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You wish to express a protein expression system that is very fast, inexpensive, and has established protocols that have been perfected over the past few decades, rather than explore a newer system. Which expression system would you choose?

Why are proteins stored in a buffer with dithiothreitol or β-mercaptoethanol?

Peak 2 below from an ion exchange column shows

Which technique involves concentrating proteins by placing the sample in special device that puts nitrogen pressure on the sample to force the buffer through a membrane?

Peak 1 below from an ion exchange column shows

The protein Src is phosphorylated at Y397, Y419, and Y530 by FAK. When exon 33 is deleted in FAK in cancer cells (Lane 3 below),

You are working with a protein that is polyubiquitinated (a variable number of ubiquitins), which you visualize with an anti-ubiquitin antibody. You treat the protein with an enzyme that cleaves ubiquitin from proteins and degrades it (+ lane). What would be the expected results?

A blue native PAGE is advantageous over a standard native gel because it

You’re working with an MBP-p53 fusion protein, which is linked by covalent peptide bonds. You would expect to see ______ band(s) on SDS-PAGE, and ______ band(s) on a native gel.

You attempt to express a large protein using yeast cells, but the protein did not properly fold with this system. Which of the following is the appropriate next step for achieving successful protein expression?