Anti-Burkholderia mallei BpaB [BpaB#4] Antibody

This mouse IgG monoclonal antibody was generated against purified his-tagged BpaB and is specific for Burkholderia mallei autotransporter BpaB.

Highlights:

  • Reacts with Burkholderia mallei autotransporter BpaB
  • Possible tool for the development of therapeutic measures against Burkholderia
  • Recommended for ELISA, Immunofluorescence, Western Blot and Flow Cytometry applications

Autotransporter proteins (AT) form one of the largest class of virulence factors in Gram-negative organisms and perform important functions in pathogenesis including flocculation, formation of biofilms , complement resistance, host cell adhesion and entry, intracellular motility and replication, cytotoxicity, and lipolytic activity. Given their function in pathogenesis and overall structure, AT are excellent targets for developing medical countermeasures (MCM) against pathogenic organisms. A significant portion of AT (passenger domain) is readily accessible for recognition by the immune system as it is exposed on the bacterial surface.

From the laboratories of Robert J. Hogan, PhD and Eric R. Lafontaine, PhD, University of Georgia.

The Investigator's Annexe Part of The Investigator's Annexe program.

Catalog Number Product Size AVAILABILITY Price Qty
EGA074
Anti-Burkholderia mallei BpaB [BpaB#4] Antibody, (supernatant), 5mL
5mL (supernatant) In stock
Price: $269.00
Specifications
Product Type: Antibody
Accession ID: Q6Y659
Antigen: BpaB autotransporter of B. mallei
Molecular Weight: 105 kDa per subunit
Isotype: IgG
Clonality: Monoclonal
Clone Name: BpaB#4
Reactivity: Burkholderia mallei
Immunogen: Purified, his-tagged BpaB
Species Immunized: Mouse
Buffer: Cell Culture supernatant
Tested Applications: ELISA, Immunofluorescence, Western Blot and Flow Cytometry
Storage: -80C
Shipped: Dry ice
Data

Western Blot

BpaB production by E. coli recombinant strains. Equivalent amounts of whole cell lysates (WCL), total membrane proteins (TMP) and sarkosyl-insoluble fractions containing OM proteins (OMP) were resolved by SDS-PAGE, transferred to PVDF membranes and analyzed by western blot with the monoclonal antibody BpaB-MAb#4. Molecular weight markers are shown to the left in kilodaltons.

Provider
From the laboratories of Robert J. Hogan, PhD and Eric R. Lafontaine, PhD, University of Georgia.
References
  1. Zimmerman SM, Michel F, Hogan RJ, Lafontaine ER. The Autotransporter BpaB Contributes to the Virulence of Burkholderia mallei in an Aerosol Model of Infection. PLoS One, 10(5), 2015.
  2. Zimmerman SM, Long ME, Dyke JS, Jelesijevic TP, Michel F, Lafontaine ER, Hogan RJ. Use of Immunohistochemistry to Demonstrate In Vivo Expression of the Burkholderia mallei Virulence Factor BpaB During Experimental Glanders. Vet Pathol. 2018 Mar;55(2):258-267. View Article

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