• Screen for antibacterial drugs targeting FtsZ
• Determine IC50 and EC50 values for FtsZ targeting lead compounds
• Biochemical characterization of S. aureus FtsZ functionality

FtsZ is a highly conserved bacterial cytoskeletal protein that polymerizes to form a contractile ring at the future site of cell division, playing a pivotal role in cytokinesis. Its dynamic assembly and GTPase activity make it a key target for studying bacterial cell cycle regulation and developing novel antimicrobial agents.

Escherichia coli FtsZ protein is produced in a bacterial expression system;

• Protein tag: C-terminal His tag for purification
• Molecular weight: ~42 kDa
• Formulation: supplied as a lyophilized powder
• Composition: when resuspended to 5 mg/ml the buffer composition is; 10 mM Hepes-KOH pH 7.5, 50 mM KCl, 10µM GDP, 5% (w/v) sucrose, 1% (w/v) dextran.

Protein purity is assessed by scanning densitometry of Coomassie Blue stained protein on a 4-20% polyacrylamide gel. Purity was determined to be ≥90% pure.

The biological activity of FTZ05 is determined by the ability of the protein to polymerize into protofilaments and sheets in vitro in the presence of Mg2+ and GTP. Under the experimental conditions (see datasheet) GTP-dependent E. coli FtsZ polymerization achieves a 65% polymer mass, in agreement with the critical concentration of FtsZ under the experimental conditions.