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AB59028

Anti-EBV LMP2A antibody [15F9]

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(13 Publications)

Rat Monoclonal LMP2 antibody. Suitable for WB, IHC-P and reacts with Epstein-Barr virus samples. Cited in 13 publications.

View Alternative Names

Latent membrane protein 2, Terminal protein, LMP2

Key facts

Host species

Rat

Clonality

Monoclonal

Clone number

15F9

Isotype

IgG1

Carrier free

No

Reacts with

Epstein-Barr virus

Applications

WB, IHC-P

applications

Specificity

ab59028 recognises LMP2A and does not cross react with LMP2B.

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Epstein-Barr virus": { "WB-species-checked": "guaranteed", "WB-species-dilution-info": "1/100 - 1/1000", "WB-species-notes": "<p></p>", "IHCP-species-checked": "guaranteed", "IHCP-species-dilution-info": "", "IHCP-species-notes": "<p></p>" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant.
Storage buffer
pH: 7.4 Preservative: 0.09% Sodium azide Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
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Supplementary information

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

The Epstein-Barr virus latent membrane protein 2A (EBV LMP2A) mechanically functions as an important player in viral latency and persistence. Known alternatively as LMP2A it is an integral membrane protein with a molecular mass of approximately 40 kDa. LMP2A is expressed in latently infected B cells and epithelial cells. This protein does not have significant expression in normal cells outside these conditions but is essential for EBV-infected cells remaining undetected by the immune system.
Biological function summary

LMP2A functions to modulate cellular signaling pathways that mirror those of normal antigen receptor pathways. Unlike other proteins it contains multiple immune-tyrosine activation motifs (ITAMs) which enable it to mimic B-cell receptor (BCR) signaling. Through this mechanism LMP2A disrupts normal cellular functions like signal transduction and can influence cellular proliferation and survival. LMP2A acts independently and lacks association with significant protein complexes operating instead on its membrane-spanning multi-domain structure.

Pathways

LMP2A is significant in modulating both PI3K/Akt and Ras/ERK signaling pathways. These pathways are vital for cell survival and proliferation contributing to the virus's ability to maintain a latent state within host cells. LMP2A influences these pathways by interacting with proteins such as Src family kinases and phosphatidylinositol 3-kinase (PI3K) altering cellular responses that typically control growth. By linking to these pathways LMP2A undermines typical apoptotic processes providing a survival advantage to infected cells.

LMP2A has a clear connection to various EBV-associated malignancies. Two significant conditions associated with LMP2A are Hodgkin's lymphoma and nasopharyngeal carcinoma. In these diseases LMP2A contributes to oncogenic processes by its continued activation of survival pathways. It interacts with cellular proteins like Lyn and Syk further promoting malignancy by driving aberrant cell division and survival. As such targeting LMP2A may offer therapeutic potential in managing these EBV-related cancers.
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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

Isoform LMP2A. Maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin-negative cells to colonize peripheral lymphoid organs (By similarity).. Isoform LMP2B. May be a negative regulator of isoform LMP2A.
See full target information LMP2
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Publications (13)

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

PLoS pathogens 21:e1013092 PubMed40367275

2025

Epstein-Barr virus latent membrane protein 1 subverts IMPDH pathways to drive B-cell oncometabolism.

Applications

Unspecified application

Species

Unspecified reactive species

Eric M Burton,Davide Maestri,Shaowen White,Jin-Hua Liang,Bidisha Mitra,John M Asara,Benjamin E Gewurz

Journal of medical virology 95:e28387 PubMed36478267

2022

Establishment and characterization of two Epstein-Barr virus-positive gastric cancer cell lines with epitheliotropic M81 strain undergoing distinct viral and altered cellular expression profiles.

