Answers from Aladdin Scientific's technical team to 290+ questions on antibodies, reagents, purity, storage and experiment troubleshooting.
BCA concentration measured protein concentration 3mg/ml, but after adding buffer found no protein bands appeared, what is the reason?
Protein samples boiled in buffer are blue in color and turn blue-violet after being left at -80°C. What is the reason for this? Does it affect the subsequent electrophoresis?
After the protein sample has been spiked with Sampling Buffer, boiled at 95°C for 10 min, and centrifuged at 14,000, individual samples will be delaminated prior to sampling, what is the reason for this?
Is there a requirement for protein concentration for this product? If the protein concentration is high, do I need to increase the concentration of the buffer?
Can it be used in non-denaturing electrophoresis?
When extracting proteins from suspension cells, can I add the product directly to boil and denature them?
What is the reason why the protein after denaturation by adding buffer tends to be difficult to sink and float up easily when spotting? What should I do to solve this problem?
How can I quickly remove the bromophenol blue that may be obscuring the bands at the end of the gel run?
After adding buffer to boil denatured proteins for cryopreservation, do they still need to be boiled after they are removed again? Why?
