Answers from Aladdin Scientific's technical team to 290+ questions on antibodies, reagents, purity, storage and experiment troubleshooting.
After lysing the cells first with the lysate, add 5x upsampling buffer in a 4:1 volume, then water bath denaturation is it better to use a 100 degree water bath or a 95 degree water bath?
What is the reason that the protein added to the buffer cooks without precipitation, but the next day when the sample is removed and spiked, precipitation appears? What should be done?
If the protein contains polymer heterobands, dimers may be present, do I need to add doubling buffer to open the dimers?
When electrophoresis is performed on a sample denatured with buffer, if the sample does not move when the sample volume is high, and if the sample volume is low, the sample runs fast and unevenly, how to solve the problem?
If the concentration of the denatured sample is high, how should it be diluted?
Does the protein's own charge affect the buffer?
Sediment has been found in this product, can I continue to use it? What should be done?
Does the sample buffer have an effect on the effectiveness of the electrophoresis solution? If the buffer is accidentally run out does it need to replace the electrophoresis solution?
Is it feasible to boil and denature proteins before adding protein upload buffer?
