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AB138345

Recombinant EBV Nuclear Antigen/EBNA1 protein

5

(1 Review)

|

(9 Publications)

Recombinant EBV Nuclear Antigen/EBNA1 protein is a Epstein-Barr Virus (Strain B95-8) Full Length protein, in the 1 to 640 aa range with >95% purity and suitable for western blot, SDS-PAGE and ELISA.The predicted molecular weight of ab138345 protein is 63 kDa.

- Save time and ensure accurate results- use our EBV Nuclear Antigen/EBNA1 protein as a control

View Alternative Names

BKRF1, EBNA1, Epstein-Barr nuclear antigen 1, EBNA-1, EBV nuclear antigen 1

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

ELISA, SDS-PAGE, WB

applications

Biologically active

No

Accession

P03211

Animal free

No

Carrier free

No

Species

Epstein-Barr Virus (Strain B95-8)

Storage buffer

Constituents: Phosphate Buffer, 36% Urea, 5.8% Sodium chloride, 0.1% Poly(oxy-1,2-ethanediyl), .alpha.-tridecyl-.omega.-hydroxy-

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"0.5 µg/mL", "notes":"<p></p>" } } }
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Product details

Ensure the validity of your results using our Recombinant EBV Nuclear Antigen/EBNA1 protein ab138345 as a positive control in western blot and SDS-PAGE. Analyze your EBV EBNA-1 ELISA data using the ab138345 protein to generate and plot a standard curve.

Check out of western blot protocol for more information here

Check out our protein gel staining guide for SDS-PAGE here

Check out our ELISA protocol for more information here.
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Sequence info

[{"sequence":"SDEGPGTGPGNGLGEKGDTSGPEGSGGSGPQRRGGDNHGRGRGRGRGRGGGRPGAPGGSGSGPRHRDGVRRPQKRPSCIGCKGTHGGTGAGAGAGGAGAGGAGAGGGAGAGGGAGGAGGAGGAGAGGGAGAGGGAGGAGGAGAGGGAGAGGGAGGAGAGGGAGGAGGAGAGGGAGAGGGAGGAGAGGGAGGAGGAGAGGGAGAGGAGGAGGAGAGGAGAGGGAGGAGGAGAGGAGAGGAGAGGAGAGGAGGAGAGGAGGAGAGGAGGAGAGGGAGGAGAGGGAGGAGAGGAGGAGAGGAGGAGAGGAGGAGAGGGAGAGGAGAGGGGRGRGGSGGRGRGGSGGRGRGGSGGRRGRGRERARGGSRERARGRGRGRGEKRPRSPSSQSSSSGSPPRRPPPGRRPFFHPVGEADYFEYHQEGGPDGEPDVPPGAIEQGPADDPGEGPSTGPRGQGDGGRRKKGGWFGKHRGQGGSNPKFENIAEGLRALLARSHVERTTDEGTWVAGVFVYGGSKTSLYNLRRGTALAIPQCRLTPLSRLPFGMAPGPGPQPGPLRESIVCYFMVFLQTHIFAEVLKDAIKDLVMTKPAPTCNIRVTVCSFDDGVDLPPWFPPMVEGAAAEGDDGDDGDEGGDGDEGEEGQE","proteinLength":"Full Length","predictedMolecularWeight":"63 kDa","actualMolecularWeight":null,"aminoAcidEnd":640,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P03211","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

EBV Nuclear Antigen 1 (EBNA1) is a protein expressed by the Epstein-Barr Virus (EBV) also known as Human Herpesvirus 4. It has a molecular weight of approximately 80 kDa and shows expression in latently infected cells. EBNA1 acts as a viral episome-maintenance protein that binds to the EBV genome ensuring viral DNA replication and partitioning during cell division. This protein facilitates the persistent infection of EBV in host cells. Occasionally it is also referred to as EBV EBNA or EBNA-1 protein.
Biological function summary

EBNA1 functions as an EBV-specific DNA-binding protein essential for maintaining the viral episome within infected cells. EBNA1 plays a role in gene regulation by interacting with specific DNA sequences called oriP to assist in the replication and maintenance of the viral DNA. It does not form part of a larger protein complex but strongly influences cellular processes through these interactions. EBNA1 ensures the survival and propagation of the virus without immediate cytopathic effects contributing to its long-term persistence.

Pathways

EBNA1 is central to viral latency and replication pathways in host cells. EBNA1 influences both the EBV lytic and latent cycles maintaining the latency by stabilizing the viral episome within the nucleus of host cells and regulating viral gene expression. It interacts with cellular proteins like USP7 a deubiquitinase important for the regulation of EBNA1 stability and function. These pathways highlight EBNA1's role in the balance between viral latency and active replication.

