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.
Concentration Value: 1.0mg/mL
ELISA Dilution: User Optimized
Western Blot Dilution: User Optimized
General Disclaimer Note: This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 5199, Limerick, Pennsylvania, USA.
Physical State: Liquid (sterile filtered)
Purity and Specificity: Crasp2 is a fusion protein with an MBP tag and was expressed in E. coli. Analysis by SDS-PAGE resulted in a pattern consistent with purified Crasp2 and was estimated to be greater than 90% pure.
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.
Low Endotoxin: No
Other: Lateral Flow Assay: User Optimized
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