Borrelia burgdorferi Recombinant Crasp2 Control Protein (from E.coli)

Supplier: Rockland Immunochemical

000-001-C19
RL000-001-C19EA 470.15 USD
RL000-001-C19
Borrelia burgdorferi Recombinant Crasp2 Control Protein (from E.coli)
Proteins and Peptides

CRASP-2 (Complement Regulator-Acquiring Surface Protein 2) of Borrelia burgdorferi binds FHL-1 and factor H binding protein in a distinct way. It may be predominantly expressed by serum-resistant Borrelia strains. Borrelia burgdorferi sensu lato has the ability to evade immune systems to persist in a variety of vertebrate hosts. This activity is dependent on a number of factors. Some Borrelia species bind host-derived fluid-phase immune regulators FHL-1 and factor H to their surface via complement regulator-acquiring surface proteins (CRASPs). 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 confers resistance of spirochetes to complement-mediated lysis. It is possible that because of discontinuous binding regions in the factor H/FHL-1, long distance interaction may be involved in binding of both immune regulators. Putative coiled-coil structural elements may be important in the interaction of B. burgdorferi CRASP-1 with factor H. Lyme disease proteins are ideal for researchers interested in immunology, neurology, and rheumatology, coinfections , autoimmune, and neurodegenerative diseases.

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