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Rabbit Anti-Borrelia burgdorferi sensu stricto (B31) CRASP-1 Antibody

$162.75$581.25 excl. VAT

Rabbit Anti-Borrelia burgdorferi CRASP-1 antibody is a polyclonal recognising Borrelia burgdorferi sensu stricto. The antibody is suitable for use in ELISA and Western blotting applications.


This is a polyclonal antibody, prepared against Complement Regulator-Acquiring Surface Protein 1 (CRASP-1, CspA) from the spirochete B. burgdorferi, for use in ELISA and western blotting applications. 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).



  • Rabbit anti-B. burgdorferi CRASP-1 polyclonal IgG antibody (strain B31).
  • Greater than 95% purity by SDS-PAGE and buffered in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2.



Native CRASP-1 is a 25.9 kDa multifunctional homodimeric protein with a previously unknown complex protein fold (Cordes, et al., 2005). CRASP-1 and four additional immune evasion proteins bind combinations of human plasma regulators, including collagen I, collagen III, collagen IV, fibronectin, laminin, factor H-like protein 1 (FHL-1) (resulting in inhibition of complement activation in mammals) and Human Bone Morphogenic Protein 2. These interactions may contribute to adhesion, bacterial colonization, and organ tropism to promote dissemination of B. burgdorferi in the host.

Borrelia species contain a large number of both linear and circular plasmids, some of which appear to be repeated or contain fragments of other genes. These regions may serve as pools of variability for the survival of Borrelia in its multiple environments during its life cycle. Multiple copies of sequences analogous to CRASP-1 genes have been detected in Borrelia plasmids. In addition, the sequence for CRASP-1 contains a repeated sequence folded into a stable stem loop structure, typical of RNA genes (Kraiczy, et al., 2004).

CRASP-1 also binds the human terminal complement components C7 and C9 and blocks assembly and membrane insertion of the terminal complement complex (TCC), as confirmed by haemolytic assays, inhibiting polymerization of C9. When CRASP-1 was expressed ectopically on the surface of serum-sensitive B. garinii, it blocked TCC assembly and induced serum resistance in the transformed bacteria. By inducing serum resistance and terminal complement pathway inhibition, B. burgdorferi is able to survive in the hostile environment of human plasma (Hallström, et al., 2010).



  • Cordes, F. S. et al., 2005. A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi. Nat Struct Mol Biol. , Volume 3, pp. 276-7.
  • Hallström, T. et al., 2010. • Complement regulator-acquiring surface protein 1 of Borrelia burgdorferi binds to human bone morphogenic protein 2, several extracellular matrix proteins, and plasminogen. J Infect Dis., 202(3), pp. 490-8.
  • Johnson, R.C., et al. 1984. Borrelia burgdorferi sp. nov.: etiologic agent of Lyme disease. Int J Syst Bacteriol, 34, pp. 496–497.
  • Kraiczy, P. et al., 2004. Complement resistance of Borrelia burgdorferi correlates with the expression of BbCRASP-1, a novel linear plasmid-encoded surface protein that interacts with human factor H and FHL-1 and is unrelated to Erp proteins. J Biol Chem. , 279(4), pp. 2421-9.

Product datasheet – PAB21447-25
Product datasheet – PAB21447-100
Safety datasheet

Western blot showing detection of 0.1µg of recombinant CRASP-1 protein. Lane 1: Molecular weight markers. Lane 2: MBP-CRASP-1 fusion protein (arrow; expected MW = 69.3 kDa). Lane 3: MBP alone. Protein was run on a 4-20% gel, then transferred to 0.45 µm nitrocellulose. After blocking with 1% BSA-TTBS overnight at 4°C, primary antibody was used at 1:1000 at room temperature for 30 min. HRP-conjugated Goat-Anti-Rabbit secondary antibody was used at 1:40,000 in HiGlo Blocking Buffer and imaged on the VersaDoc™ MP 4000 imaging system (Bio-Rad).