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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PN1313 | Recombinant Protein-Porcine lymphotropic herpesvirus 1 Glycoprotein L (a.a.21 to 142) | Q8JYB6 | 100 µg | 1195 | |
PN1314 | Recombinant Protein-Porcine lymphotropic herpesvirus 1 Capsid protein (a.a.51 to 567) | Q8JYB9 | 100 µg | 1195 | |
PN1315 | Recombinant Protein-Porcine lymphotropic herpesvirus 1 Major capsid protein (a.a.51 to 450) | Q8JYC8 | 100 µg | 1195 | |
PN1316 | Recombinant Protein-Porcine lymphotropic herpesvirus 3 Capsid protein (a.a.51 to 450) | Q8AYV3 | 100 µg | 1195 | |
PN1317 | Recombinant Protein-Porcine lymphotropic herpesvirus 3 Glycoprotein M (a.a.33 to 382) | Q8B3Y3 | 100 µg | 1195 | |
RPN1313 | cDNA-Porcine lymphotropic herpesvirus 1 Glycoprotein L (a.a.21 to 142) | Q8JYB6 | 2 µg | 800 | |
RPN1314 | cDNA-Porcine lymphotropic herpesvirus 1 Capsid protein (a.a.51 to 567) | Q8JYB9 | 2 µg | 2580 | |
RPN1315 | cDNA-Porcine lymphotropic herpesvirus 1 Major capsid protein (a.a.51 to 450) | Q8JYC8 | 2 µg | 1995 | |
RPN1316 | cDNA-Porcine lymphotropic herpesvirus 3 Capsid protein (a.a.51 to 450) | Q8AYV3 | 2 µg | 1995 | |
RPN1317 | cDNA-Porcine lymphotropic herpesvirus 3 Glycoprotein M (a.a.33 to 382) | Q8B3Y3 | 2 µg | 1745 |
Porcine lymphotropic herpesvirus cDNA and recombinant antigen
Porcine lymphotropic herpesvirus (PLHV) is a herpesvirus that affects pigs. It is a cause of lymphoid tumors and lymphoproliferative disease in pigs. PLHV is also known as porcine herpesvirus 4 (PHV-4).
An antigen is a molecule that triggers an immune response in the body. In the case of PLHV (Porcine lymphotropic herpesvirus), specific antigens from the virus can be used to develop diagnostic tests or vaccines to detect or prevent PLHV infection in pigs. Recombinant antigens, which are produced through biotechnology techniques, can also be used to study PLHV and its effects on pigs.
The genome of Porcine lymphotropic herpesvirus (PLHV) is a linear double-stranded DNA molecule, which contains the genetic information needed for the virus to replicate and cause disease. The genome of PLHV is composed of approximately 170 kilobases and contains several genes encoding for structural and non-structural proteins that are involved in various aspects of the virus life cycle. The study of the PLHV genome provides important information on the evolution, diversity, and pathogenesis of PLHV and can contribute to the development of new diagnostic tools and therapies against PLHV infections in pigs.
Glycoprotein L (gL) is a key structural protein found in the envelope of herpesviruses. It is involved in viral entry into host cells and plays a role in cell-to-cell spread of the virus. In PLHV-1 and PLHV-3, gL has been identified as a potential target for neutralizing antibodies, which could be used in the development of vaccines or therapeutics.
Capsid protein, also known as the minor capsid protein or VP26, is a structural protein that forms the outer shell of the virus particle. This protein plays a critical role in protecting the viral genome and facilitating its transport to the host cell nucleus. In PLHV-1, capsid protein has been shown to interact with host cell proteins involved in the immune response, potentially helping the virus evade detection by the host immune system.
Major capsid protein, also known as VP5, is another structural protein that forms the capsid of the virus. This protein is involved in the assembly of the capsid and is important for viral replication and infectivity. In PLHV-1 and PLHV-3, major capsid protein has been identified as a target for antibodies that can neutralize the virus.
Glycoprotein M (gM) is a membrane-bound protein that is involved in the assembly and release of herpesvirus particles. It is also involved in the regulation of viral entry into host cells. In PLHV-1 and PLHV-3, gM has been shown to interact with other viral proteins, and may play a role in the evasion of the host immune response.
Research into these proteins and their interactions with the host immune system is ongoing, with the goal of developing effective treatments and vaccines for PLHV-1 and PLHV-3 infections 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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