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Evasin-1 was expressed using the baculovirus system in insect cells (Bac-to-Bac, Life technologies/Invitrogen).
A recombinant protein was produced using the baculovirus system and we tested its catabolic properties towards a plant volatile and the sex pheromone components.
The MVP sequence alone encodes all the needed structural information that enables the protein to self-assemble and form a recombinant vault nanoparticle using the baculovirus system [9].
These dimeric fusion proteins are expressed at high levels using the baculovirus system, and unpurified supernatants are used directly for staining.
For production of chimeric antibody using the baculovirus system, cTA12 reached a concentration of 5 µg/ml, corresponding to the lower part of the range (between 6 and 18 µg/ml) previously published [28].
Expression of MVP in insect cells using the baculovirus system results in production of vault-like particles formed entirely from the expressed MVP, leading to the conclusion that MVP alone is sufficient to form vault-like particles.
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We used the baculovirus system and a dual-tag strategy to purify intact recombinant WT and mutant CHD7 proteins.
Initially we used the baculovirus system to generate cell lysates expressing both cdk2 (wild type or P45L mutant) and cyclin E1.
In this study, VLPs were produced in HEK293 suspension cells using the Bacmam transduction system and Sf9 cells using the baculovirus infection system.
Recombinant Integrator subunits with an N-terminal Flag tag were expressed in Sf9 cells using the baculovirus expression system.
Margine, I., Palese, P. & Krammer, F. Expression of functional recombinant hemagglutinin and neuraminidase proteins from the novel H7N9 influenza virus using the baculovirus expression system.
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