Greater than 95.0% as determined by SDS-PAGE.
Recombinant Borrelia Afzelii Outer Surface Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 30kDa.
Borrelia Afzelii OspA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Recombinant Borrelia Afzelii Outer Surface Protein A, produced in E. coli, is a non-glycosylated polypeptide chain with an estimated molecular weight of 30kDa. This protein is expressed with a 6x His tag at the N-terminus and purified using proprietary chromatographic techniques.
Borrelia Afzelii OspA is provided in a buffer solution containing 20mM HEPES (pH 8.0) and 20% glycerol.
Purity exceeds 95.0%, as determined by SDS-PAGE analysis.
Borrelia afzelii is a species of spirochete bacteria that is one of the primary causative agents of Lyme borreliosis in Europe. This bacterium is transmitted to humans through the bite of infected Ixodes ticks. One of the key proteins involved in the pathogenesis and immune response to Borrelia afzelii is the Outer Surface Protein A (OspA). Recombinant forms of this protein have been extensively studied for their potential use in vaccines and diagnostic tools.
Outer Surface Protein A (OspA) is a membrane-anchored lipoprotein that plays a crucial role in the life cycle of Borrelia species. It is predominantly expressed by the bacteria while residing in the tick midgut. OspA is essential for the stable persistence of Borrelia within the tick, but its expression is downregulated when the bacteria are transmitted to the mammalian host .
The protein’s structure consists of a lipid moiety that anchors it to the bacterial membrane and a protein domain that is exposed on the surface. This exposed domain is the target of the host’s immune response and has been the focus of vaccine development efforts .
Recombinant OspA refers to the protein that has been genetically engineered and produced in a laboratory setting, typically using bacterial expression systems such as Escherichia coli. The recombinant form of OspA retains the immunogenic properties of the native protein, making it a valuable tool for research and vaccine development .
The potential of OspA as a vaccine antigen was first realized in the 1990s with the development of LYMErix™, a vaccine that was based on the OspA protein from Borrelia burgdorferi, another species of Borrelia. Although LYMErix™ was eventually withdrawn from the market, research into OspA-based vaccines has continued .
Recent studies have focused on developing multivalent vaccines that target multiple serotypes of OspA, including those from Borrelia afzelii. These efforts aim to provide broader protection against Lyme borreliosis by inducing an immune response that can neutralize various Borrelia species .