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In studies where the aim was to solubilize and extract the cuticle, Cox and colleagues [29] showed that treatment with SDS and a 5% solution of the reducing agent ß-mercaptoethanol, along with sonication and heating, solubilized 69% of cuticle content.
The chromatin proteins were then solubilized by heating in WCL-buffer.
Briefly, cell samples were solubilized by heating for 15 min at 90°C in 1.0 N NaOH and total proteins were measured using BCA method [ 44].
Immune complexes were solubilized by heating (5 min 95 °C) in 30 μl 2× SDS-PAGE sample buffer (0.2 % SDS, 62.5 mM Tris HCl pH 6.8, 10%% glycerol and 0.2 μM DTT).
The steel undergoes heat treatments to solubilize the commercial material and later controlling its sensitization degree.
Proteins were solubilized in sample buffer, heated at 95°C for 5 min, separated by SDS-PAGE on 8% polyacrylamide gel and transferred on a 0.2 µm nitrocellulose membrane.
Urinary protein was solubilized and reduced by heating at 100°C for 10 min before loading unto gels.
It has the distinct feature of containing a large amount of starch, which, unlike cellulose, can be easily solubilized by water when heated and hydrolyzed to glucose by amylolytic enzymes without pretreatment for breaking down the biomass recalcitrance.
In stark contrast to the age-associated aggregates, Q-bodies induced upon heat stress (42°C, 30 min) were transient and readily solubilized after the removal of the stress factor.
The wash was discarded and keratins were solubilized in 1% SDS in water by heating at 100°C.
Proteins from the lysates were solubilized in 4× SDS loading buffer and were heated for 5 min at 100°C.
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