“…The composition of the running solution can strongly affect LFA performances, partly because undesirable interfacial problems can occur. In particular, nonspecific interactions with capture or detection antibodies or steric hindrance on the NP or nitrocellulose membrane can modify the background signal on the membrane as well as the assay sensitivity. , Based on empirical observations, it is generally accepted that a relatively high salt concentration increases the reproducibility and sensitivity of the LFA by controlling the pH and ionic strength of the running solution, thus avoiding protein denaturation. , On the other hand, zwitterionic or nonionic detergents, such as CHAPS or Tween 20, (i) stabilize proteins (particularly membrane proteins), (ii) can renature antibody epitopes, (iii) allow the sample to flow through the strip, (iv) elute antigens adsorbed nonspecifically on the membrane, and (v) act as blocking agents to saturate free binding sites, alone or in combination with proteins (BSA, ovalbumin, casein, etc), thereby reducing background on the membrane. − The addition of sodium azide also protects buffers from microbial contamination …”