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This study reports the first procedure for expressing full-length DGAT1 from any species using a bacterial expression system.
The current study reports the first procedure for expressing the full-length recombinant DGAT1 from any species using a bacterial expression system.
Finally, it turned out that a natural procedure for expressing such relations is to calculate the number of the first neighboring vertices, the number of the second neighboring vertices, etc. and, hence, this just corresponds to the definition of the j-sphere.
The objective of this study was to establish a procedure for expressing full-length DGAT1 in E. coli.
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The current work describes a colorimetric assay for measuring RFAP synthase activity, and two modified procedures for expressing recombinant RFAP synthase genes to produce soluble, active enzyme.
In a follow-up study by the same group, Webster et al [ 17] used more stringent inclusion procedures for expressed transcripts, analyzing 8650 transcripts in 486 late-onset Alzheimer's disease (LOAD) cases and 279 control brain samples.
Here a procedure was described for expressing recombinant full-length DGAT1 in a bacterial expression system.
These results suggest that our electroporation procedure is applicable for expressing transgenes in neural progenitors and that in utero electroporation between E35 and E40 is appropriate for obtaining transfected neural progenitors at birth.
We have followed same procedure for over expressed MsDps2 strain; here the vector is pAGAN msdps2.
We have recently developed vectors and procedures for readily expressing and purifying various EBNA1 constructs in E. coli, described in [12], allowing us to generate a diverse library of EBNA1-specific murine monoclonal antibodies (mAbs).
It also describes the general protocols for expressing streptavidin-containing chimeras in E. coli by using the bacteriophage T7 expression system and procedures for purifying and characterizing expressed streptavidin-containing chimeric proteins.
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