Recombinant ASFV F317L Protein, N-His

Reference: YVV10201
Product nameRecombinant ASFV F317L Protein, N-His
Origin speciesAfrican swine fever virus
Expression systemProkaryotic expression
Molecular weight38.75 kDa
BufferLyophilized from a solution in PBS pH 7.4, 1mM EDTA, 4% Trehalose, 1% Mannitol.
FormLiquid
Delivery conditionDry Ice
Delivery lead time in business days3-5 days if in stock; 3-5 weeks if production needed
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandAntibodySystem
Host speciesEscherichia coli (E.coli)
Fragment TypeMet1-Thr317
Aliases /SynonymsF317L, African Swine Fever Virus (ASFV)
ReferenceYVV10201
NoteFor research use only.

Description of Recombinant ASFV F317L Protein, N-His

Introduction

Recombinant proteins have revolutionized the field of biotechnology and have become essential tools in various areas of research, diagnostics, and therapeutics. One such protein is the Recombinant African Swine Fever Virus (ASFV) F317L protein, which has gained significant attention in recent years due to its potential as an antigen for vaccine development against ASFV. In this article, we will discuss the structure, activity, and applications of Recombinant ASFV F317L protein.

Structure of Recombinant ASFV F317L Protein

ASFV F317L protein is a 317 amino acid-long protein encoded by the F317L gene of the African Swine Fever Virus. The protein has a molecular weight of approximately 35 kDa and is composed of three distinct domains: a transmembrane domain, a cytoplasmic domain, and an extracellular domain. The transmembrane domain anchors the protein to the viral envelope, while the cytoplasmic domain contains a conserved sequence motif that is crucial for viral replication. The extracellular domain is the largest domain and is responsible for the antigenic properties of the protein.

Activity of Recombinant ASFV F317L Protein

The main function of ASFV F317L protein in the virus is to facilitate viral entry into host cells. It acts as a receptor-binding protein, binding to specific receptors on the surface of host cells and mediating the fusion of the viral envelope with the host cell membrane. This allows the virus to enter the host cell and initiate infection. The extracellular domain of ASFV F317L protein is responsible for receptor binding, and any mutations in this domain can affect the virus’s ability to infect cells.

Application of Recombinant ASFV F317L Protein

One of the most promising applications of Recombinant ASFV F317L protein is in the development of a vaccine against ASFV. Currently, there is no effective vaccine against ASFV, and the disease has a devastating impact on the swine industry. However, studies have shown that the extracellular domain of ASFV F317L protein can elicit a strong immune response in pigs, making it a potential candidate for vaccine development.

Recombinant ASFV F317L protein can be produced in large quantities using recombinant DNA technology, making it a feasible option for vaccine production. Furthermore, the protein can be easily purified and formulated into a vaccine, making it a cost-effective solution for controlling ASFV.

Apart from its potential as a vaccine antigen, Recombinant ASFV F317L protein also has diagnostic applications. The extracellular domain of the protein can be used as a diagnostic marker for ASFV infection, as it is highly specific and can distinguish between different strains of the virus. This can aid in early detection and control of ASF outbreaks.

Conclusion

In conclusion, Recombinant ASFV F317L protein is a promising antigen for vaccine development against ASFV. Its unique structure and activity make it a potential candidate for controlling this devastating disease. Additionally, the protein has diagnostic applications, making it a valuable tool for early detection and control of ASF outbreaks. Further research and development in this area can lead to the development of an effective vaccine against ASFV, providing a solution to the ongoing threat to the swine industry.

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