Crasp-2 蛋白

Application Note: Crasp2 is suitable as a control in immunological assays. Specific conditions for reactivity should be optimized by the end user. Expect bands at 67.8 kDa for CRASP-2-MBP, (25.4 kDa for CRASP-2 and 42.4 kDa for MBP) and in size corresponding to Crasp2 by Western blotting in the appropriate cell lysate or extract. Complement Regulator-Acquiring Surface Protein 2 was tested in SDS-page and western blot.

Western Blot Dilution: User Optimized

ELISA Dilution: User Optimized

Other: Lateral Flow Assay: User Optimized

Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

Stabilizer: None

Synonyms: control protein, Borrelia burgdorferi CRASP-2, CRASP2

Background: 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, rheumatology, coinfections, autoimmune, and neurodegenerative diseases.