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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
New
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