For making a general mammalian cell lysis buffer, I have been using HEPES as a component. However, I came across a paper where they have used Tris in place of HEPES while the rest of the parameters are the same. They used 293t cells while I am using lentivirus infected A549 cells with a PLJM1 backbone and a histag-fused protein insert. Upon running a western blot and probing with anti-His primary antibody, the bands look very faint. All components of my buffers are pH balanced as per published protocols.
Tris should work just fine as long as the pH is not too low for it (the pKa is 8.1), so don't go below 7.4, and make sure the Tris concentration is high enough to supply sufficient buffering capacity (at least 50 mM). The components you want to avoid in the lysis buffer are reducing agents (e.g. dithiothreitol, mercaptoethanol), chelating agents (e.g., EDTA, EGTA, citrate), and, of course, imidazole that interfere with immobilized metal affinity chromatography.
In my experience, the only matter for it was the pH of the solution you were using. as it mentioned by @Adam, the consideration is the optimum pH buffering ability of the compound, e.g. tris is good at 7 to 9.2, HEPES 6.8 to 8.2, MES 5.5. to 6.7, etc.
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