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MABE8

Sigma-Aldrich

Anti-EBNA2 Antibody, clone R3

clone R3, from rat

Synonym(s):

Epstein-Barr nuclear antigen 2

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rat

Quality Level

100

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

R3, monoclonal

species reactivity

human

technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG2aκ

NCBI accession no.

YP_001129441

UniProt accession no.

Q69022

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

Epstein-Barr virus ... Ebna-2(3783761)

General description

Gross, H., et al. (2010). Virology. 397(2): 299-310.
PMID: 19969318
Kremmer, E., et al. (1995). Virology. 208(1): 336-342.
PMID: 11831716
The Epstein-Barr virus or EBV is associated with several human cancers and actively immortalizes B lymphocytes. EBV is leads to expression by a small group of viral proteins, including Epstein-Barr nuclear antigen 2 (EBNA2) which is required for immortalization. EBNA2 is a transcriptional activator belonging to the herpesviridae EBNA2 family, and performs a crucial role in activating the host resting B-cell and inducing B-cell proliferation. EBNA2 possesses an acidic activating domain with which it is able to recruit various cellular and viral involved in B-cell immortalization. Implicated in cellular phenotypic modifications, EBNA2 is known to upregulate the expression of cell surface receptors, such as CD21, MYC, and CD23, as well as upregulating viral genes such as LMP1, LMP2A, LMP2B, and EBNA1-6.

Specificity

Demonstrated to react with human cell infected with EBV.

Immunogen

Epitope: C-terminus of EBNA2
GST-tagged recombinant protein corresponding to human EBNA2.

Application

Anti-EBNA2 Antibody, clone R3 is a Rat Monoclonal Antibody for detection of EBNA2 also known as Epstein-Barr nuclear antigen 2 & has been validated in WB, IP & IHC.
Immunoprecipitation Analysis: A representative lot was used by an independent laboratory in IP. (Gross, H., et al. (2010). Virology. 397(2):299-310.)

Immunohistochemistry Analysis: A representative lot was used by an independent laboratory in IH. (Kremmer, E., et al. (1995). Virology. 208(1):336-342.)
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Transcription Factors

Quality

Evaluated by Western Blot in B95-8 cell lysate.

Western Blot Analysis: 0.5 µg/mL of this antibody detected EBNA2 on 10 µg of B95-8 cell lysate.

Target description

~ 75 kDa observed; Although the calculated molecular weight is 49 kDa, this protein is typically observed at ~ 75-80 kDa

Physical form

Format: Purified
Protein G
Purified rat monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Control
B95-8 cell lysate

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Matthew R Harter et al.
PLoS pathogens, 12(2), e1005414-e1005414 (2016-02-06)
Epstein-Barr virus (EBV) nuclear antigen 2 (EBNA2) plays an important role in driving immortalization of EBV-infected B cells through regulating the expression of many viral and cellular genes. We report a structural study of the tumor suppressor BS69/ZMYND11 C-terminal region
Qiu Peng et al.
Journal of virology, 94(7) (2020-01-17)
Biological macromolecule condensates formed by liquid-liquid phase separation (LLPS) have been discovered in recent years to be prevalent in biology. These condensates are involved in diverse processes, including the regulation of gene expression. LLPS of proteins have been found in
Xiang Zheng et al.
Immunity, inflammation and disease, 9(2), 351-362 (2021-01-13)
N6 -methyladenosine (m6 A) is the most prevalent modification that occurs in messenger RNA (mRNA), affecting mRNA splicing, translation, and stability. This modification is reversible, and its related biological functions are mediated by "writers," "erasers," and "readers." The field of
Fang Lu et al.
Journal of virology, 95(13), e0008821-e0008821 (2021-04-23)
Epstein-Barr virus (EBV) is a human gammaherpesvirus that is causally associated with various lymphomas and carcinomas. Although EBV is not typically associated with multiple myeloma (MM), it can be found in some B-cell lines derived from MM patients. Here, we
Wei-Hang Huang et al.
Heliyon, 9(11), e21486-e21486 (2023-11-29)
Originally extracted from Momordica charantia seeds, the antiviral and anti-tumor activities of Momordica anti-HIV protein MAP30 have become well known. Although MAP30 has been reported to possess antiviral activity against several human viruses, the current understanding of the MAP30-mediated antiviral
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