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Recombinant antibodies give you the highest level of consistency between batches, peace of mind with an uninterrupted supply, and the ability to engineer sensitivity and specificity.
Monoclonal antibodies are typically made using B-cells from an immunized animal to form immortal hybridoma cells that secrete the desired antibody clone. This hybridoma technique produces highly consistent, specific and sensitive monoclonal antibodies in large quantities. However, over time, hybridoma cell lines can experience genetic drift, resulting in slight variations to the antibodies produced. There is also a growing demand for antibodies against difficult targets, ie toxins, nucleotides, and membrane-bound proteins, that can’t always be made with this in vivo model.
Recombinant antibodies overcome many of the limitations of hybridoma-production of monoclonal antibodies.
Recombinant antibodies are produced in vitro by cloning antibody genes for immune-specific heavy and light antibody chains into high-yield expression vectors. These vectors are then introduced into expression hosts (eg bacteria, yeast, or mammalian) to generate the recombinant monoclonal antibodies. Recombinant antibodies can be used wherever you would normally use a traditional monoclonal antibody.
Recombinant antibodies offer several advantages over both traditional monoclonal and polyclonal antibodies:
In order to provide you with antibodies that have excellent sensitivity with the highest degree of consistency, we have engineered recombinant versions of our RabMAb rabbit monoclonal antibodies. This combination delivers several unique advantages.
At the moment, we have over 10,000 recombinant RabMAb antibodies and can also offer a custom RabMAb development service.
Table 1. The benefits of recombinant antibodies and RabMAb antibodies
RabMAb rabbit monoclonal antibodies
High consistency and reproducibility
High affinity (10-12 kD possible)
Diverse epitope recognition
In addition to the benefits of recombinant antibodies and RabMAb antibodies, recombinant RabMAb antibodies are
In vitro phage display technology and library provide the ability to screen, validate, and manufacture recombinant monoclonal antibodies more rapidly and against especially difficult targets. For example, here’s an in vitro derived recombinant monoclonal antibody developed against Diphtheria toxin.
Figure 2. Human monoclonal IgG1 to Diphtheria toxin (ab209329): Due to toxic effects it is difficult to develop antibodies using an in vivo approach against toxins hence why we isolated an antibody using the in vitro phase display library.
Our phage display relies on a large library of bacteriophage particles (>1010 clones), each carrying the genetic information and the unique phenotypic binding function of one antibody clone. The libraries we make use of are M13 phagemid libraries with diversity restricted to the most variable positions in the complementary determining regions (CDRs) of natural antibody sequences. This method limits the number of parental clones in the library to less than 1%. Screen procedures are as follows:
Figure 3. Schematic of the phage display process.
Selected references for our phage display recombinant antibody technology