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Tris gels

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Tris gels are a type of gel electrophoresis system used for the separation and analysis of proteins. They are composed of a polyacrylamide matrix with Tris-based buffer solutions. Tris gels provide a stable and consistent environment for the separation of protein samples based on their molecular weight.

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Lab products found in correlation

Anti tsg101, by GeneTex (2 mentions) Anti flotillin 1, by BD (2 mentions) Anti cd81, by Thermo Fisher Scientific (2 mentions) Anti hsp90, by Enzo Life Sciences (2 mentions) Anti ferritin, by Abcam (2 mentions) Anti lactoferrin, by Santa Cruz Biotechnology (2 mentions) Anti mhc 1, by LifeSpan BioSciences (2 mentions) Anti calnexin, by Santa Cruz Biotechnology (2 mentions) Anti transferrin, by Santa Cruz Biotechnology (2 mentions) Pvdf membrane, by Bio-Rad (2 mentions) Anti gm130, by BD (2 mentions)

Close spelling variants of this product

SDS/PAGE Tris·HCl gels 4–20% Tris-glycine sodium dodecyl sulfate-polyacrylamide gels Precast 4–20% Tris-HCl gels Precast 4–15 Bis-Tris gels Tris-Glycine-eXtendet SDS-PAGE gels Any-kD Tris-glycine gels Tris-Glycine SDS gradient gels Polyacrylamide Tris–Borate–EDTA gels Bis-Tris XT denaturing 10% SDS polyacrylamide gels 4–15% gradient Tris–HCl polyacrylamide gels for electrophoresis fractionation

3 protocols using tris gels

1

Protein Separation and Detection via SDS-PAGE and Western Blotting

Cited 1 time
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Proteins were separated by SDS-PAGE on Tris gels (Bio-Rad) and were transferred onto PVDF membranes (Bio-Rad), as previously described (Bomberger et al., 2011 (link)). The following antibodies were used for protein detection: anti-ALIX (EMD Milllipore), anti-calnexin (Santa Cruz Biotechnology), anti-CD81 (Thermo Fisher), anti-Flotillin-1 (BD Biosciences), anti-ferritin (Abcam), anti-GM130 (BD Biosciences), anti-Hsp90 (Enzo Life Sciences), anti-lactoferrin (Santa Cruz Biotechnology), anti-MHC-I (LifeSpan Biosciences), anti-RSV (Meridian Life Science, Inc.), anti-transferrin (Santa Cruz Biotechnology), anti-Tsg101 (GeneTex). Secondary antibodies were goat anti-mouse, goat anti-rabbit, and rat anti-goat conjugated to HRP (Bio-Rad).
Hendricks M.R., Lane S., Melvin J.A., Ouyang Y., Stolz D.B., Williams J.V., Sadovsky Y, & Bomberger J.M. (2021). Extracellular vesicles promote transkingdom nutrient transfer during viral-bacterial co-infection. Cell reports, 34(4), 108672.
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2

Protein Separation and Detection via SDS-PAGE and Western Blotting

Cited 1 time
Check if the same lab product or an alternative is used in the 5 most similar protocols
Proteins were separated by SDS-PAGE on Tris gels (Bio-Rad) and were transferred onto PVDF membranes (Bio-Rad), as previously described (Bomberger et al., 2011 (link)). The following antibodies were used for protein detection: anti-ALIX (EMD Milllipore), anti-calnexin (Santa Cruz Biotechnology), anti-CD81 (Thermo Fisher), anti-Flotillin-1 (BD Biosciences), anti-ferritin (Abcam), anti-GM130 (BD Biosciences), anti-Hsp90 (Enzo Life Sciences), anti-lactoferrin (Santa Cruz Biotechnology), anti-MHC-I (LifeSpan Biosciences), anti-RSV (Meridian Life Science, Inc.), anti-transferrin (Santa Cruz Biotechnology), anti-Tsg101 (GeneTex). Secondary antibodies were goat anti-mouse, goat anti-rabbit, and rat anti-goat conjugated to HRP (Bio-Rad).
Hendricks M.R., Lane S., Melvin J.A., Ouyang Y., Stolz D.B., Williams J.V., Sadovsky Y, & Bomberger J.M. (2021). Extracellular vesicles promote transkingdom nutrient transfer during viral-bacterial co-infection. Cell reports, 34(4), 108672.
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3

Isolation and Characterization of Membrane Vesicles

Cited 2 times
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CPE-treated claudin-4 transfectant or Caco-2 cell cultures were centrifuged at 2, 000 × g for 3 min, and those supernatants were subjected to sequential centrifugation (30 min at 10,000 × g to collect large membrane vesicles and then 90 min at 100,000 × g to collect small membrane vesicles [49 (link), 50 (link)]). Pelleted membrane vesicles resuspended back to natural (1×) concentrations, or supernatant fractions from centrifugations, were applied to parent cells for MTT cytotoxicity testing or Western blotted with a cadherin antibody (Cell Signaling Technology, Inc.) to validate vesicle depletion from supernatants. For cadherin Western blots, equal amounts of protein were separated by SDS-PAGE on Tris gels (Bio-Rad) and transferred to a polyvinylidene difluoride (PVDF) membrane.
Shrestha A., Hendricks M.R., Bomberger J.M, & McClane B.A. (2016). Bystander Host Cell Killing Effects of Clostridium perfringens Enterotoxin. mBio, 7(6), e02015-16.
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