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.
Applications:Suitable for use in ELISA and Western Blot.
Other applications not tested.
Recommended Dilution:ELISA: 1:2000Western Blot: 1:1000Optimal dilutions to be determined by the researcher.
Storage and Stability:Lyophilized powder may be stored at -20°C.
Stable for 12 months at -20°C.
Reconstitute with sterile dH2O or PBS.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Reconstituted product is stable for 12 months at -20°C.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Further dilutions can be made in assay buffer.
仕様
Size：100ug
Host：rabbit
Grade：Affinity Purified
Purity：Purified by Protein A affinity chromatography.
Form：Supplied as a lyophilized powder in 0.02M potassium phosphate, 0.15M sodium chloride, pH 7.2, 0.01% sodium azide. Reconstitute with sterile dH2O or PBS.
