Borrelia Bavariensis DbpA
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| Amount : | 20 µg |
| Purification : | Greater than 80.0% as determined by SDS-PAGE. |
| Content : | Borrelia Bavariensis DbpA is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol. |
| Storage condition : | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles. |
| Alternative Name : | Decorin binding protein A, dbpA. |
Source: Escherichia Coli.
Sterile Filtered clear solution.
Borrelia is a part of a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Borreliella bavariensis is one of the pathogens of the Borreliella burgdorferi sensu lato complex which causes Lyme disease. Decorin binding protein A (DbpA), also known as Osp17 or p17 is expressed during the mammalian phase of infection. Â DbpA is binds the pathogen to host collagen-associated proteoglycan decorin.
Recombinant Borrelia Bavariensis DbpA produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 18kDa. Borrelia Bavariensis DbpA is expressed with a 10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Sterile Filtered clear solution.
Borrelia is a part of a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Borreliella bavariensis is one of the pathogens of the Borreliella burgdorferi sensu lato complex which causes Lyme disease. Decorin binding protein A (DbpA), also known as Osp17 or p17 is expressed during the mammalian phase of infection. Â DbpA is binds the pathogen to host collagen-associated proteoglycan decorin.
Recombinant Borrelia Bavariensis DbpA produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 18kDa. Borrelia Bavariensis DbpA is expressed with a 10x His tag at N-terminus and purified by proprietary chromatographic techniques.
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