The OmpA protein is one of the main outer-membrane proteins of a large array of gram-negative bacteria such as A. salmonicida, Shigella dysenteriae and E. coli. OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding. Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein. The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E. coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein. Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A. salmonicida bacterial cells by the glycine and the membrane extraction methods.

The Recombinant Salmonella Enteritidis Outer Membrane Protein A, is E. coli derived, with 330 amino acids, and contains the ompA immunodominant regions. The protein is fused to a His tag at C-terminal and purified by standard chromatography techniques.

Physical Appearance: Sterile Filtered clear solution.

Stability: OmpA S.Enteritidis Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

Formulation: PBS.