Ancylostoma duodenale is a parasitic hookworm that infects humans and is a leading cause of anemia and malnutrition in developing countries. The parasite has developed several strategies to survive in the host and establish a successful infection. These strategies include the production of several proteins, such as secreted protein 1, ASP-2, and Anticoagulant peptide 4.

Secreted protein 1 is a protein that is secreted by Ancylostoma duodenale and has been shown to have immunomodulatory effects on the host, inhibiting the host’s immune response and allowing the parasite to establish infection. ASP-2, another protein produced by the parasite, is involved in host tissue invasion and has been shown to induce antibody responses in the host. Anticoagulant peptide 4 is a protein that inhibits blood clotting in the host, allowing the parasite to feed on blood without interference.

The study of Ancylostoma duodenale and its associated proteins is important for understanding the mechanisms behind the parasite’s virulence and for developing new treatments and prevention strategies. The parasite is a major public health concern in many parts of the world, and efforts to control its spread and reduce its impact on human health are ongoing.

Recent research has focused on the use of vaccines and other immunotherapies to prevent and treat hookworm infections, and several promising candidates have been identified, including ASP-2. Further research on the biology of Ancylostoma duodenale and its associated proteins is critical for the development of effective strategies to control this important human parasite.

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.