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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PN1297 | Recombinant Protein-Porcine enteric sapovirus Protein p28 (a.a.57 to 310) | Q9QEJ5 | 100 µg | 1195 | |
PN1298 | Recombinant Protein-Porcine enteric sapovirus Protein p32 (a.a.651 to 934) | Q9QEJ5 | 100 µg | 1195 | |
PN1299 | Recombinant Protein-Porcine enteric sapovirus Capsid protein (a.a.1763 to 2254) | Q9QEJ5 | 100 µg | 1195 | |
PN1300 | Recombinant Protein-Porcine enteric sapovirus Viral genome-linked protein (a.a.935 to 1048) | Q9QEJ5 | 100 µg | 1195 | |
RPN1297 | cDNA-Porcine enteric sapovirus Protein p28 (a.a.57 to 310) | Q9QEJ5 | 2 µg | 1265 | |
RPN1298 | cDNA-Porcine enteric sapovirus Protein p32 (a.a.651 to 934) | Q9QEJ5 | 2 µg | 1415 | |
RPN1299 | cDNA-Porcine enteric sapovirus Capsid protein (a.a.1763 to 2254) | Q9QEJ5 | 2 µg | 2455 | |
RPN1300 | cDNA-Porcine enteric sapovirus Viral genome-linked protein (a.a.935 to 1048) | Q9QEJ5 | 2 µg | 800 |
Porcine enteric sapovirus cDNA and recombinant antigen
Porcine enteric sapovirus (PESV) is a type of calicivirus that infects pigs. Caliciviruses are a group of viruses that cause gastrointestinal illness in various animals and humans. PESV is a relatively new virus that was first identified in 2011, and it has been associated with outbreaks of diarrhea in pigs, particularly in Asia. The virus is spread through fecal-oral transmission, and it can cause significant economic losses in the pig industry, as it can lead to decreased growth, reduced feed efficiency, and increased death rates. Currently, there is no specific treatment for PESV, but efforts are being made to develop vaccines and improve diagnostic tests for the virus.
The porcine enteric sapovirus (PESV) antigen refers to a substance that is specifically recognized and targeted by the immune system as being foreign or harmful. Antigens are typically proteins or other molecules found on the surface of viruses and bacteria, and they trigger an immune response. In the case of PESV, the virus surface antigen can be used to develop diagnostic tests for the virus and to potentially design vaccines. By exposing the immune system to a specific antigen, it can learn to recognize and respond to the virus if it encounters it again in the future. In other words, the PESV antigen can be used to help the body build immunity against the virus.
The porcine enteric sapovirus (PESV) genome is the genetic material of the virus, which contains all the information necessary for the virus to replicate and cause disease. The PESV genome is a single-stranded RNA (ribonucleic acid) that is approximately 7.5 kilobases in length. The genome codes for multiple proteins, including the structural proteins (which form the virus shell), the enzymes (which are involved in replication), and the immune modulatory proteins (which help the virus evade the host immune response). Understanding the PESV genome is important for developing diagnostic tests, treatments, and vaccines for the virus. Studying the genome can also provide insights into the evolution and transmission of the virus.
Protein p28 and Protein p32 are two non-structural proteins found in PeSV that are involved in the replication of the viral genome.
Capsid protein is a structural protein that forms the outer shell of the virus and is responsible for protecting the viral genome.
The Viral genome-linked protein is a small protein that is covalently linked to the viral RNA and is involved in the translation and replication of the viral genome.
Understanding the roles of these various PeSV proteins is critical for developing effective treatments and vaccines against the virus. Research in this area is ongoing, with the goal of developing new approaches to prevent and treat this highly infectious disease in pigs.
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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