Lysine residues of bovine serum albumin (BSA) have been chemically acetylated by acetic anhydride under basic conditions. A major Ac-BSA band runs at approximately 66 KDa and Ac-BSA oligos run at approximately 120-260 KDa. NOTE: Ac-BSA oligomerization is not caused by the acetylation reaction as these species are also present in unmodified BSA as seen in a Coomassie stain of unmodified BSA protein. Acetylated BSA is supplied as a lyophilized powder.
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