Recombinant EBV Nuclear Antigen/EBNA1 Protein

Name: Recombinant EBV Nuclear Antigen/EBNA1 Protein
Brand: Beta LifeScience
SKU: BLA-11514P
Availability: InStock

Collections: Featured viral antigens molecules, Other viral antigens, Recombinant proteins, Viral antigen

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Product Overview

Accession	P03211
Synonym	EBNA1 EBV nuclear antigen 1 Epstein Barr nuclear antigen 1 Epstein Barr virus HHV4 Human Herpesvirus 4
Description	Recombinant EBV Nuclear Antigen/EBNA1 Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MSDEGPGTGP GNGLGEKGDT SGPEGSGGSG PQRRGGDNHG RGRGRGRGRG GGRPGAPGGS GSGPRHRDGV RRPQKRPSCI GCKGTHGGTG AGAGAGGAGA GGAGAGGGAG AGGGAGGAGG AGGAGAGGGA GAGGGAGGAG GAGAGGGAGA GGGAGGAGAG GGAGGAGGAG AGGGAGAGGG AGGAGAGGGA GGAGGAGAGG GAGAGGAGGA GGAGAGGAGA GGGAGGAGGA GAGGAGAGGA GAGGAGAGGA GGAGAGGAGG AGAGGAGGAG AGGGAGGAGA GGGAGGAGAG GAGGAGAGGA GGAGAGGAGG AGAGGGAGAG GAGAGGGGRG RGGSGGRGRG GSGGRGRGGS GGRRGRGRER ARGGSRERAR GRGRGRGEKR PRSPSSQSSS SGSPPRRPPP GRRPFFHPVG EADYFEYHQEGGPDGEPDVP PGAIEQGPAD DPGEGPSTGP RGQGDGGRRK KGGWFGKHRG QGGSNPKFEN IAEGLRALLA RSHVERTTDE GTWVAGVFVY GGSKTSLYNL RRGTALAIPQ CRLTPLSRLP FGMAPGPGPQ PGPLRESIVC YFMVFLQTHI FAEVLKDAIK DLVMTKPAPT CNIRVTVCSF DDGVDLPPWF PPMVEGAAAE GDDGDDGDEG GDGDEGEEGQ E
Molecular Weight	63 kDa including tags
Purity	>95% SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function	Plays an essential role in replication and partitioning of viral genomic DNA during latent viral infection. During this phase, the circular double-stranded viral DNA undergoes replication once per cell cycle and is efficiently partitioned to the daughter cells. EBNA1 activates the initiation of viral DNA replication through binding to specific sites in the viral latent origin of replication, oriP. Additionally, it governs the segregation of viral episomes by mediating their attachment to host cell metaphase chromosomes. Also activates the transcription of several viral latency genes. Finally, it can counteract the stabilization of host p53/TP53 by host USP7, thereby decreasing apoptosis and increasing host cell survival.
Subcellular Location	Host nucleus.
Protein Families	Herpesviridae EBNA1 family
Database References	KEGG: vg:3783774

