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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PN1349 | Recombinant Protein-Pseudorabies virus Ea Glycoprotein M (a.a.42 to 393) | Q9DL74 | 100 µg | 1195 | |
PN1350 | Recombinant Protein-Pseudorabies virus Ea Glycoprotein I (a.a.35 to 366) | Q99F67 | 100 µg | 1195 | |
RPN1349 | cDNA-Pseudorabies virus Ea Glycoprotein M (a.a.42 to 393) | Q9DL74 | 2 µg | 1755 | |
RPN1350 | cDNA-Pseudorabies virus Ea Glycoprotein I (a.a.35 to 366) | Q99F67 | 2 µg | 1655 |
Pseudorabies virus cDNA and recombinant antigen
Pseudorabies virus (PRV), also known as Aujeszky’s disease virus, is a highly contagious virus that affects a wide range of animals, including swine, cattle, dogs, and cats. This virus is characterized by its Ea glycoprotein M and Ea glycoprotein I, which play critical roles in viral replication and pathogenesis.
The Ea glycoprotein M is a type III transmembrane protein that is involved in the formation and budding of viral particles. It is also important in the maturation and stability of virions. Furthermore, the glycoprotein M of PRV has been shown to play a role in the modulation of the host’s immune response.
The Ea glycoprotein I is a type I transmembrane protein that is involved in viral entry into host cells. It mediates the attachment of the virus to host cells and is responsible for the fusion of the virus with the host cell membrane. It is also involved in the evasion of the host’s immune response by modulating several host proteins and suppressing the production of cytokines.
PRV infections can cause significant morbidity and mortality in susceptible animals and can have a significant economic impact on the agricultural industry. Ongoing research is focused on understanding the roles of these glycoproteins in viral pathogenesis and host immune response and developing effective treatments and prevention strategies for PRV 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.
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