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Cat# | Product Name | Swiss Prot# | Size | Price (US$) | Order |
PN0143 | Recombinant Protein-Bovine viral diarrhea virus E2 protein (a.a.31 to 110) | A8VM12 | 100 µg | 1195 | |
PN0144 | Recombinant Protein-Bovine viral diarrhea virus Structural glycoprotein E0 (a.a.21 to 245) | O10644 | 100 µg | 1195 | |
PN0145 | Recombinant Protein-Bovine viral diarrhea virus Structural glycoprotein E2 (a.a.31 to 405) | O10645 | 100 µg | 1195 | |
PN0146 | Recombinant Protein-Bovine viral diarrhea virus Glycoprotein E2 (a.a.21 to 140) | Q9JEW5 | 100 µg | 1195 | |
PN0147 | Recombinant Protein-Bovine viral diarrhea virus Envelope protein (a.a.31 to 314) | Q9PZB3 | 100 µg | 1195 | |
PN0148 | Recombinant Protein-Bovine viral diarrhea virus P20 protein (a.a.21 to 168) | Q02632 | 100 µg | 1195 | |
PN0149 | Recombinant Protein-Bovine viral diarrhea virus Surface glycoprotein (a.a.26 to 388) | Q65809 | 100 µg | 1195 | |
PN0150 | Recombinant Protein-Bovine viral diarrhea virus N-terminal protease (a.a.21 to 168) | P19711 | 100 µg | 1195 | |
PN0151 | Recombinant Protein-Bovine viral diarrhea virus Capsid protein C (a.a.169 to 270) | P19711 | 100 µg | 1195 | |
PN0152 | Recombinant Protein-Bovine viral diarrhea virus E glycoprotein (a.a.305 to 497) | P19711 | 100 µg | 1195 | |
PN0153 | Recombinant Protein-Bovine viral diarrhea virus Envelope glycoprotein E1 (a.a.515 to 659) | P19711 | 100 µg | 1195 | |
PN0154 | Recombinant Protein-Bovine viral diarrhea virus Non-structural protein 4B (a.a.2427 to 2773) | P19711 | 100 µg | 1195 | |
PN0155 | Recombinant Protein-Bovine viral diarrhea virus Non-structural protein 5A (a.a.2808 to 3269) | P19711 | 100 µg | 1195 | |
PN0156 | Recombinant Protein-Bovine viral diarrhea virus Capsid protein C (a.a.169 to 270) | P19711 | 100 µg | 1195 | |
PN0157 | Recombinant Protein-Bovine viral diarrhea virus E glycoprotein (a.a.271 to 497) | P19711 | 100 µg | 1195 | |
PN0158 | Recombinant Protein-Bovine viral diarrhea virus Envelope glycoprotein E1 (a.a.498 to 659) | P19711 | 100 µg | 1195 | |
PN0159 | Recombinant Protein-Bovine viral diarrhea virus Envelope glycoprotein E2 (a.a.660 to 1066) | P19711 | 100 µg | 1195 | |
PN0160 | Recombinant Protein-Bovine viral diarrhea virus Non-structural protein 4B (a.a.2427 to 2773) | P19711 | 100 µg | 1195 | |
PN0161 | Recombinant Protein-Bovine viral diarrhea virus Non-structural protein 5A (a.a.2774 to 3269) | P19711 | 100 µg | 1195 | |
RPN0143 | cDNA-Bovine viral diarrhea virus E2 protein (a.a.31 to 110) | A8VM12 | 2 µg | 800 | |
RPN0144 | cDNA-Bovine viral diarrhea virus Structural glycoprotein E0 (a.a.21 to 245) | O10644 | 2 µg | 1120 | |
RPN0145 | cDNA-Bovine viral diarrhea virus Structural glycoprotein E2 (a.a.31 to 405) | O10645 | 2 µg | 1870 | |
RPN0146 | cDNA-Bovine viral diarrhea virus Glycoprotein E2 (a.a.21 to 140) | Q9JEW5 | 2 µg | 800 | |
RPN0147 | cDNA-Bovine viral diarrhea virus Envelope protein (a.a.31 to 314) | Q9PZB3 | 2 µg | 1415 | |
RPN0148 | cDNA-Bovine viral diarrhea virus P20 protein (a.a.21 to 168) | Q02632 | 2 µg | 800 | |
RPN0149 | cDNA-Bovine viral diarrhea virus Surface glycoprotein (a.a.26 to 388) | Q65809 | 2 µg | 1810 | |
RPN0150 | cDNA-Bovine viral diarrhea virus N-terminal protease (a.a.21 to 168) | P19711 | 2 µg | 735 | |
RPN0151 | cDNA-Bovine viral diarrhea virus Capsid protein C (a.a.169 to 270) | P19711 | 2 µg | 800 | |
RPN0152 | cDNA-Bovine viral diarrhea virus E glycoprotein (a.a.305 to 497) | P19711 | 2 µg | 960 | |
RPN0153 | cDNA-Bovine viral diarrhea virus Envelope glycoprotein E1 (a.a.515 to 659) | P19711 | 2 µg | 720 | |
RPN0154 | cDNA-Bovine viral diarrhea virus Non-structural protein 4B (a.a.2427 to 2773) | P19711 | 2 µg | 1730 | |
RPN0155 | cDNA-Bovine viral diarrhea virus Non-structural protein 5A (a.a.2808 to 3269) | P19711 | 2 µg | 2305 | |
RPN0156 | cDNA-Bovine viral diarrhea virus Capsid protein C (a.a.169 to 270) | P19711 | 2 µg | 505 | |
RPN0157 | cDNA-Bovine viral diarrhea virus E glycoprotein (a.a.271 to 497) | P19711 | 2 µg | 1130 | |
RPN0158 | cDNA-Bovine viral diarrhea virus Envelope glycoprotein E1 (a.a.498 to 659) | P19711 | 2 µg | 805 | |
RPN0159 | cDNA-Bovine viral diarrhea virus Envelope glycoprotein E2 (a.a.660 to 1066) | P19711 | 2 µg | 2030 | |
RPN0160 | cDNA-Bovine viral diarrhea virus Non-structural protein 4B (a.a.2427 to 2773) | P19711 | 2 µg | 1730 | |
RPN0161 | cDNA-Bovine viral diarrhea virus Non-structural protein 5A (a.a.2774 to 3269) | P19711 | 2 µg | 2475 |
Bovine viral diarrhea virus cDNA and recombinant antigen
