Pollock D.D., Goldstein R.A., Smielewska A., Skittrall J.P., Gouliouris T., Goodfellow I.G., Gkrania-Klotsas E., Illingworth C.J., McCoy L.E, & Gupta R.K. (2021). SARS-CoV-2 evolution during treatment of chronic infection. Nature, 592(7853), 277-282.
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2

SARS-CoV-2 Spike Protein Characterization

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Forty-eight hours after transfection of cells with plasmid preparations, the culture supernatant was harvested and passed through a 0.45-μm-pore-size filter to remove cellular debris. The filtrate was centrifuged at 15,000 rpm for 120 min to pellet virions. The pelleted virions were lysed in Laemmli reducing buffer (1 M Tris-HCl [pH 6.8], SDS, 100% glycerol, β-mercaptoethanol, and bromophenol blue). Pelleted virions were subjected to electrophoresis on SDS–4 to 12% bis-Tris protein gels (Thermo Fisher Scientific) under reducing conditions. This was followed by electroblotting onto polyvinylidene difluoride (PVDF) membranes. The SARS-CoV-2 Spike proteins were visualized by a ChemiDoc> MP imaging system (Biorad) using anti-Spike S2 (Invitrogen at 1:1000 dilution) and anti-p24 Gag antibodies (NIH AIDS Reagents 1:1000 dilution).
Kemp S.A., Collier D.A., Datir R.P., Ferreira I.A., Gayed S., Jahun A., Hosmillo M., Rees-Spear C., Mlcochova P., Lumb I.U., Roberts D.J., Chandra A., Temperton N., Sharrocks K., Blane E., Modis Y., Leigh K., Briggs J., van Gils M., Smith K.G., Bradley J.R., Smith C., Doffinger R., Ceron-Gutierrez L., Barcenas-Morales G., Pollock D.D., Goldstein R.A., Smielewska A., Skittrall J.P., Gouliouris T., Goodfellow I.G., Gkrania-Klotsas E., Illingworth C.J., McCoy L.E, & Gupta R.K. (2021). SARS-CoV-2 evolution during treatment of chronic infection. Nature, 592(7853), 277-282.
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3

Immunoblotting Analysis of SARS-CoV-2 Spike Proteins

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Forty-eight hours after transfection of cells with plasmid preparations, the culture supernatant was harvested and passed through a 0.45-μm-pore-size filter to remove cellular debris. The filtrate was centrifuged at 15,000 rpm for 120 min to pellet virions. The pelleted virions were lysed in Laemmli reducing buffer (1 M Tris-HCl [pH 6.8], SDS, 100% glycerol, β-mercaptoethanol, and bromophenol blue). Pelleted virions were subjected to electrophoresis on SDS–4 to 12% bis-Tris protein gels (Thermo Fisher Scientific) under reducing conditions. This was followed by electroblotting onto polyvinylidene difluoride (PVDF) membranes. The SARSCOV-2 Spike proteins were visualized by a ChemiDoc® MP imaging system (Biorad) using anti-Spike S2 (Invitrogen) and anti-p24 Gag antibodies.
Kemp S., Collier D., Datir R., Ferreira I., Gayed S., Jahun A., Hosmillo M., Rees-Spear C., Mlcochova P., Lumb I.U., Roberts D.J., Chandra A., Temperton N., Sharrocks K., Blane E., Briggs J., van G.M., Smith K., Bradley J., Smith C., Doffinger R., Ceron-Gutierrez L., Barcenas-Morales G., Pollock D., Goldstein R., Smielewska A., Skittrall J., Gouliouris T., Goodfellow I., Gkrania-Klotsas E., Illingworth C., McCoy L, & Gupta R. (2020). Neutralising antibodies in Spike mediated SARS-CoV-2 adaptation. medRxiv.
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4

Quantifying Viral Particle Production

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Using a previously described method (51 (link)), equal amounts of each of the viral clone plasmid were used to transfect 293T cells, in addition to a VSV-G plasmid and reporter genome-expressing plasmid. Each of the pseudovirions was produced in the absence and presence of a range of concentrations of LPV, added 16 h following transfection.
Forty-eight hours after transfection with the plasmid preparations, the culture supernatant was harvested and passed through a 0.45-μm-pore-size filter to remove cellular debris. The filtrate was centrifuged at 14,000 rpm for 90 min to pellet virions. The pelleted virions were lysed in Laemmli reducing buffer (1 M Tris-HCl [pH 6.8], SDS, 100% glycerol, β-mercaptoethanol, and bromophenol blue). Cell lysates were subjected to electrophoresis on SDS–4 to 12% bis-Tris protein gels (Thermo Fisher Scientific) under reducing conditions. This was followed by electroblotting onto polyvinylidene difluoride (PVDF) membranes. The HIV-1 Gag proteins were visualized by a transilluminator (Alpha Innotech) using anti-p24 Gag antibody.
Datir R., Kemp S., El Bouzidi K., Mlchocova P., Goldstein R., Breuer J., Towers G.J., Jolly C., Quiñones-Mateu M.E., Dakum P.S., Ndembi N, & Gupta R.K. (2020). In Vivo Emergence of a Novel Protease Inhibitor Resistance Signature in HIV-1 Matrix. mBio, 11(6), e02036-20.
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