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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant EBV/HHV4 EBNA1/BKRF1 Protein, N-His |
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Origin species | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
Expression system | Prokaryotic expression |
Molecular weight | 17.52 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°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) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | His468-Pro607 |
Aliases /Synonyms | Epstein-Barr nuclear antigen 1, EBNA-1, EBV nuclear antigen 1, EBNA1, BKRF1 |
Reference | ARO-P11538 |
Note | For research use only. |
The Epstein-Barr virus (EBV), also known as human herpesvirus 4 (HHV4), is a common virus that infects over 90% of the world’s population. It is associated with various diseases, including infectious mononucleosis and several types of cancers. One of the key proteins of EBV is EBNA1, which plays a crucial role in the virus’s life cycle and pathogenesis. In this article, we will explore the structure, activity, and application of recombinant EBV/HHV4 EBNA1/BKRF1 protein, a key antigen in the development of vaccines and diagnostic tools.
EBNA1 is a nuclear protein that is expressed during the latent phase of EBV infection. It is a highly conserved protein, with a molecular weight of approximately 85 kilodaltons. The recombinant form of EBV/HHV4 EBNA1 protein is produced by cloning the gene encoding EBNA1 into an expression vector and expressing it in a suitable host, such as bacteria or yeast. The resulting protein is then purified using various techniques, such as chromatography, to obtain a highly pure and active form of the protein.
The crystal structure of EBNA1 has been determined, revealing that it consists of two domains: the N-terminal domain and the C-terminal domain. The N-terminal domain is responsible for the DNA-binding activity of EBNA1, while the C-terminal domain is involved in protein-protein interactions. The recombinant form of EBNA1 retains these structural features and is able to perform its functions in a similar manner to the native protein.
EBNA1 is a multifunctional protein that is essential for EBV’s survival and persistence in the host. It has various activities, including DNA-binding, transcriptional regulation, and protein-protein interactions. One of its key functions is to maintain the viral genome in the host cells during the latent phase of infection. EBNA1 binds to specific sequences in the viral genome, known as the oriP, and ensures that the viral DNA is replicated and segregated during cell division.
In addition to its role in viral replication, EBNA1 also plays a crucial role in regulating the expression of other viral genes. It interacts with various cellular proteins and modulates their activity to promote the expression of viral genes and suppress the host’s immune response. This activity is crucial for EBV’s ability to establish and maintain a latent infection in the host.
The recombinant form of EBV/HHV4 EBNA1 protein has various applications in the development of vaccines and diagnostic tools. Due to its ability to induce a strong immune response, EBNA1 is a potential candidate for the development of a vaccine against EBV. Recombinant EBNA1 protein can be used to stimulate the production of antibodies and T cells that can target and eliminate EBV-infected cells.
In addition to its use in vaccine development, recombinant EBNA1 protein is also used in the development of diagnostic tools for EBV infection. Antibodies against EBNA1 can be used to detect the presence of the virus in patient samples, making it a valuable tool for diagnosing EBV-associated diseases.
In summary, recombinant EBV/HHV4 EBNA1/BKRF1 protein is a key antigen in the development of vaccines and diagnostic tools for EBV. Its structure and activity have been extensively studied, and its potential applications in the prevention and diagnosis of EBV-associated diseases are promising. Further research and development of
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