Application Note: DbpB protein has been tested by SDS-PAGE and Western blotting and is suitable as a control in other immunological assays. Specific conditions for reactivity should be optimized by the end user. Expect bands at 60.3 kDa for DbpB-MBP, (17.9 kDa for DbpB and 42.4 kDa for MBP) in size corresponding to DbpB by Western blotting in the appropriate cell lysate or extract.
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: DbpB is a fusion protein synthesized with an MBP tag and was expressed in E. coli. Analysis by SDS-PAGE resulted in a pattern consistent with purified DbpB and was estimated to be greater than 90% pure.
Background: Decorin-binding protein B, or DbpB, binds to decorin, which may mediate the adherence of B. burgdorferi to collagen fibers in skin and other tissues. Spirochetal surface adhesions mediate attachment to decorin, a major component of the host extracellular matrix enabling bacteria to colonize in mammalian tissues. The spirochete migrates from the tick midgut during feeding to its salivary glands and are thus transmitted to the mammal host. This transition may be facilitated by changes in expression of some B. burgdorferi genes. It is believed that expression of the various proteins associated with the spirochete may be regulated by the changes in tick life cycle, changes in conditions during tick feeding (such as temperature, pH, and nutrients) and/or in coordination with the course of infection of the mammal host. Borrelia burgdorferi can colonize multiple tissues, and is capable of attachment to diverse cell types. The expression of decorin-binding protein (Dbp) A and/or DbpB, two B. burgdorferi surface proteins that bind GAGs, is sufficient to convert a high-passage nonadherent B. burgdorferi strain into one that efficiently binds 293 epithelial cells. 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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