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Sds gel loading buffer

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SDS-gel loading buffer is a solution used to prepare protein samples for separation by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). It contains SDS, a detergent that denatures proteins and gives them a uniform negative charge, as well as other components that help the samples load and run properly on the gel.

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Lab products found in correlation

Hiv ig serum, by Jackson ImmunoResearch (2 mentions) Western lightning, by PerkinElmer (2 mentions) Leupeptin, by Roche (1 mentions)

Close spelling variants of this product

SDS loading buffer (17 citations) Gel loading buffer (23 citations) Loading buffer (104 citations)

3 protocols using sds gel loading buffer

1

Kinetics of 17b Fab Binding

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The kinetics of 17b binding were measured by incubating SOSIP.664 trimers at 1 mg/mL with a 3-fold molar excess of 17b Fab (relative to protomers), and monitoring complex formation by BN-PAGE. Immunoprecipitation experiments were initiated by addition of 2 μg of 17b Fab to 3 μg of KNH1144 SOSIP.664 trimers in 120 μl of PBS plus 2 % DMSO, together with: no ligand; 100 μM NBD-556; 100 μM BMS-806 or 0.4 μM of sCD4. Pre-washed protein G sepharose beads were added after the mixtures were incubated at 25°C for various times, and rotated on a nutator for 1 h. The beads were pelleted by centrifugation and washed four times in PBS plus 0.1 % tween 20, followed by re-suspension and boiling in reducing SDS-gel loading buffer (Invitrogen). Western blots were probed with HIV-Ig serum (1:1000 dilution), followed by anti-human-HRP (1:5000 dilution) (Jackson Immunoresearch). The labeled bands were visualized by chemilluminescence (Western lightning, Perkin Elmer).
Guttman M., Cupo A., Julien J.P., Sanders R.W., Wilson I.A., Moore J.P, & Lee K.K. (2015). Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env. Nature communications, 6, 6144.
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2

RecBCD-Mediated DNA Cleavage Kinetics

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Reactions (typically 10 µl per gel lane) were at room temperature and
typically contained 5 nM (as molecules) lambda DNA, 2.5 nM RecBCD enzyme in 20 mM Mops-KOH
(pH 7.4), and 2.5 or 8 mM magnesium acetate. RecBCD enzyme was allowed to bind DNA, and
reactions were started by addition of ATP to 5 mM. After (typically) 15 s, trypsin was
added, incubation continued for a further 60 s, and the trypsin reaction terminated by
addition of leupeptin (Roche) to 16 mM, followed by chilling, addition of SDS-gel loading
buffer (Invitrogen), and heating to 65 °C. Reactions with other proteases, or
those requiring concentration before analysis, were terminated by addition of an equal
volume of cold 20% trichloroacetic acid. Following addition of insulin to 0.25
mg/ml, we recovered precipitates by centrifugation, washed them with cold acetone, and
dissolved them in loading buffer.
Taylor A.F., Amundsen S.K., Guttman M., Lee K.K., Luo J., Ranish J, & Smith G.R. (2014). Control of RecBCD Enzyme Activity by DNA Binding- and Chi Hotspot-Dependent Conformational Changes. Journal of molecular biology, 426(21), 3479-3499.
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3

Kinetics of 17b Fab Binding

Check if the same lab product or an alternative is used in the 5 most similar protocols
The kinetics of 17b binding were measured by incubating SOSIP.664 trimers at 1 mg/mL with a 3-fold molar excess of 17b Fab (relative to protomers), and monitoring complex formation by BN-PAGE. Immunoprecipitation experiments were initiated by addition of 2 μg of 17b Fab to 3 μg of KNH1144 SOSIP.664 trimers in 120 μl of PBS plus 2 % DMSO, together with: no ligand; 100 μM NBD-556; 100 μM BMS-806 or 0.4 μM of sCD4. Pre-washed protein G sepharose beads were added after the mixtures were incubated at 25°C for various times, and rotated on a nutator for 1 h. The beads were pelleted by centrifugation and washed four times in PBS plus 0.1 % tween 20, followed by re-suspension and boiling in reducing SDS-gel loading buffer (Invitrogen). Western blots were probed with HIV-Ig serum (1:1000 dilution), followed by anti-human-HRP (1:5000 dilution) (Jackson Immunoresearch). The labeled bands were visualized by chemilluminescence (Western lightning, Perkin Elmer).
Guttman M., Cupo A., Julien J.P., Sanders R.W., Wilson I.A., Moore J.P, & Lee K.K. (2015). Antibody potency relates to the ability to recognize the closed, pre-fusion form of HIV Env. Nature communications, 6, 6144.
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