Borrelia Garinii OspC
Greater than 95.0% as determined by SDS-PAGE.
Description
Recombinant Borrelia Garinii Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 22kDa.
Borrelia Garinii OspC is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Recombinantly produced in E.coli, this non-glycosylated polypeptide chain represents Borrelia Garinii Outer Surface Protein C. With a predicted molecular weight of 22kDa, this protein is expressed with a 10xHis tag at the N-terminus and purified using proprietary chromatographic methods.
The provided Borrelia Garinii OspC is prepared in a buffer solution consisting of 20mM HEPES (pH 8.0), 200mM NaCl, and 20% glycerol.
For short-term storage (up to 2-4 weeks), maintain the product at a temperature of 4°C. For extended storage, freeze the vial at -20°C. To preserve the integrity of the product, minimize repeated cycles of freezing and thawing.
Analysis by SDS-PAGE indicates a purity level exceeding 95%.
2. Exhibits reactivity in immunodot assays employing plasma samples from individuals with positive and negative Lyme disease status.
Product Science Overview
Recombinant OspC refers to the OspC protein that has been produced using recombinant DNA technology. This involves inserting the gene encoding OspC into a suitable expression system, such as Escherichia coli, to produce the protein in large quantities. The recombinant OspC protein is often fused with a tag, such as a his-tag, to facilitate purification and detection .
The recombinant OspC protein is valuable in both research and diagnostic applications. In research, it is used to study the immune response to Borrelia infection and to develop vaccines. In diagnostics, recombinant OspC is used in serological assays to detect antibodies against Borrelia in patient samples. These assays are crucial for the diagnosis of Lyme disease, as they help confirm the presence of an immune response to the infection .
The production of recombinant OspC typically involves the following steps:
- Gene Cloning: The gene encoding OspC is cloned into an expression vector.
- Transformation: The vector is introduced into a host organism, such as E. coli.
- Expression: The host organism is cultured under conditions that induce the expression of the OspC protein.
- Purification: The recombinant OspC protein is purified using techniques such as affinity chromatography, which exploits the his-tag for easy isolation .
Recombinant OspC has several applications:
- Western Blotting (WB): Used to detect specific proteins in a sample.
- Dot Blotting (DB): A technique similar to Western blotting but simpler and faster.
- Enzyme-Linked Immunosorbent Assay (ELISA): Used to detect antibodies in patient samples.
- Chemiluminescent Immunoassay (CLIA): A highly sensitive assay for detecting antibodies.
- Lateral-Flow Assays: Used in rapid diagnostic tests .
Producing recombinant proteins can present several challenges, including:
- Protein Aggregation: Recombinant proteins can aggregate, which may affect their functionality. Proper handling and storage conditions are essential to minimize aggregation.
- Purity: Ensuring the purity of the recombinant protein is crucial for its use in research and diagnostics. Techniques such as SDS-PAGE and Western blotting are used to assess purity .
In conclusion, the recombinant OspC protein of Borrelia garinii is a vital tool in the study and diagnosis of Lyme disease. Its production and purification require careful attention to detail, but the benefits it provides in understanding and detecting Borrelia infections are invaluable.
