Aggregatib acteractinomycetemcomitans cDNA and Antigen

Aggregatib acteractinomycetemcomitans is a gram-negative bacterium that is associated with periodontitis, a severe form of gum disease. The bacterium produces several key proteins that are involved in its virulence and pathogenesis.

One of the key proteins of Aggregatib acteractinomycetemcomitans is the Cpn60 groEL protein, which is a chaperonin that is involved in the folding and assembly of other proteins in the bacterium. This protein has been shown to be immunogenic and is a potential target for the development of vaccines and therapeutics.

Another important protein of Aggregatib acteractinomycetemcomitans is the Hemoglobin binding protein A, which is involved in the bacterium’s ability to utilize hemoglobin as an iron source. This protein is also involved in the bacterium’s ability to adhere to and invade host cells.

The ORF17 protein is another key protein of Aggregatib acteractinomycetemcomitans that is involved in the bacterium’s ability to evade the host’s immune response. This protein has been shown to be highly immunogenic and is a potential target for the development of vaccines and therapeutics.

Aggregatib acteractinomycetemcomitans also produces several antigenic lipoproteins, including lipoprotein B and lipoprotein pcp, which are involved in the bacterium’s ability to interact with the host’s immune system. These proteins are potential targets for the development of diagnostic tests and vaccines.

Other important proteins of Aggregatib acteractinomycetemcomitans include the Aggregatib acteractinomycetemcomitans 100, 18-16, 26, 39, 64, A, and W proteins, which are involved in various aspects of the bacterium’s virulence and pathogenesis. The outer-membrane lipoprotein lolB is also important for the bacterium’s adhesion to host tissues.

The use of recombinant proteins and cDNA in academic research and therapeutic applications has experienced substantial growth. However, the success of heterologous expression systems largely depends on various factors, such as codon preference, RNA secondary structure, and GC content.

The Benefits of Codon Optimization:
• Increased Expression: Numerous experimental results have shown that codon optimization can dramatically increase the expression level of recombinant proteins, ranging from two to a hundred times depending on the gene.
• Proprietary Technology: Bioclone has developed 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), ready to produce recombinant proteins.
• E. coli Expression Vector: The optimized cDNA clones are cloned in E. coli, a commonly used expression system known for its efficient production of recombinant proteins.

The Importance of Optimal Expression:
• Better Research: Improved expression levels lead to better research outcomes and a better understanding of the functions of recombinant proteins.
• Therapeutic Applications: Optimal expression is crucial for the successful production of recombinant proteins for therapeutic applications, ensuring that treatments are effective and safe.
• Enhanced Productivity: By optimizing expression, researchers can maximize productivity and achieve better results in a shorter amount of time.

Bioclone’s proprietary technology platform offers a solution to the challenges faced in heterologous expression systems, unlocking the full potential of recombinant proteins. With over 6,000 artificially synthesized codon-optimized cDNA clones, researchers can enjoy increased expression levels and better research outcomes. Whether for academic research or therapeutic applications, Bioclone’s technology is a valuable tool for maximizing the production of recombinant proteins.