Borrelia NapA
Greater than 95.0% as determined by SDS-PAGE.
Description
Recombinant Borrelia Burgdorferi NapA produced in E.coli is a non-glycosylated, full-length polypeptide chain having a calculated molecular mass of 21 kDa. Borrelia NapA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Borrelia burgdorferi is a spirochete bacterium responsible for Lyme disease, a tick-borne illness prevalent in the Northern Hemisphere. One of the critical proteins associated with Borrelia burgdorferi is the Neutrophil Activating Protein A (NapA). This protein plays a significant role in the bacterium’s ability to evade the host immune system and establish infection. The recombinant form of this protein, produced through genetic engineering techniques, is used in various research and diagnostic applications.
The discovery of Borrelia burgdorferi dates back to the 1980s when it was identified as the causative agent of Lyme disease. Since then, extensive research has been conducted to understand its pathogenic mechanisms. NapA was identified as a key virulence factor due to its ability to activate neutrophils, a type of white blood cell crucial for the immune response .
NapA is a non-glycosylated, full-length polypeptide chain with a calculated molecular mass of approximately 22,094 Daltons. It is expressed with a 6x His tag at the N-terminus and purified using proprietary chromatographic techniques . Structurally, NapA is similar to ferritins, forming a dodecameric hollow sphere that can bind and store iron .
Functionally, NapA plays a pivotal role in the immune response by promoting the recruitment of neutrophils and T lymphocytes to the site of infection. It achieves this by inducing the production of pro-inflammatory cytokines and chemokines, which attract immune cells to the infected area . This recruitment is essential for controlling the infection but also contributes to the inflammation observed in Lyme disease.
Recombinant NapA is produced in Escherichia coli (E. coli) expression systems. The recombinant protein is typically supplied in a sterile filtered clear solution, formulated in 20mM HEPES buffer (pH 7.6), 250mM NaCl, and 20% glycerol . The purity of the recombinant protein is greater than 80%, as determined by SDS-PAGE analysis .
Recombinant NapA is used extensively in research to study the pathogenesis of Lyme disease and the immune response to Borrelia burgdorferi infection. It is also employed in the development of diagnostic assays for Lyme disease, as its presence can be indicative of infection. Additionally, understanding the role of NapA in immune activation can aid in the development of new therapeutic strategies to modulate the immune response and reduce inflammation in Lyme disease patients .
