Rabies virus cDNA and Antigen

Rabies virus is a highly lethal virus that affects mammals, including humans, causing significant morbidity and mortality. The virus has several important proteins that are critical for its replication and pathogenesis.

The glycoprotein of Rabies virus is a key protein that is responsible for virus entry into host cells and is also the main target of virus-neutralizing antibodies. The nucleoprotein of the virus is involved in viral replication and is also an important target for host immune responses.

The matrix protein of Rabies virus is a structural protein that plays a key role in virus assembly and is important for the stability of the viral particle. The matrix protein glycoprotein G is another important protein that is involved in virus entry into host cells and is also a target for virus-neutralizing antibodies.

Rabies is a serious disease that can be fatal if left untreated. The most effective way to prevent rabies is through vaccination, and there are also treatments available to help prevent the onset of the disease after exposure to the virus.

Ongoing research is focused on understanding the roles of these proteins in the replication and pathogenesis of the virus and developing effective treatments and prevention strategies for rabies. By studying these proteins and their interactions, researchers hope to gain a better understanding of how the virus works and how it can be effectively targeted to prevent or treat infections.

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.