Borrelia Bavarriensis 58
Description
Recombinant Borrelia Bavarriens 58 produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 61kDa.
Borrelia Bavarriensis 58 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Borrelia bavariensis is a species of bacteria belonging to the genus Borrelia, which is part of the spirochete phylum. This genus is known for causing borreliosis, a zoonotic, vector-borne disease transmitted primarily by ticks and, in some cases, by lice. Among the 36 known species of Borrelia, 12 are known to cause Lyme disease or borreliosis, with major species including Borrelia burgdorferi, Borrelia afzelii, Borrelia garinii, and Borrelia valaisiana .
The p58 protein is a significant antigen associated with Borrelia bavariensis. It plays a crucial role in the bacterium’s ability to infect and persist within its host. The p58 protein is often targeted in diagnostic assays and research studies due to its immunogenic properties.
Recombinant p58 protein from Borrelia bavariensis is produced using recombinant DNA technology. This involves cloning the gene encoding the p58 protein into an expression system, typically E. coli, to produce the protein in large quantities. The recombinant protein is then purified using various chromatographic techniques to ensure high purity and functionality .
- Diagnostic Assays: The recombinant p58 protein is used in ELISA (Enzyme-Linked Immunosorbent Assay) and other immunoassays to detect antibodies against Borrelia bavariensis in patient samples. This helps in the diagnosis of Lyme disease and other borreliosis-related conditions.
- Vaccine Development: Research is ongoing to explore the potential of the p58 protein as a vaccine candidate. Its immunogenic properties make it a promising target for developing vaccines to prevent Borrelia infections.
- Research Studies: The recombinant p58 protein is used in various research studies to understand the pathogenesis of Borrelia bavariensis, its interaction with the host immune system, and the development of new therapeutic strategies .
The recombinant p58 protein is typically expressed with a hexa-histidine purification tag, which facilitates its purification using nickel-affinity chromatography. The protein is stored in a buffer with neutral to slightly alkaline pH and 20% glycerol as a cryoprotective agent. It is recommended to store the protein at -70°C or below to maintain its stability and prevent degradation .
