Greater than 95.0% as determined by SDS-PAGE.
Recombinant Borrelia Burgdorferi p66 produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 66kDa. Borrelia p66 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Borrelia p66 is provided in a solution containing 20mM HEPES buffer (pH 7.5), 0.01mM EDTA, and 0.02% SDS.
The purity of the product is determined to be greater than 95.0% based on SDS-PAGE analysis.
The P66 protein is a bifunctional protein that serves as both an integrin ligand and a porin. As an integrin ligand, P66 binds to β1- and β3-chain integrins on host cells, facilitating the bacterium’s adhesion and invasion into host tissues . This interaction is essential for the bacterium’s ability to disseminate from the initial site of infection to other parts of the body, including the heart, joints, and nervous system .
As a porin, P66 forms channels in the bacterial outer membrane, allowing the passage of small molecules and ions. This function is critical for maintaining the bacterium’s homeostasis and nutrient acquisition .
The interaction between P66 and host integrins plays a significant role in the pathogenesis of Lyme disease. By binding to integrins, P66 can modulate the host immune response, aiding the bacterium in evading immune detection and establishing a persistent infection . This interaction also facilitates the bacterium’s ability to cross the blood-brain barrier and invade the central nervous system, contributing to the neurological manifestations of Lyme disease .
Recombinant P66 refers to the P66 protein that has been produced using recombinant DNA technology. This involves cloning the gene encoding P66 into an expression vector, which is then introduced into a host organism (such as E. coli) to produce the protein in large quantities. Recombinant P66 is used in various research applications, including studies on the protein’s structure and function, as well as in the development of diagnostic tools and potential vaccines for Lyme disease .
Research on P66 has provided valuable insights into the mechanisms of Borrelia burgdorferi infection and pathogenesis. Studies have identified specific amino acid domains of P66 that are important for its localization, oligomerization, and porin function . Understanding these domains can help in the design of targeted therapies and vaccines.
Additionally, recombinant P66 is used in immunological studies to investigate the host immune response to Borrelia burgdorferi infection. This research is crucial for developing more effective diagnostic tests and treatments for Lyme disease .