EBNA1 is closely associated with several EBV-related cancers such as Burkitt's lymphoma and nasopharyngeal carcinoma. The persistent expression of EBNA1 contributes to oncogenic processes by disrupting normal cellular control mechanisms. EBNA1's interaction with p53 a tumor suppressor protein can interfere with the host's cell-cycle regulation and apoptosis allowing for malignant transformation. These interactions illustrate EBNA1's significant role in the pathogenesis of disorders linked to EBV infection.
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Specifications

Form

Liquid

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General info

Function

Responsible for the origin of replication (oriP) dependent replication and maintenance of viral episomes during latent infection (PubMed : 15479791, PubMed : 2996781). EBNA1 dimer interacts with the DS (dyad symmetry) element within the origin of replication oriP and with a host mitotic chromosome to initiate viral DNA replication during latency (PubMed : 24067969, PubMed : 2996781, PubMed : 31142669, PubMed : 8551585). EBNA1 binding to DS recruits the host origin recognition complex (ORC) (PubMed : 12953058). Governs the faithful mitotic segregation of the viral episomes by binding both the FR (family of repeats) element within oriP and the host mitotic chromosomes (PubMed : 11172042, PubMed : 15479791, PubMed : 24067969). Forms a cell cycle-dependent tyrosine-dependent DNA cross-link and single-strand cleavage at oriP required for terminating replication and maintaining viral episomes (PubMed : 33482082). Counteracts the stabilization of host p53/TP53 by host USP7, thereby decreasing apoptosis and increasing host cell survival (PubMed : 15808506). Induces degradation of host PML through the ubiquitin-proteasome system, which promotes lytic reactivation and may impair the host cell DNA repair (PubMed : 18833293). Increases the association of CK2 with PML proteins which increases the phosphorylation of PML proteins by CK2, triggering the polyubiquitylation and degradation of PML (PubMed : 20719947). Displays inhibitory effects on a SUMO2-modified complex that includes STUB1, KAP1 and USP7 (PubMed : 32176739). This inhibitory effect possibly participates to the maintenance of latency linked to PML silencing (PubMed : 32176739).

Sequence similarities

Belongs to the herpesviridae EBNA1 family.

Post-translational modifications

Phosphorylation at Ser-385 increases the nuclear import efficiency of EBNA1.. Phosphorylation at Ser-393 is required for interaction with CSNK2B.

Subcellular localisation

Host nucleus

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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Responsible for the origin of replication (oriP) dependent replication and maintenance of viral episomes during latent infection (PubMed : 15479791, PubMed : 2996781). EBNA1 dimer interacts with the DS (dyad symmetry) element within the origin of replication oriP and with a host mitotic chromosome to initiate viral DNA replication during latency (PubMed : 24067969, PubMed : 2996781, PubMed : 31142669, PubMed : 8551585). EBNA1 binding to DS recruits the host origin recognition complex (ORC) (PubMed : 12953058). Governs the faithful mitotic segregation of the viral episomes by binding both the FR (family of repeats) element within oriP and the host mitotic chromosomes (PubMed : 11172042, PubMed : 15479791, PubMed : 24067969). Forms a cell cycle-dependent tyrosine-dependent DNA cross-link and single-strand cleavage at oriP required for terminating replication and maintaining viral episomes (PubMed : 33482082). Counteracts the stabilization of host p53/TP53 by host USP7, thereby decreasing apoptosis and increasing host cell survival (PubMed : 15808506). Induces degradation of host PML through the ubiquitin-proteasome system, which promotes lytic reactivation and may impair the host cell DNA repair (PubMed : 18833293). Increases the association of CK2 with PML proteins which increases the phosphorylation of PML proteins by CK2, triggering the polyubiquitylation and degradation of PML (PubMed : 20719947). Displays inhibitory effects on a SUMO2-modified complex that includes STUB1, KAP1 and USP7 (PubMed : 32176739). This inhibitory effect possibly participates to the maintenance of latency linked to PML silencing (PubMed : 32176739).
See full target information EBNA1
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Publications (9)

Recent publications for all applications. Explore the full list and refine your search

Genome medicine 17:65 PubMed40457459

2025

Associations between HLA-II variation and antibody specificity are predicted by antigen properties.

Applications

Unspecified application

Species

Unspecified reactive species

Gabriel Innocenti,Sergio Andreu-Sánchez,Nicolai V Hörstke,Hesham Elabd,Iros Barozzi,Andre Franke,Máté Manczinger,Thomas Vogl

iScience 26:107575 PubMed37622005

2023

Preservation of whole antibodies within ancient teeth.

