Recombinant EEEV Spike glycoprotein E2 Protein, N-His

Reference: YVV34401
Product nameRecombinant EEEV Spike glycoprotein E2 Protein, N-His
Origin speciesEastern equine encephalitis virus (EEEV) (Eastern equine encephalomyelitis virus)
Expression systemProkaryotic expression
Molecular weight42.72 kDa
BufferLyophilized from a solution in PBS pH 7.4, 0.02% NLS, 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 TypeAsp323-Arg681
Aliases /SynonymsStructural polyprotein, p130, Capsid protein, 3.4.21.90, Coat protein, C, Precursor of protein E3/E2, p62, pE2, Assembly protein E3, Spike glycoprotein E2, E2 envelope glycoprotein, 6K protein, Spike glycoprotein E1, E1 envelope glycoprotein
ReferenceYVV34401
NoteFor research use only.

Description of Recombinant EEEV Spike glycoprotein E2 Protein, N-His

Recombinant EEEV Spike Glycoprotein E2 Protein, N-His: Structure, Activity, and Applications

Overview of Eastern Equine Encephalitis Virus (EEEV)

Eastern Equine Encephalitis Virus (EEEV) is a highly pathogenic mosquito-borne virus that causes severe encephalitis in humans and horses. The virus poses a significant threat to public health due to its high fatality rate and the lack of effective therapeutic options. EEEV is primarily transmitted through the bite of infected mosquitoes, leading to a rapid onset of neurological symptoms in those affected. Understanding and targeting the viral components responsible for infection is critical in the development of effective treatments.

Structure of EEEV Spike Glycoprotein E2

The E2 glycoprotein is a vital component of the EEEV virion, playing a crucial role in the virus’s ability to infect host cells. E2 is part of the viral envelope and works closely with the E1 glycoprotein to facilitate the virus’s attachment and entry into the host cell. Structurally, E2 is responsible for binding to host cell receptors, a key step that triggers the subsequent fusion of the viral and cellular membranes mediated by E1. The E2 protein’s surface-exposed domains make it an ideal target for neutralizing antibodies and antiviral therapies.

Recombinant EEEV Spike Glycoprotein E2 Protein, N-His: Structure and Characteristics

The Recombinant EEEV Spike Glycoprotein E2 Protein, N-His is produced using recombinant DNA technology, allowing for the generation of a highly purified and consistent protein product. This recombinant E2 protein includes an N-terminal His-tag, which facilitates its purification and detection in experimental applications. The protein retains the essential structural and functional features of the native E2 glycoprotein, including the receptor-binding domains. The N-His tag is a versatile tool that allows for easy affinity purification and detection in assays, making the recombinant protein highly useful in various research settings.

Activity of Recombinant EEEV Spike Glycoprotein E2 Protein

The primary function of the Recombinant EEEV Spike Glycoprotein E2 Protein, N-His is to mimic the activity of the native E2 protein, particularly in binding to host cell receptors. This recombinant protein can be used to study the molecular interactions between EEEV and host cells, providing insights into the mechanisms of viral entry. Additionally, it serves as a crucial tool for screening potential antiviral compounds that can block E2-mediated entry, thereby preventing infection. The N-His tag allows for straightforward incorporation into binding assays, ELISA, and other experimental setups where detection and quantification are required.

Applications of Recombinant EEEV Spike Glycoprotein E2 Protein, N-His

Research Applications: The Recombinant EEEV Spike Glycoprotein E2 Protein, N-His is extensively used in research to study the pathogenesis of Eastern Equine Encephalitis. Researchers can utilize this protein to investigate the receptor-binding properties of EEEV, screen for neutralizing antibodies, and identify inhibitors that block E2’s interaction with host cell receptors. Its role in understanding the virus-host interaction is crucial for developing effective therapeutic strategies. Diagnostic Applications: This recombinant E2 protein can also be employed in diagnostic assays to detect the presence of EEEV-specific antibodies in patient samples. By coating ELISA plates with the Recombinant EEEV Spike Glycoprotein E2 Protein, N-His, it is possible to develop sensitive and specific assays for serological testing, aiding in the diagnosis and monitoring of EEEV infections. Therapeutic Potential: The E2 glycoprotein is an attractive therapeutic target due to its essential role in viral entry. The recombinant EEEV Spike Glycoprotein E2 Protein, N-His is being explored in the development of vaccines and antiviral therapies. By eliciting an immune response against E2, it is possible to prevent EEEV infection or reduce its severity. Furthermore, compounds identified through screening efforts that target E2 could lead to the development of new antiviral drugs.

Conclusion

The Recombinant EEEV Spike Glycoprotein E2 Protein, N-His is a valuable tool in the study and treatment of Eastern Equine Encephalitis Virus. Its use in research, diagnostics, and therapeutic development highlights the importance of targeting the E2 glycoprotein in the fight against this deadly virus. As research progresses, the insights gained from studying this recombinant protein will be instrumental in developing effective interventions to combat EEEV.

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