Bacteria have a unique adaptation where they can bypass steps in the Tricarboxylic Acid (TCA) cycle to conserve carbon. The bypass is regulated by the Isocitrate Lyase Regulator (IclR) protein which works on the aceBAK operon. This bypass can be a target for antibacterial therapeutics that would not harm humans, as they do not possess the bypass. Previous researchers at Millersville prepared IclR with a C-terminal His-tag for purification, however, previous studies used IclR that did not have a tag. This study aimed to evaluate whether the Histag has an effect on the IclR protein’s ability to bind to DNA. The His-tag from purified IclR using enterokinase. Electromobility shift assay (EMSA) was then used to evaluate the binding of the IclR to aceBAK DNA with and without the His-tag at several concentrations and quantified. The His-tagged and tag-cleaved proteins had different banding patterns, especially at higher concentrations, indicating that a His-tag on the protein tends to stabilize multimerization. EMSA reactions were also performed using mutated protein where one residue, serine 147, was replaced with an alanine, as this serine is suspected to be important for multimerization. Reactions comparing His-tagged and cleaved S147A revealed a difference in binding activity as well as less overall multimerization when compared to wild type IclR.