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Expression and Purification of Recombinant Proteins That Have Native Amino,,,Acid Sequence

ide gaps had been repaired in vivo by E. coli. This result confirms that there are no constraints on the location of the first adenine residue in the sequence of the insert DNA.

Expression and Purification of CBP Affinity-Tagged Fusion Proteins

The CBP affinity-tag system was used for expressing and purifying the JNK fusion protein from clones of the pCAL-n-EK vector containing the JNK insert ((pCAL-n-EK/JNK).). Epicurian Coli BL21(DE3) competent cells, which encode T7 RNA polymerase, were transformed with a pCAL-n-EK/JNK plasmid, and a culture was grown and induced according to a standard protocol.7 Lysates were prepared, incubated with calmodulin affinity resin, applied to a disposable column, washed with CaCl2 and eluted with 2 mM EGTA as described previously.1 Figure 3 shows the induced and uninduced sample, the calmodulin affinity resin flowthrough fraction depleted of the CBPJNK fusion protein (CBPJNK) and the fraction of pure, 52kDa, EGTAeluted CBPJNK.

Figure 3

Enterokinase Cleavage of the CBP Affinity Tag

The pCALnEK vector contains the 5-amino-acid target sequence for the site-specific protease EK to allow removal of the CBP affinity tag following purification of the fusion protein. Cleavage with EK results in recombinant proteins that contain no extraneous amino acids. Stratagene offers purified recombinant Enterokinase, which exhibits high specific activity and is free of contaminating proteases. Each order of Enterokinase is provided with Soybean Trypsin Inhibitor Agarose. (See the accompanying article in this newsletter, pages 2425, for a description of treating the purified JNK fusion protein with EK. This arti
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