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Rabbit Anti-Borrelia burgdorferi sensu stricto (B31) CRASP-2 Antibody

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产品名称: Rabbit Anti-Borrelia burgdorferi sensu stricto (B31) CRASP-2 Antibody
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简单介绍

Rabbit Anti-Borrelia burgdorferi CRASP-2 antibody is a polyclonal recognising Borrelia burgdorferi sensu stricto. The antibody is suitable for use in ELISA and Western blotting applications.


Rabbit Anti-Borrelia burgdorferi sensu stricto (B31) CRASP-2 Antibody  的详细介绍

Rabbit Anti-Borrelia burgdorferi sensu stricto (B31) CRASP-2 Antibody

 

This is a polyclonal antibody, prepared against CRASP-2 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). CRASP-2 (CSPz) is a 20/21-kDa protein which binds to FHL-1 and factor H binding protein (although it interacts preferentially with Factor H) and may be predominantly expressed by serum-resistant Borrelia strains (Rossmann, et al., 2006).

B. burgdorferi differ in their susceptibility to normal human serum and are therefore classified as complement-resistant, complement-sensitive and intermediate complement-sensitive. Complement resistant bacteria absorb human immune regulators FHL-1/reconectin and factor H using two outer surface Complement Regulator-Acquiring Surface Proteins (CRASP-1 and CRASP-2). Surface-attached FHL-1/reconectin retains its complement regulatory and cleavage activity (Kraiczy, et al., 2001). Factor H and FHL-1 serve as cofactors for factor I, a serine protease that cleaves complement component 3b (C3b) directly on the cell surface and thereby ensures resistance of spirochetes to complement-mediated lysis (Kraiczya, et al., 2007). It is possible that because of discontinuous binding regions in the factor H/FHL-1, a long-distance interaction may be involved in binding of both immune regulators. Putative coiled-coil structural elements may also be important in the interaction of B. burgdorferi CRASP-1 with factor H (Kraiczya, et al., 2007).

These proteins represent another immune evasion mechanism of B. burgdorferi, as bacteria acquire human complement regulators to control complement activation on their surface and prevent formation of toxic activation products  (Kraiczy, et al., 2001).

 

References

Johnson, R.C., et al. 1984. Borrelia burgdorferi sp. nov.: etiologic agent of Lyme disease. Int J Syst Bacteriol, 34, pp. 496–497.

Kraiczya, P. et al., 2007. Assessment of the regions within complement regulator-acquiring surface protein (CRASP)-2 of Borrelia burgdorferi required for interaction with host immune regulators FHL-1 Proceedings IX. International Jena Symposium on Tick-borne Diseases (formerly IPS). International Journal of Medical Microbiology, 298(1), pp. 268-271.

Kraiczy, P. et al., 2001. Immune evasion of Borrelia burgdorferi by acquisition of human complement regulators FHL-1/reconectin and Factor H. Eur J Immunol, 31(6), pp. 1674-84.

Rossmann, E. et al., 2006. Borrelia burgdorferi Complement Regulator-Acquiring Surface Protein 1 of the Lyme Disease spirochetes is expressed in humans and induces antibody responses restricted to nondenatured structural determinants. Infection and Immunity, 74(12), pp. 7024-7028.


Product datasheet – PAB21448-25
Product datasheet – PAB21448-100
Safety datasheet

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