Rat Monoclonal LMP2 antibody. Suitable for WB, IHC-P and reacts with Epstein-Barr virus samples. Cited in 12 publications.
pH: 7.4
Preservative: 0.09% Sodium azide
Constituents: PBS
| WB | IHC-P | |
|---|---|---|
| Epstein-Barr virus | Expected | Expected |
| Species | Dilution info | Notes |
|---|---|---|
Species Epstein-Barr virus | Dilution info 1/100.00000 - 1/1000.00000 | Notes - |
| Species | Dilution info | Notes |
|---|---|---|
Species Epstein-Barr virus | Dilution info Use at an assay dependent concentration. | Notes - |
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.
Latent membrane protein 2, Terminal protein, LMP2
Rat Monoclonal LMP2 antibody. Suitable for WB, IHC-P and reacts with Epstein-Barr virus samples. Cited in 12 publications.
pH: 7.4
Preservative: 0.09% Sodium azide
Constituents: PBS
ab59028 recognises LMP2A and does not cross react with LMP2B.
Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant.
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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.
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.
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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