Applications

Unspecified application

Species

Unspecified reactive species

Barry Shaw,Thomas McDonnell,Elizabeth Radley,Brian Thomas,Lynn Smith,Carol A L Davenport,Silvia Gonzalez,Anisur Rahman,Rob Layfield

mBio 12:e0224321 PubMed34781735

2021

The Epstein-Barr Virus Oncogene EBNA1 Suppresses Natural Killer Cell Responses and Apoptosis Early after Infection of Peripheral B Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Danielle Westhoff Smith,Adityarup Chakravorty,Mitch Hayes,Wolfgang Hammerschmidt,Bill Sugden

Clinical & translational immunology 10:e1312 PubMed34295471

2021

Systematic evaluation of SARS-CoV-2 antigens enables a highly specific and sensitive multiplex serological COVID-19 assay.

Applications

Unspecified application

Species

Unspecified reactive species

Sophia Hober,Cecilia Hellström,Jennie Olofsson,Eni Andersson,Sofia Bergström,August Jernbom Falk,Shaghayegh Bayati,Sara Mravinacova,Ronald Sjöberg,Jamil Yousef,Lovisa Skoglund,Sara Kanje,Anna Berling,Anne-Sophie Svensson,Gabriella Jensen,Henric Enstedt,Delaram Afshari,Lan Lan Xu,Martin Zwahlen,Kalle von Feilitzen,Leo Hanke,Ben Murrell,Gerald McInerney,Gunilla B Karlsson Hedestam,Christofer Lendel,Robert G Roth,Ingmar Skoog,Elisabet Svenungsson,Tomas Olsson,Anna Fogdell-Hahn,Ylva Lindroth,Maria Lundgren,Kimia T Maleki,Nina Lagerqvist,Jonas Klingström,Rui Da Silva Rodrigues,Sandra Muschiol,Gordana Bogdanovic,Laila Sara Arroyo Mühr,Carina Eklund,Camilla Lagheden,Joakim Dillner,Åsa Sivertsson,Sebastian Havervall,Charlotte Thålin,Hanna Tegel,Elisa Pin,Anna Månberg,My Hedhammar,Peter Nilsson

Nature communications 12:3695 PubMed34140485

2021

Multianalyte serology in home-sampled blood enables an unbiased assessment of the immune response against SARS-CoV-2.

Applications

Unspecified application

Species

Unspecified reactive species

Niclas Roxhed,Annika Bendes,Matilda Dale,Cecilia Mattsson,Leo Hanke,Tea Dodig-Crnković,Murray Christian,Birthe Meineke,Simon Elsässer,Juni Andréll,Sebastian Havervall,Charlotte Thålin,Carina Eklund,Joakim Dillner,Olof Beck,Cecilia E Thomas,Gerald McInerney,Mun-Gwan Hong,Ben Murrell,Claudia Fredolini,Jochen M Schwenk

Proceedings of the National Academy of Sciences of : PubMed31822610

2019

Reactivation of Epstein-Barr virus by a dual-responsive fluorescent EBNA1-targeting agent with Zn-chelating function.

Applications

Unspecified application

Species

Unspecified reactive species

Lijun Jiang,Hong Lok Lung,Tao Huang,Rongfeng Lan,Shuai Zha,Lai Sheung Chan,Waygen Thor,Tik-Hung Tsoi,Ho-Fai Chau,Cecilia Boreström,Steven L Cobb,Sai Wah Tsao,Zhao-Xiang Bian,Ga-Lai Law,Wing-Tak Wong,William Chi-Shing Tai,Wai Yin Chau,Yujun Du,Lucas Hao Xi Tang,Alan Kwok Shing Chiang,Jaap M Middeldorp,Kwok-Wai Lo,Nai Ki Mak,Nicholas J Long,Ka-Leung Wong

Methods in molecular biology (Clifton, N.J.) 2044:303-318 PubMed31432421

2019

Array-Based Profiling of Proteins and Autoantibody Repertoires in CSF.

Applications

Unspecified application

Species

Unspecified reactive species

Elisa Pin,Ronald Sjöberg,Eni Andersson,Cecilia Hellström,Jennie Olofsson,August Jernbom Falk,Sofia Bergström,Julia Remnestål,David Just,Peter Nilsson,Anna Månberg

Autoimmunity 52:1-11 PubMed30835561

2019

Individual and stable autoantibody repertoires in healthy individuals.

Applications

Unspecified application

Species

Unspecified reactive species

Maja Neiman,Cecilia Hellström,David Just,Cecilia Mattsson,Linn Fagerberg,Ina Schuppe-Koistinen,Anders Gummesson,Göran Bergström,Olli Kallioniemi,Adnane Achour,Riitta Sallinen,Mathias Uhlén,Peter Nilsson

Lung cancer (Amsterdam, Netherlands) 125:157-163 PubMed30429015

2018

Detection of autoantibodies against cancer-testis antigens in non-small cell lung cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Dijana Djureinovic,Tea Dodig-Crnković,Cecilia Hellström,Georg Holgersson,Michael Bergqvist,Johanna S M Mattsson,Fredrik Pontén,Elisabeth Ståhle,Jochen M Schwenk,Patrick Micke
View all publications
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Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions
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