Application Note: Crasp1 is suitable as a control in immunological assays. Specific conditions for reactivity should be optimized by the end user. Expect bands at 69.3 kDa for CRASP-1-MBP, (26.9 kDa for CRASP-1 and 42.4 kDa for MBP) in size corresponding to Crasp1 by Western blotting in the appropriate cell lysate or extract. Complement Regulator-Acquiring Surface Protein 1 was tested in SDS-page and western blot.
Concentration Value: 1.0 mg/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: Crasp1 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 Crasp1 and was estimated to be greater than 90% pure.
Background: CRASP-1, or Complement Regulator-Acquiring Surface Protein 1, is a multifunctional protein of Lyme disease-causing B. burgdorferi that binds to several human extracellular matrix proteins and plasminogen, including factor H (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 and may allow dissemination of B. burgdorferi in the host. B. burgdorferi spirochetes express up to 5 complement regulator-acquiring surface proteins. Multiple copies of sequences analagous to CRASP-1 genes have been detected in Borrelia plasmids. Borrelia species contain a large number of plasmids, of linear and circular, some of which appear to repeat sequences or contain fragments of other genes. These regions may serve as potentially usable information for the survival of Borrelia in its multiple environments during its life cycle. In addition, the sequence for CRASP-1 contains a repeated sequence folded into a stable stem loop structure typical of RNA genes. 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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