Outer Membrane Protein-A Bacterial Recombinant ( OmpA )
Catalog # PT_41666
$1,147.00
DescriptionThe recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 48 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated
Data sheet
- Formulation
- The OmpA protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
- Solubility
- It is recommended to reconstitute the lyophilized OmpA in sterile 0.4% NaHCO3, not less than 100ug/ml, which can then be further diluted to other aqueous solutions.
- Purity
- Greater than 98.0% as determined by:(a) Analysis by SEC-HPLC.(b) Analysis by SDS-PAGE.
- Description
- The recombinant form was found to be undistinguishable from the wild type when examined by SDS-PAGE and gel filtration chromatography yielding a 48 kDa monomeric protein. The immunological similarity of the protein samples was demonstrated by employing po
- Protein Background
- 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 morpholog
- Expression host
- Escherichia Coli.
- Synonyms
- Outer Membrane Protein-A, OmpA.
- Reagent Appearance
- Sterile Filtered White lyophilized (freeze-dried) powder.
- Stability
- 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
- Amino acid sequence
- mdvvispndn tfvttslasv tkqpvldfst aqqnltlnfs evgdlknngf ivleiqgegq fndaeirqwl sngfwrrpft gllvnpndhg nfansgevnd vrkffkiisd gtqltivhti dsngkrlrla lasdveetin fadaevelkl nlanqafklt sgsqgtvalt agalwnasyt adpvatkplf klgklfqlsl tnagkatalv segflklnig danisatdfa it
- Biological Activity
- 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 pro
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