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The biochemical, immunological, and functional activities of C-rmCRP were shown to be comparable to biological mCRP, making the recombinant protein an excellent and advantageous research reagent for the study of mCRP.
It has recently been engineered to glycosylate proteins in a human-like manner, making the recombinant products more acceptable to the regulatory authorities [1].
Proteolytic cleavage resulting in removal of disulfide-bonding cysteine residues would have also removed the N-terminal FLAG epitope, making the recombinant protein undetectable using antibodies against the FLAG epitope.
The goal of these delivery approaches was that of making the recombinant proteins available for therapy of local pathologies or for local effects: antibodies for passive immunotherapy of local infections [ 3, 4], cytokines as adjuvants for mucosal vaccines [ 5, 6], inhibitory cytokines for anti-inflammatory therapy of localised chronic inflammatory diseases (IBD-like pathologies) [ 7- 9].
Since the enzyme has a relatively low PI of 4.4 and few secreted proteins are present in the supernatant, we used one-step weak anion exchange chromatography to isolate the target protein, thus making the recombinant production of the enzyme more favorable.
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Moreover, it is one of the most xylose tolerant enzymes and this quality has made the recombinant enzyme very useful for saccharification of xylan-containing polysaccharides.
The overexpression of the threonine synthesis pathway and threonine dehydrogenase made the recombinant Halomonas TD08 able to produce poly 3-hydroxybutyrate-co-3-hydroxyvalerate) or poly 3-hydroxybutyrate-co-3-hydroxyvaleratete or 3HV, from various carbohydrates as the sole carbon source.
To test this idea, we made the recombinant adenovirus expressing green fluorescent protein-tagged Brn2 (GFP-Brn2), and transduced cultured human epidermal keratinocytes.
Glu at position 705 in the BPSM BvgS made the recombinant strain more responsive to nicotinate than its parent, with 4 mM nicotinic acid causing the complete loss of BvgS activity (Fig. 5B).
The replacement of both VFT1 and VFT2 of the BPSM BvgS by those of RB50 (BPBb1+2) did not affect the level of BvgS activity in the absence of modulation, but it made the recombinant bacteria much more sensitive to nicotinic acid than their parent (Fig. 4B,C).
TC made the recombinant SVec plasmids carrying the FTM- genes and established the expression system.
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