Applications

Unspecified application

Species

Unspecified reactive species

Mingqian Xu,Liang Zhang,Jinfu Feng,Shuaibing Yang,Yixuan Wang,Yuyi Wang,Meiyang Chen,Li Zhou,Junjie Zhang,Qingsong Qin

Microbiology spectrum 11:e0089822 PubMed36475746

2022

Epstein-Barr Virus Regulates Endothelin-1 Expression through the ERK/FOXO1 Pathway in EBV-Associated Gastric Cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Wen Liu,Qianqian Zhang,Yan Zhang,Lingling Sun,Hua Xiao,Bing Luo

Cell metabolism 34:1280-1297.e9 PubMed36070681

2022

Methionine metabolism controls the B cell EBV epigenome and viral latency.

Applications

Unspecified application

Species

Unspecified reactive species

Rui Guo,Jin Hua Liang,Yuchen Zhang,Michael Lutchenkov,Zhixuan Li,Yin Wang,Vicenta Trujillo-Alonso,Rishi Puri,Lisa Giulino-Roth,Benjamin E Gewurz

Nature microbiology 5:1051-1063 PubMed32424339

2020

DNA methylation enzymes and PRC1 restrict B-cell Epstein-Barr virus oncoprotein expression.

Applications

Unspecified application

Species

Unspecified reactive species

Rui Guo,Yuchen Zhang,Mingxiang Teng,Chang Jiang,Molly Schineller,Bo Zhao,John G Doench,Richard J O'Reilly,Ethel Cesarman,Lisa Giulino-Roth,Benjamin E Gewurz

Infectious agents and cancer 15:28 PubMed32391073

2020

Immune landscape in Burkitt lymphoma reveals M2-macrophage polarization and correlation between PD-L1 expression and non-canonical EBV latency program.

Applications

Unspecified application

Species

Unspecified reactive species

Massimo Granai,Lucia Mundo,Ayse U Akarca,Maria Chiara Siciliano,Hasan Rizvi,Virginia Mancini,Noel Onyango,Joshua Nyagol,Nicholas Othieno Abinya,Ibrahim Maha,Sandra Margielewska,Wenbin Wi,Michele Bibas,Pier Paolo Piccaluga,Leticia Quintanilla-Martinez,Falko Fend,Stefano Lazzi,Lorenzo Leoncini,Teresa Marafioti

Pathogens (Basel, Switzerland) 9: PubMed31963774

2020

Differences in Epstein-Barr Virus Characteristics and Viral-Related Microenvironment Could Be Responsible for Lymphomagenesis in Children.

Applications

Unspecified application

Species

Unspecified reactive species

Aldana Vistarop,Oscar Jimenez,Melina Cohen,Elena De Matteo,Maria Victoria Preciado,Paola Chabay

Nature communications 9:5009 PubMed30479336

2018

Vasculogenic mimicry formation in EBV-associated epithelial malignancies.

Applications

Unspecified application

Species

Unspecified reactive species

Tong Xiang,Yu-Xin Lin,Wenlong Ma,Hao-Jiong Zhang,Ke-Ming Chen,Gui-Ping He,Xiao Zhang,Miao Xu,Qi-Sheng Feng,Ming-Yuan Chen,Mu-Sheng Zeng,Yi-Xin Zeng,Lin Feng

Oncology letters 16:2613-2619 PubMed30013656

2018

Dihydroartemisinin suppresses the proliferation of Epstein-Barr virus-associated gastric carcinoma cells via downregulation of latent membrane protein 2A.

Applications

Unspecified application

Species

Unspecified reactive species

Wei Gong,Lei Zhang,Hui Yu,Qiang Yu,Wei-Kang Pan,Yin Wang,Xuan-Lin Wu,Qiang Liu

PloS one 10:e0136476 PubMed26361042

2015

PD-1 Blockade Can Restore Functions of T-Cells in Epstein-Barr Virus-Positive Diffuse Large B-Cell Lymphoma In Vitro.

Applications

IHC-P

Species

Human

Lina Quan,Xue Chen,Aichun Liu,Yan Zhang,Xiuchen Guo,Shujie Yan,Yue Liu
View all publications
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Product promise

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