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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PP0471 | Recombinant Protein-Leptospira borgpetersenii Cpn60 groEL protein (a.a.61 to 546) | Q04S01 | 100 µg | 1195 | |
PP0472 | Recombinant Protein-Leptospira borgpetersenii Surface Antigen OrfC lipoprotein (a.a.34 to 446) | Q04QA2 | 100 µg | 1195 | |
RPP0471 | cDNA-Leptospira borgpetersenii Cpn60 groEL protein (a.a.61 to 546) | Q04S01 | 2 µg | 2425 | |
RPP0472 | cDNA-Leptospira borgpetersenii Surface Antigen OrfC lipoprotein (a.a.34 to 446) | Q04QA2 | 2 µg | 2060 |
Leptospira borgpetersenii cDNA and recombinant antigen
Leptospira borgpetersenii is a pathogenic spirochete that causes leptospirosis, a zoonotic disease that affects both humans and animals. Two key proteins of L. borgpetersenii, Cpn60 groEL and Surface Antigen OrfC lipoprotein, have been identified and studied for their roles in the pathogenicity of this bacterium.
Cpn60 groEL is a chaperonin protein that is involved in protein folding and stability. It has been identified in L. borgpetersenii and is believed to be involved in the survival and replication of the bacterium within the host. This protein is also a potential target for diagnosis and treatment of leptospirosis, as it has been shown to elicit a strong immune response in infected hosts.
Surface Antigen OrfC lipoprotein is a surface-exposed lipoprotein that is believed to play a role in adhesion and invasion of host cells by L. borgpetersenii. This protein has also been identified as a potential target for diagnosis and treatment of leptospirosis, as it is highly conserved across different Leptospira species and is immunogenic in infected hosts.
Understanding the roles and functions of these key proteins can aid in the development of novel therapies and vaccines for leptospirosis caused by L. borgpetersenii. Further research is needed to fully understand the mechanisms of action of these proteins and their potential as targets for diagnosis and treatment of leptospirosis.
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.
The application of cDNA (complementary DNA) and recombinant antigens derived from L. borgpetersenii has been of significant interest for the development of diagnostic and vaccine tools for the control of leptospirosis.
Diagnostics: cDNA from L. borgpetersenii can be used to develop molecular diagnostic tools such as PCR (Polymerase Chain Reaction) assays for the rapid and specific detection of the bacterium in infected animals. This is especially useful in cases where traditional culture methods are not feasible or are slow.
Vaccine development: Recombinant antigens of L. borgpetersenii can be used as potential vaccine candidates to protect against leptospirosis in animals. Recombinant antigens have shown to provide protective immunity against challenge with the wild-type L. borgpetersenii strain in preclinical trials.
Serotyping: The recombinant antigens can also be used for serotyping of L. borgpetersenii isolates, which is important for understanding the diversity of the bacterium and for the development of new vaccines.
Overall, the application of cDNA and recombinant antigens of L. borgpetersenii has the potential to contribute to the control and prevention of leptospirosis in animals, which will benefit the veterinary and livestock industries by reducing the economic losses associated with the disease.
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