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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PP0254 | Recombinant Protein-Chlamydophila pecorum OmpB (a.a.31 to 178) | Q46165 | 100 µg | 1195 | |
PP0255 | Recombinant Protein-Chlamydophila pecorum Surface antigen repeat-(a.a.61 to 460) | D1A142 | 100 µg | 1195 | |
PP0256 | Recombinant Protein-Chlamydophila pecorum Major (a.a.22 to 391) | B5LMT7 | 100 µg | 1195 | |
RPP0254 | cDNA-Chlamydophila pecorum OmpB (a.a.31 to 178) | Q46165 | 2 µg | 735 | |
RPP0255 | cDNA-Chlamydophila pecorum Surface antigen repeat-(a.a.61 to 460) | D1A142 | 2 µg | 1995 | |
RPP0256 | cDNA-Chlamydophila pecorum Major (a.a.22 to 391) | B5LMT7 | 2 µg | 1845 |
Chlamydophila pecorum cDNA and recombinant antigen
Chlamydophila pecorum is an obligate intracellular bacterium that can infect a wide range of animals, including cattle, sheep, and koalas. The bacterium produces several important proteins that play key roles in its pathogenesis and immune response to infection.
Outer membrane protein B (OmpB): OmpB is a major protein that is located in the outer membrane of Chlamydophila pecorum. It plays a key role in the adhesion of the bacterium to host cells and is a major target of the host immune response.
Surface antigen repeats: Chlamydophila pecorum produces several surface antigen repeats that are thought to be involved in immune evasion and host cell adhesion. These repeats are highly variable among different strains of the bacterium and can be used as markers for strain identification.
Major proteins: Chlamydophila pecorum produces several major proteins, including the chlamydial polymorphic outer membrane proteins (Pmps) and the chlamydial heat shock protein 60 (Cpn60). These proteins are important targets of the host immune response and play a role in the pathogenesis of the infection.
Understanding the function of these proteins is important for the development of vaccines and therapeutic strategies against Chlamydophila pecorum infections. For example, OmpB is a promising vaccine candidate due to its high immunogenicity and surface exposure, while Pmps and Cpn60 are potential targets for the development of novel antibiotics.
The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E. coli expression Vector), which are ready for production of the recombinant proteins.
Chlamydophila pecorum cDNA and recombinant antigen are essential tools for the diagnosis and study of chlamydial diseases in animals. This cDNA is derived from the Chlamydophila pecorum bacterium, a species of the Chlamydiaceae family, and is used to produce recombinant antigens for the detection of Chlamydophila-associated infections. These cDNAs and recombinant antigens offer an accurate and reliable method of diagnosis and can be used to monitor the progression of the disease.
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