Bovine viral diarrhea virus (BVDV) is a highly contagious virus that affects cattle worldwide. It causes a range of clinical signs, including fever, decreased appetite, weight loss, and reproductive disorders in infected animals. BVDV is primarily spread through direct contact with infected animals or contaminated equipment and environments and can also be transmitted via vertical transmission from infected dams to their offspring. BVDV infection can have a significant impact on the health and productivity of infected herds, and control measures include vaccination, biosecurity practices, and culling of persistently infected animals.
The BVDV Genome
The bovine viral diarrhea virus (BVDV) genome refers to the complete genetic material of the virus. BVDV is a positive-sense single-stranded RNA virus and has a genome size of approximately 12 kilobases. The BVDV genome encodes for at least two major structural proteins and several non-structural proteins that are involved in viral replication and pathogenesis. Analysis of the BVDV genome has provided important insights into the molecular biology and evolution of the virus and has facilitated the development of improved diagnostic tools and vaccines for controlling BVDV infection.
BVDV Antigen
Bovine viral diarrhea virus (BVDV) antigen refers to any substance that is recognized and specifically reacted with by the immune system of an animal, usually from a vaccine, to produce an immune response. In the context of BVDV, the antigen is typically a protein or viral particle that is used in a vaccine to stimulate the production of antibodies that protect against BVDV infection. The use of a BVDV antigen in a vaccine helps to reduce the incidence of BVDV-associated diseases and improve the health and productivity of infected cattle.
Proteins of BVDV
The virus has several proteins, including the E2 protein, structural glycoprotein E0, structural glycoprotein E2, glycoprotein E2, envelope protein, P20, surface glycoprotein, N-terminal protease, capsid protein C, E glycoprotein, envelope glycoprotein E1, non-structural protein 4B, non-structural protein 5A, and envelope glycoprotein E2.
E2 Protein
The E2 protein is a viral protein that is involved in the attachment of the virus to host cells, as well as in the formation of the virus particle.
Structural Glycoprotein E0
The structural glycoprotein E0 is involved in the formation and assembly of the virus particle.
Structural Glycoprotein E2
The structural glycoprotein E2 is involved in the formation of the outer layer of the virus particle and is a target for the host immune response to the virus.
Envelope Protein
The envelope protein is important for the stability and infectivity of the virus and is a target for the host immune response.
P20 Protein
The P20 protein is involved in the processing and maturation of the E2 protein.
Surface Glycoprotein
The surface glycoprotein is involved in the attachment of the virus to host cells.
N-Terminal Protease
The N-terminal protease is involved in the cleavage and processing of the viral polyprotein.
Capsid Protein C
The capsid protein C forms the inner layer of the virus particle and is involved in the assembly and stabilization of the virus.
E Glycoprotein
The E glycoprotein is involved in the formation of the virus envelope.
Envelope Glycoprotein E1
The envelope glycoprotein E1 is involved in the fusion of the viral and host cell membranes during viral entry.
The non-structural protein 4B
The non-structural protein 4B is involved in the replication and transcription of the viral RNA.
Non-structural protein 5A
The non-structural protein 5A is involved in the regulation of viral gene expression and in the suppression of the host immune response to the virus.
The comprehension of the distinctive proteins found in BVDV, and their corresponding functions is of significant value for research and designing prevention and treatment methods against infections that affect cattle. Scientists have developed vaccines that aim to target specific proteins found in BVDV, thereby aiding in the prevention of the virus in cattle. Additionally, antiviral drugs that are tailored to treat BVDV infections are being created.
The utilization of recombinant proteins/cDNA in academic research and therapeutic applications has experienced an unprecedented increase. Nonetheless, in heterologous expression systems, the triumph of generating recombinant protein expression is reliant on various factors, including the preference for codons, the secondary structure of RNA, and GC content. The experimental outcomes have illustrated that there has been a significant rise in expression levels ranging from two to a hundred times, relative to pre-optimization. The research organization, Bioclone, has formulated a unique technology platform that has resulted in the fabrication of over 6,000 artificially synthesized codon-optimized cDNA clones, cloned in E. coli expression Vector, that are primed for production of the recombinant proteins.
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