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Practical lab tips for working with protease inhibitor tablets

Practical tips for working with protease inhibitor tablets… grind them up first to make it easier to dissolve (I like folding a weigh paper in half, sticking a table in the middle, fold it back in half, then using the spatula to gently grind it up, then pour it into the liquid) if you don’t need a whole tablets-worth, make a concentrated stock solution (e.g. dissolve a 50-ml-worth tablet in 2ml of water or 100 mM phosphate buffer, pH 7.0 for 25X) and store aliquots at -20°C for up to 6 months or in the fridge for 1-2 weeks always add to your buffers right before you’re ready to use them (for example, if you’re preparing buffers the day before a purification, make the rest of the buffer but hold off on adding the inhibitor) if you’re doing something with metal-dependent protein(s) or planning to do a metal affinity chromatography step (e.g. NiNTA for a His-tag purification), make sure to use an EDTA-free one. EDTA is a chelator (metal-biter) so it will steal metals from your proteins (and those of metal-dependent proteases, which is one reason it’s sometimes added) and it will strip the metal off of your column. here are some more random practical lab tips: https://bit.ly/lab_tricks_page more on chelators: https://bit.ly/edta_stock &    • Chelators in the lab: EDTA & EGTA bio...   more on his-tag purification: http://bit.ly/histagpurification & http://bit.ly/histagpurification &    • His-Tag Protein Purification theory &...       more about all sorts of things: #365DaysOfScience All (with topics listed) 👉 http://bit.ly/2OllAB0 or search blog: http://thebumblingbiochemist.com