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The results showed that both proteins could be effectively adsorbed on the membrane, but the adsorption capacities were influenced by the pH, the initial protein concentration and the CMCS content in the membrane.

Analysis of Hv1 and Nox2 colocalization was performed only in cells in which at least moderate labeling (two times above background) for both proteins could be detected.

A previous study investigating the interaction between NOXO1 and NOXA1 showed that both proteins could be co-immunopricipitated from COS cells [34], which led to the suggestion that they interacted in a manner similar to p47phox and p67phox.

As shown in Figure 3A and 3B both proteins could be detected at their expected molecular weight at approx. 40 and 50 kDa, respectively, which is in agreement with the protein bands of the control lysate of HeLa cells.

In general immunoreactivity for both proteins could be detected in the larger processes, but in many of the finer processes, TK immunoreactivity was visible while GFAP was not, and TK immunoreactivity generally occupied a greater area of the soma than did GFAP (Figure 1).

Furthermore, a significant relationship between both proteins could be demonstrated (P less than 0.0001).

Both recombinant proteins could be abundantly and solubly expressed and easily purified, exhibiting high stability and potent inhibitory activity on HIV-1 fusion with IC50 values of 16.2 ± 2.8 and 2.8 ± 0.63 nM, respectively.

Both recombinant proteins could be detected by the anti-histidine mAb, with a positive signal located in the cytoplasm.

Both CREG proteins could be processed by either enzyme, leading to a final processing product of about 18 kDa (msCREG) and 17 kDa (dCREG), respectively.

The high affinity of RanGTP and RanGDP for Imp-βKetD and Imp-βKetRE34 suggests that both mutant proteins could be prone to dissociate from Imp-α2, thus inducing a release of the cargo proteins carried by Imp-α2, or it may prevent their binding to Imp-α2.

After confirming that both modified EspG proteins could be secreted at equivalent levels to Δ espG + pEspG HA (Fig.  5A) we investigated their cellular localization by immunofluorescence (Fig.  5B).