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Contributor Information

  • Name Martin Rowe
  • Institute University of Birmingham

Tool Details

  • Tool name: Anti-EBV Latent Membrane Protein 1 [CS 1-4]
  • Clone: CS 1-4
  • Tool type: Antibodies
  • Tool sub-type: Primary antibody
  • Class: Monoclonal
  • Conjugate: Unconjugated
  • Reactivity: Virus
  • Host: Mouse
  • Molecular weight of the target: 57-66 kDa
  • Application: IHC ; IHC ; IF ; IP ; WB
  • Description: 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.
  • Immunogen: P03230
  • Immunogen UniProt ID: P03230
  • Isotype: IgG1 kappa
  • Research area: Cell biology; Cancer; Cell signaling and signal transduction; Immunology; Microbiology
  • Myeloma used: P3X63Ag8.653

  • For Research Use Only

Target Details

  • Target: Epstein-Barr Virus, Latent Membrane Protein 1 (EBV-LMP1)
  • Target molecular weight: 57-66 kDa
  • Target background: 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.

Application Details

  • Application: IHC ; IHC ; IF ; IP ; WB

Handling

  • Format: Liquid
  • Concentration: 1 mg/ml
  • Storage buffer: PBS with 0.02% azide
  • Storage conditions: Store at -20°C frozen. Avoid repeated freeze / thaw cycles
  • Shipping conditions: Shipping at 4°C

Documentation

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References

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  • •  Shi et al. 2019. Theranostics. 9(9):2424-2438. PMID: 31131045.
  • •  Wang et al. 2017. Virol Sin. 32(5):423-430. PMID: 29116594.
  • •  Martin et al. 2016. J Virol. 90(19):8520-30. PMID: 27440880.
  • •  Castrale et al. 2011. J Transplant. 2011:865957. PMID: 21559262.
  • •  Flanagan et al. 2003. J Gen Virol. 84(Pt 7):1871-9. PMID: 12810882.
  • •  Localization of the Epstein-Barr virus protein LMP 1 to exosomes.
  • •  Nakatsuka et al. 2002. J Clin Oncol. 20(20):4255-60. PMID: 12377970.
  • •  Pyothorax-associated lymphoma: a review of 106 cases.
  • •  Xu et al. 2002. J Virol. 76(8):4080-6. PMID: 11907247.
  • •  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.
  • •  Ascani et al. 1997. Ann Oncol. 8(11):1133-8. PMID: 9426333.
  • •  Pyothorax-associated lymphoma: description of the first two cases detected in Italy.
  • •  Epstein-Barr virus (EBV)-associated lymphoproliferative disease in the SCID mouse model: implications for the pathogenesis of EBV-positive lymphomas in man.
  • •  Rowe et al. 1991. J Exp Med. 173(1):147-58. PMID: 1845872.
  • •  Rowe et al. 1987. J Gen Virol. 68 ( Pt 6):1575-86. PMID: 2438376.
  • •  Monoclonal antibodies to the latent membrane protein of Epstein-Barr virus reveal heterogeneity of the protein and inducible expression in virus-transformed cells.