Exalpha Biologicals, Inc.

Accelerating the Pace of Discovery

Product Highlight

Mouse anti-M13 phage coat protein g8p

Antibodies recognising M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface. The monoclonal antibodies manufactured and supplied by Exalpha react with either the pIII (g3p) or pVIII (g8p) proteins of M13 filamentous bacteriophage. All antibodies are available in a purified format. The antibodies are fully validated and are suitable for a wide range of techniques including:

  • ELISA
  • Flow Cytometry
  • Western Blot
  • Immunohistochemistry
  • Immunoprecipitation
For more information, click here for our M13 Bacteriophage information page.

News

Two more of our excellent products have been published by PubMed:

Potential actionable targets in appendiceal cancer detected by immunohistochemistry, fluorescent in situ hybridization, and mutational analysis
Borazanci, E., et al., J. Gastrointest. Oncol., 8, 164-172 (2017)
Using Exalpha SPARC Antibody (Cat. No. X1867P)

Molecular mechanism underlying the pharmacological interactions of the protein kinase C-β inhibitor enzastaurin and erlotinib in non-small cell lung cancer cells
Steen, N.V., et al., Am. J. Cancer Res., 7, 816-830 (2017)
Using Exalpha's FITC labeled anti PY20 Antibody (Cat. No. X1017)

Exalpha Biologicals, Inc.

EBNA 3B

  • Product Code: F120P
  • Size: 250 µg
  • Availability: In Stock In Stock
  • Price (USD): $244

Cat #

F120P		 Quantity:      

Data Sheet

Product Name

EBNA 3B

Synonyms

EBNA3B; Epstein-Barr Virus nuclear antigen 4

Host/Source

Sheep

Isotype

IgG

Product Type

Polyclonal Antibody

Reactivity

N/A

Applications

Western Blot

Purification

Ammonium Sulfate Precipitation

Size

250 µg

Price (USD)

$244

Background

EBNA-3B is one of only 10 viral proteins expressed in EBV-transformed B lymphoblasts cultured in vitro, through the expression of EBNA 3B is not required for EBV-mediated transformation in vitro. This 165kDa nuclear protein functions as a transcription factor.

Immunogen

Recombinant EBNA-3B protein

Formulation

Provided as solution in phosphate buffered saline with 0.08% sodium azide

Customer Storage

Product should be stored at -20°C. Aliquot to avoid freeze/thaw cycles

Target Molecular Weight

102.9

Database Links:

SwissProtP03203EB Virus

References

1. Anderton, E., et al, 'Two Epstein-Barr virus (EBV) oncoproteins cooperate to repress expression of the proapoptotic tumour-suppressor Bim: clues to the pathogenesis of Burkitt's lymphoma' Oncogene 2007, 27, , 421-433
2. O'Nions, J., et al, 'Epstein–Barr virus can inhibit genotoxin-induced G1 arrest downstream of p53 by preventing the inactivation of CDK2' Oncogene 2003, 22, , 7181-7191
3. Jiménez-Ramírez, C., et al, 'Epstein-Barr Virus EBNA-3C Is Targeted to and Regulates Expression from the Bidirectional LMP-1/2B Promoter' Journal of Virology 2006, 80, , 11200-11208
4. Yuan, J., et al, 'Virus and Cell RNAs Expressed during Epstein-Barr Virus Replication' Journal of Virology 2006, 80, , 2548-2565
5. Hong, G.K., et al, 'Epstein-Barr Virus Lytic Infection Contributes to Lymphoproliferative Disease in a SCID Mouse Model' Journal of Virology 2005, 79, , 13993-14003
6. Rosendorff, A., et al, 'EBNA3C Coactivation with EBNA2 Requires a SUMO Homology Domain' Journal of Virology 2004, 78, , 367-377
7. Maruo, S., et al, 'Epstein-Barr Virus Nuclear Protein EBNA3A Is Critical for Maintaining Lymphoblastoid Cell Line Growth' Journal of Virology 2003, 77, , 10437-10447
8. Gordadze, A.V., et al, 'Notch1IC Partially Replaces EBNA2 Function in B Cells Immortalized by Epstein-Barr Virus' Journal of Virology 2001, 75, , 5899-5912


Product Specific References


This product has been used in:

1. Anderton, E., et al, 'Two Epstein-Barr virus (EBV) oncoproteins cooperate to repress expression of the proapoptotic tumour-suppressor Bim: clues to the pathogenesis of Burkitt's lymphoma' Oncogene 2007, 27, , 421-433
2. O'Nions, J., et al, 'Epstein–Barr virus can inhibit genotoxin-induced G1 arrest downstream of p53 by preventing the inactivation of CDK2' Oncogene 2003, 22, , 7181-7191
3. Jiménez-Ramírez, C., et al, 'Epstein-Barr Virus EBNA-3C Is Targeted to and Regulates Expression from the Bidirectional LMP-1/2B Promoter' Journal of Virology 2006, 80, , 11200-11208
4. Yuan, J., et al, 'Virus and Cell RNAs Expressed during Epstein-Barr Virus Replication' Journal of Virology 2006, 80, , 2548-2565
5. Hong, G.K., et al, 'Epstein-Barr Virus Lytic Infection Contributes to Lymphoproliferative Disease in a SCID Mouse Model' Journal of Virology 2005, 79, , 13993-14003
6. Rosendorff, A., et al, 'EBNA3C Coactivation with EBNA2 Requires a SUMO Homology Domain' Journal of Virology 2004, 78, , 367-377
7. Maruo, S., et al, 'Epstein-Barr Virus Nuclear Protein EBNA3A Is Critical for Maintaining Lymphoblastoid Cell Line Growth' Journal of Virology 2003, 77, , 10437-10447
8. Gordadze, A.V., et al, 'Notch1IC Partially Replaces EBNA2 Function in B Cells Immortalized by Epstein-Barr Virus' Journal of Virology 2001, 75, , 5899-5912
9. McClellan, M.J., et al. ‘Downregulation of Integrin Receptor-Signaling Genes by Epstein-Barr Virus EBNA 3C via Promoter-Proximal and -Distal Binding Elements’ J. Virol. (2012), 86(9):5165-5178