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We illustrate the technique with two different fusions used to raise antibodies against the porcine and human analogues of a complement (C) regulatory protein, decay accelerating factor (DAF) (CD55).
Since long-lived antigens are much more likely to be cross-presented than short-lived antigens [24], [25], our results imply that the CD8+ T cell response during CMV infection is limited by the kinetics of protein decay.
For each cell we fit a production rate γ for non-fluorescent Venus; a fluorescence maturation rate β (p and p* represent respectively the unmatured and fluorescent protein concentration); a protein decay rate α and the lag δ.
Overall, the distributions of mRNA abundance, protein abundance and protein decay rates for genes with enhanced ribosome occupancy are similar to those for genes expressed during log phase growth (p-value >0.1; Table 1).
One can biologically manipulate the relevant parameters by controlling e.g. the number of plasmids per cell, protein decay rate or pH of the solution etc., which enables experimental control of the circuits dynamics.
Finally, the third reaction represents protein decay.
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Supplementing them were analyses of uranium, which resembles fluorine in its increase with time, and nitrogen, which decreases as bone protein decays away.
Linear stability analysis shows that in the absence of environmental stimulus this state (the origin) is stable for all model parameter values as long as the protein decay-rate b>0.
CD55, a glycosylphosphatidylinositol-anchored, complement-regulating protein (decay-accelerating factor), is expressed by fibroblast-like synoviocytes (FLS) with high local abundance in the intimal lining layer.
The expression of another complement-inhibitory protein, decay-accelerating factor (DAF), is known to be increased by atorvastatin in normoxia; this response was also significantly enhanced under hypoxic conditions.
Upon shifting of cells to 37°C, the tsTAg protein decayed to almost undetectable levels within 48 hours (data not shown).
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