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To date, there are only a few members of the V1r and V2r families of receptors that have been functionally expressed in heterologous expression systems (Shirokova et al., 2008; Dey and Matsunami, 2011).
One representative of these genes has been functionally expressed in Escherichia coli.
These three OTases have been functionally expressed in Escherichia coli and exhibit relaxed glycan specificity, which opens the door to the possibility of engineering recombinant glycoproteins for biotechnological applications.
Moreover, the hANT1, 2, 3 proteins have all been functionally expressed in yeast mitochondria [8], [9].
Several GPCRs have been functionally expressed in E.coli and purified in milligram quantities as fusion proteins [22], [23], [24].
Human adenosine A2a receptor has been functionally expressed in E. coli as fusion with periplasmic maltose-binding protein (MBP) at the N-terminus.
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In this study, pullulanase gene (pulN) was functionally expressed in E. coli through expression vector replacement and induction expression strategy optimization.
This novel clone was functionally expressed in both prokaryotic and eukaryotic expression systems and exhibited ODD activity.
The co-factors required for NaV1.9 expression have not been defined, but this channel can only be functionally expressed in dorsal root ganglion neurons where it rescues the expression of persistent current in NaV1.9 knockout neurons (Ostman et al., 2008).
The CPPS and KS from S. rebaudiana were functionally expressed in a heterologous host E. coli.
The XylA gene encoding the Piromyces xylose isomerase was functionally expressed in Saccharomyces cerevisiae.
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