Gene Functions References

Endemic variants of EBNA1 play a significant role in EBV-driven carcinogenesis by altering key regulatory interactions that destabilize latent infection. PMID: 28077791
Epstein-Barr Virus EBNA1 bound to host genes of high significance for B-cell growth and function, including MEF2B, IL6R, and EBF1. PMID: 26468528
both LANA1 and EBNA1 undergo highly efficient +1/-2 programmed ribosomal frameshifting to generate previously undescribed alternative reading frame (ARF) proteins in their repeat regions. PMID: 25271323
Epstein-Barr virus EBNA1 protein regulates viral latency through effects on let-7 microRNA and dicer. PMID: 25031339
EBNA-1 miRNA targets human casp3 expression to inhibit apoptosis. PMID: 23503461
These results support the idea that the chromosome binding of EBNA1 is mediated by electrostatic interactions between the basic amino acids within the chromosome binding domains and negatively charged cellular chromatin. PMID: 23836915
There is no association between EBNA1 titers and multiple sclerosis in Indian populations. PMID: 23312038
EBNA1 is not naturally released from Epstein-Barr virus-infected cells as a source of antigen for CD4(+) T cell priming. PMID: 23569328
EBNA1 repeat mRNA sequence, not the encoded protein sequence, underlies immune evasion in this class of virus suggests a novel approach to therapeutic development through the use of anti-sense strategies or small molecules targeting EBNA1 mRNA structure. PMID: 23300450
EBNA1 binds specifically to many sites in the human genome and may regulate some cellular genes in infected cells. [review] PMID: 23325328
These findings highlight a previously unrecognized property of the interaction of EBNA1 with cellular chromatin that may fine-tune its function in the maintenance of viral latency. PMID: 23348225
EBNA1 may reset cellular transcription during infection and prime the infected cells for malignant transformation. PMID: 23358825
Data show that purified Epstein-Barr nuclear antigen 1 EBNA1 recruits purified Human Orc1 and Cdc6 onto replication origin oriP. PMID: 22589552
These results provide the first function for EBNA1 in lytic infection and show that EBNA1 interactions with PML IV lead to a loss of PML nuclear bodies (NBs) that promotes lytic infection. PMID: 22491455
Studies indicate that that EBNA1 is a very important protein for the development and/or progression of nasopharyngeal carcinoma. PMID: 22206863
Although the depletion of HMGB2 partly altered EBNA-1 association with chromatin in HeLa cells during interphase and mitosis, it did not significantly impact the maintenance of EBV episomes in Raji cells. PMID: 22345443
These findings support the hypothesis that Epstein-Barr virus EBNA1 initiates transcription at the C promoter via interactions between multiple EBNA1 homodimers and cellular transcription such as E2F1, ARID3A and Oct-2. PMID: 22302879
Report Epstein-Barr virus nuclear antigen-1 B-cell epitopes in multiple sclerosis twins. PMID: 21757535
PML disruption by EBNA1 is one mechanism by which EBV contribute to the development of gastric cancer. PMID: 22013060
EBNA1 of Epstein-Barr virus modulated cellular oxidative stress responses and promoted metastasis. PMID: 22013061
The pathogenesis of multiple sclerosis may involve intrathecal Epstein-Barr virus nuclear antigen-1 (EBNA-1) specific T cells susceptible to modulation by vitamin D. PMID: 22018702
These results provide evidence that EBNA1 is a new target for the transcription factor HSF1. PMID: 22018489
expression of EBNA1 induced telomere abnormalities including loss or gain of telomere signals, telomere fusion and heterogeneous length of telomeres PMID: 21394098
antibodies to the EBNA-1 protein cross-react with dsDNA PMID: 21245919
These data indicate that roscovitine effects are serine 393 specific and that serine 393 is important in EBNA1- and oriPCp-dependent transcription and episome persistence. PMID: 21209116
Epstein Barr virus-encoded EBNA1 interference with MHC class I antigen presentation reveals a close correlation between mRNA translation initiation and antigen presentation. PMID: 20976201
These results suggest that EBV encoded EBNA1 can contribute to the oncogenic process by up-regulating the apoptosis suppressor protein, survivin in EBV-associated B-lymphoma cells. PMID: 21093004
Findings reveal that RNA polymerase III-dependent EBER expression through induction of cellular transcription factors and add to the repertoire of EBNA1's transcription-regulatory properties. PMID: 20843307
EBNA1 can interact with a large number of cellular genes and chromosomal loci in latently infected cells, but that these sites are likely to represent a complex ensemble of direct and indirect EBNA1 binding sites. PMID: 20929547
an interaction between EBNA1 and the host CK2 kinase is crucial for EBNA1 to disrupt PML bodies and degrade PML proteins. PMID: 20719947
EBNA-1 may directly influence the transcription of a subset of genes PMID: 20706582
40 novel regions are identified in the human genome, constituted of tandemly repeated binding sites for EBNA1. PMID: 20655080
EBV infection with EBNA1 expression in gastric carcinomas provides advantages for host cell survival, growth ability and transformation potential involving escape from immunosurveillance PMID: 19956844
effect of EBNA1 on cellular gene expression by microarray analysis using the B cell BJAB and the epithelial 293 cell lines transfected with EBNA1 PMID: 20080792
findings suggest amino-terminal 379Lys-Arg380 is essential for EBNA-1 NLS & Ser385 phosphorylation up-regulates nuclear transport efficiency of EBNA-1 by increasing its binding affinity to NPI-1, while phosphorylation of Ser386 & Ser383 down-regulates it PMID: 16439554
The partitioning of EBNA1 molecules onto sister chromatids during cellular DNA replication underlies the non-stochastic segregation of extrachromosomally replicating viral genomes. PMID: 17405814
EBNA1 apparently disables TGF-beta signaling, which subsequently decreases transcription of the PTPRK tumor suppressor PMID: 17720884
The mechanism by which EBNA-1 represses Qp promoter through binding downstream of the transcription start site and the role of this autoregulatory function in EBV latency were addressed. PMID: 18077719
targeting EBNA1 to human DEC-205 receptor, in the presence of the DC maturation stimulus poly(I:C), expanded EBNA1-specific CD4 and CD8 memory T cells; these lymphocytes control the outgrowth of autologous EBV-infected B cells PMID: 18519810
low-level expression of p27 protein may partially attribute to latent EBV infection in extranodal nasal-type NK cell lymphoma involving EBNA1 PMID: 18769118
EBNA1-NT may act as a repressor of the HER2/neu oncogene PMID: 18805633
Epstein-Barr virus nuclear antigen-1 promotes genomic instability via induction of reactive oxygen species PMID: 19139406
EBNA1 regulates oriP replication by impeding the migration of replication forks, and upon binding the family of repeats it blocks the migration of transcription forks. PMID: 19265546
Phosphorylation-deficient mutant reduced its ability to activate transcription. PMID: 19439552
These findings suggest that the EBNA1 replication and maintenance function uses a common G-quadruplex binding capacity of LR1 and LR2. PMID: 19656898
USP7 can stimulate EBNA1-DNA interactions and EBNA1 can alter histone modification at oriP through recruitment of USP7. PMID: 19834552

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.