Surface Lipoprotein P27, Strain B31, Recombinant, Borrelia burgdorferi, MBP-Tag

Surface Liporotein P27 is encoded by the spirochete B. burgdorferi, which is carried by Ixodes ticks. Strain B31 is the type strain (ATCC 35210) for this organism and was derived by limited dilutional cloning from the original Lyme-disease tick isolate obtained by A. Barbour (Johnson, et al., 1984). Spirochetal outer surface proteins (Osps) play a major role in both protection from and pathogenesis of Lyme disease. All Osps (OspA to OspF and P27) have been shown to be lipoproteins, containing hydrophobic N-terminal domains and putative cleavage sites (Leu-X-Y-Z-Cys) thought to be recognized by a lipoprotein signal peptidase (Brandt, et al., 1990). The p27 gene is located on a linear plasmid of a size of approximately 55kb and expressed as a basic protein of 248aa with a typical prokaryotic leader sequence of 17 amino acid residues at the N-terminal of the proposed translation product, as confirmed by Northern and Western blot analysis (Reindl, et al., 1993). Borrelia spirochetes are unique among gram-negative (diderm or double-membrane) bacteria in their abundance of surface-displayed lipoproteins, some of which play important roles in the pathogenesis of Lyme disease and relapsing fever. There is evidence that Borrelia lipoproteins are specifically targeted to the bacterial surface, but that they can be retained in the periplasm by sequence-specific signals (Schulze & Zückert, 2006). Recombinant protein corresponding to Borrelia burgdorferi Surface Lipoprotein P27, strain B31, fused to MBP-Tag, expressed in E. coli. , Molecular Weight:, ~73.3kD, Storage and Stability: Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.