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Monoclonal Antibodies

Anti-EBV Latent Membrane Protein 1 [CS 1-4]

Invented by Prof Martin Rowe from University Of Birmingham
Invented at University Of Birmingham
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Image thumbnail for Anti-EBV Latent Membrane Protein 1 [CS 1-4]
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Adapted from Shi et al. 2019. Theranostics. 9(9):2424-2438. PMID: 31131045. Figure. RIP3 protein expression is down-regulated in EBV(LMP1)-positive cells detected by Western blot analysis.
Adapted from Martin et al. 2016. J Virol; 90(19):8520-30. PMID: 27440880. Figure. LMP1 expression was confirmed by Western blotting, and actin served as a loading control in G75 (A) and Rat1 (B) cells transfected with an LMP1 expression construct or plasmid vector.
Adapted from Wang et al. 2017. Virol Sin; 32(5):423-430. PMID: 29116594 Figure. EBV expression in brain tissues of RE patients and controls. (A) Representative images of strong, moderate, and weak positive staining and negative staining for EBV antigen under low (scale bar = 100 µm) and high (scale bar = 50 µm) magnification.
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Catalogue Number 151471
Applications IHC IF IP WB
Antigen/Gene or Protein Targets Epstein-Barr Virus, Latent Membrane Protein 1 (EBV-LMP1)
Reactivity Virus
Relevance Anti-EBV (CS1) is a latent membrane protein 1 antibody, which detects a specific epitope upon LMP fusion protein in B-cell transformations, following EBV infection.

Background and Research Application
A combination of four pooled antibodies which collectively detect the latent membrane protein (LMP) of EBV, an important effector protein in B-cell transformation under EBV infection, across 20 geographically distinct EBV isolates.
EBV is a human herpesvirus that establishes a life-long persistence in the host. The virus infects the vast majority of the world's adult population and is well known for its association with a broad spectrum of benign and malignant diseases. These include infectious mononucleosis, Burkitt's lymphoma, nasopharyngeal carcinoma, and is causally associated with lymphoid and epithelial malignancies, including post-transplant lymphoproliferative disorders, Hodgkin's disease, anaplastic nasopharyngeal carcinoma and gastric carcinomas. Latent membrane protein 1 (LMP1) of Epstein-Barr virus (EBV) is a transforming protein that affects multiple cell signalling pathways and contributes to EBV-associated oncogenesis. LMP1 can be expressed in some states of EBV latency, and significant induction of full-length LMP1 is also observed frequently during virus reactivation into the lytic cycle. LMP1 is critical for EBV-infected cell activation, adhesion and survival, and is usually expressed in the malignant cells.
These antibodies were created to examine various aspects of LMP expression in B-cell lines transformed in vitro, detecting LMPs from 20 geographically varied EBV isolates.
Host Mouse
Immunogen UniProt ID P03230
Positive Control EBV transformed lymphoblastoid cell lines
Subclass IgG1 kappa
Molecular Weight (kDa) 57-66
Myeloma Used P3X63Ag8.653
Notes Production Details
Purified using multi-step affinity chromatography with protein A.

Storage Conditions
Store at -20 degrees frozen. Avoid repeated freeze/thaw cycles.

Points of Interest
Anti-EBV LMP 1, along with 2-4, showed the expression of full length LMP was strongly inducible by phorbol ester and/or sodium butyrate not just in cells entering a lytic cycle. This indicates expression of LMP in EBV transformed B-cells is under specific regulations.

Concentration
1mg/ml as standard

Difference Between Clones
4 antibodies directed against EBV LMP1 were produced in the original experiment, CS1-4. Anti-EBV (CS1) reacted strongly with both of the major pKH548 bands, whilst CS2-4 only reacted with the higher 150kDa band. This suggests CS1 recognises an epitope within the LMP fusion protein distinct to the other three anti-LMP antibodies. All antibodies are specific for the carboxy terminus of LMP 1 aa 186–386
Research Area Adhesion, Cancer, Cell Signaling & Signal Transduction, Immunology, Virology

References

There are 17 reference entries for this reagent.

