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The N-terminal domain (1–318 amino acids) of mouse NFκB (p65) has been purified to homogeneity from the soluble fraction of Escherichia coli cells expressing this protein. Its complex with a full-length iκB-α (MAD3, 1–317 amino acids) molecule was generated by binding the E. coli-derived iκB-α to the purified NFκB and purifying the complex by sequential chromatography. The stoichiometry of NFκB to...
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