Catalogue Number: AB03230-2.0-BT-ABA
| Manufacturer: | Vector Laboratories, Inc (ABA) |
| Type: | Recombinant Monoclonal |
| Alias: | phase I lipopolysaccharide; LPS phase I; C. burnetii PI-LPS; C. burnetii phase I lipopolysaccharide |
| Shipping Condition: | Blue Ice |
| Unit(s): | 1 mg |
| Host name: | Mouse |
| Clone: | 1E4 |
| Isotype: | IgG2a |
| Immunogen: | The original antibody was generated by immunizing BALB/c mice with formalin-inactivated C. burnetii Nine Mile PI antigen. |
| Application: | ELISA, WB, InVitroA, InVivoA |
Purified
Recombinant Monoclonal
Store at 4⁰C for up to 3 months. Note, this antibody is provided without added preservatives, it is therefore recommed this antibody be handled under sterile conditions. For longer storage, aliquot and store at -20⁰C.
The specificity of the antibody (IgG2a) for PI-LPS was confirmed by ELISA analysis. The antibody detected PI-LPS by western blot analysis. The antibody was able to inhibit C. burnetii infection in vivo in a dose-dependent manner (Peng et al., 2012; PMID: 23053512). The original antibody could confer protection against C. burnetii aerosol infection. The Fab fragment, the scFv fragment and the humanized version of the antibody were constructed and characterized by indirect ELISA and Western Blot. They were able to bind to C. burnetii and to inhibit the infection in mice and in mouse Bone Marrow-Derived Macrophages (BMDM) in vitro. The humanized version inhibited C. burnetii infection in human macrophages in vitro. The Fab fragment was able to neutralize virulent C. burnetii resulting in inhibiting C. burnetii infection in both in vitro and in vivo systems (US20150087807A1). The ability of the original antibody, Fab, scFv, and humanized version of the antibody to inhibit C. burnetii infection in vivo was evaluated by comparing splenomegaly, bacterial burden, and pathological changes in the spleen with control mice at 14 days postinfection. IFA was used to analyze the ability of the original antibody to bind live virulent C. burnetii. The ability of the original to inhibit C. burnetii was higher than the ability of the other fragments. The humanized version of the antibody showed potential as a therapeutic against C. burnetii exposure (Peng et al., 2014; PMID: 25114119).