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References: 17 entries

Ye et al. 2020. J Cancer. 11(5):1257-1269. PMID: 31956372.

WB

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Shi et al. 2019. Theranostics. 9(9):2424-2438. PMID: 31131045.

View  

Wang et al. 2017. Virol Sin. 32(5):423-430. PMID: 29116594.

IHC

View  

Martin et al. 2016. J Virol. 90(19):8520-30. PMID: 27440880.

WB

View  

Castrale et al. 2011. J Transplant. 2011:865957. PMID: 21559262.

View  

Flanagan et al. 2003. J Gen Virol. 84(Pt 7):1871-9. PMID: 12810882.

View  

Localization of the Epstein-Barr virus protein LMP 1 to exosomes.

Europe PMC ID: 12810882

View  

Nakatsuka et al. 2002. J Clin Oncol. 20(20):4255-60. PMID: 12377970.

View  

Pyothorax-associated lymphoma: a review of 106 cases.

Europe PMC ID: 12377970

View  

Xu et al. 2002. J Virol. 76(8):4080-6. PMID: 11907247.

View  

Preferential localization of the Epstein-Barr virus (EBV) oncoprotein LMP-1 to nuclei in human T cells: implications for its role in the development of EBV genome-positive T-cell lymphomas.

Europe PMC ID: 11907247

View  

Ascani et al. 1997. Ann Oncol. 8(11):1133-8. PMID: 9426333.

View  

Pyothorax-associated lymphoma: description of the first two cases detected in Italy.

Europe PMC ID: 9426333

View  

Epstein-Barr virus (EBV)-associated lymphoproliferative disease in the SCID mouse model: implications for the pathogenesis of EBV-positive lymphomas in man.

Europe PMC ID: 1845872

View  

Rowe et al. 1991. J Exp Med. 173(1):147-58. PMID: 1845872.

IF

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Rowe et al. 1987. J Gen Virol. 68 ( Pt 6):1575-86. PMID: 2438376.

View  

Monoclonal antibodies to the latent membrane protein of Epstein-Barr virus reveal heterogeneity of the protein and inducible expression in virus-transformed cells.

Europe PMC ID: 2438376

View  

Add a reference

References: 17 entries

Ye et al. 2020. J Cancer. 11(5):1257-1269. PMID: 31956372.

WB

View  

Shi et al. 2019. Theranostics. 9(9):2424-2438. PMID: 31131045.

View  

Wang et al. 2017. Virol Sin. 32(5):423-430. PMID: 29116594.

IHC

View  

Martin et al. 2016. J Virol. 90(19):8520-30. PMID: 27440880.

WB

View  

Castrale et al. 2011. J Transplant. 2011:865957. PMID: 21559262.

View  

Flanagan et al. 2003. J Gen Virol. 84(Pt 7):1871-9. PMID: 12810882.

View  

Localization of the Epstein-Barr virus protein LMP 1 to exosomes.

View  

Nakatsuka et al. 2002. J Clin Oncol. 20(20):4255-60. PMID: 12377970.

View  

Pyothorax-associated lymphoma: a review of 106 cases.

View  

Xu et al. 2002. J Virol. 76(8):4080-6. PMID: 11907247.

View  

Preferential localization of the Epstein-Barr virus (EBV) oncoprotein LMP-1 to nuclei in human T cells: implications for its role in the development of EBV genome-positive T-cell lymphomas.

View  

Ascani et al. 1997. Ann Oncol. 8(11):1133-8. PMID: 9426333.

View  

Pyothorax-associated lymphoma: description of the first two cases detected in Italy.

View  

Epstein-Barr virus (EBV)-associated lymphoproliferative disease in the SCID mouse model: implications for the pathogenesis of EBV-positive lymphomas in man.

View  

Rowe et al. 1991. J Exp Med. 173(1):147-58. PMID: 1845872.

IF

View  

Rowe et al. 1987. J Gen Virol. 68 ( Pt 6):1575-86. PMID: 2438376.

View  

Monoclonal antibodies to the latent membrane protein of Epstein-Barr virus reveal heterogeneity of the protein and inducible expression in virus-transformed cells.

View  

Add a reference

Inventor Information