Name: Recombinant Bacterial Outer Membrane Protein-A
Price: Inquiry

- Overview
  - 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. OmpAs 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.
    
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- Properties
  - Protein Name
    
    Outer Membrane Protein-A, OmpA.
    
    Source
    
    E. coli
    
    Type
    
    Recombinant Proteins
    
    Purification
    
    Greater than 98.0% as determined by: (a) Analysis by SEC-HPLC. (b) Analysis by SDS-PAGE.
    
    Storage
    
    Lyophilized Bacterial Outer Membrane Protein-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon C between 2-7 days and for future use reconstituted OmpA should be stored at 4 below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please avoid freeze-thaw cycles.
    
    * For Research Use Only. Not for use in diagnostic/therapeutics procedures.
- Applications
  - Application Description
    
    It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100μg/ml, which can then be further diluted to other aqueous solutions. The interaction of bacterial and recombinant A-layer protein with murine macrophages was directed at determining the effect of A-protein on intracellular events that occur in primed macrophages. This was accomplished by measuring the cytotoxic product produced by peritoneal macrophages when exposed to A-protein coated latex beads. Thioglycolate elicited macrophages exhibited a low level of activation (18% cytotoxicity) that was significantly increased (48% cytotoxicity) in the presence of latex beads. Coating of the latex beads with each of the three A-protein products resulted in an increase of cytoxicity (mean +/- SEM) from 48% to 91%.

Recombinant Bacterial Outer Membrane Protein-A

Recombinant Bacterial Outer Membrane Protein-A

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