Our Mission
For a more sustainable future. And higher quality of your results.
We provide animal-free antibodies and services to help diagnostic companies and researchers improve the quality, reliability and continuity of their tests and experiments with sequence defined antibodies.
We provide animal-free antibodies and services to help diagnostic companies and researchers improve the quality, reliability and continuity of their tests and experiments with sequence defined antibodies.
The four key aspects to our mission
So why go recombinant?
Reproducibility
Scientific progress as well as life-saving diagnostic decisions are based on assays built on the fundamental principle of reproducibility of experimental results. A second essential requirement is utmost capability to discriminate true from false-positive and false-negative results.
Despite all care we built into our sophisticated biological, biochemical or immunological assays, today we still depend on one component which is neither available in unlimited amounts to provide reproducibility, nor is it defined well enough to assure minimal false-positive and false-negative results. These are animal derived serum products, still used as first and/or secondary antibodies in countless diagnostic tests.
In a PCR-based assay, would you use a primer set without knowing the exact sequence of these primers and without the possibility to sequence the generated PCR amplicon for confirmation? Nowadays, when using non-recombinant antibodies for detection of a specific protein, we have to do exactly that, since typical diagnostic or research antibodies are not defined by their sequence, often contain many undefined additional components and other IgGs present in the animal which produced them, and vary in their composition over time1.
Most antibodies used for research and diagnostics today are still polyclonal serum products obtained after animal immunization – mainly due to the low price of this method. On the other hand, this animal origin is responsible for significant batch to batch variations and the risk of product discontinuity.
Specificity
Animal derived antisera always contain many unwanted Immunglobulins of unknown specificity, causing an intrinsic risk of unwanted reactivities which can never be completely excluded by affinity purification steps2-7.
While also still depending on animal immunization, the hybridoma technology substantially improved this scenario, as it allowed the production of monoclonal antibodies for the first time.
Yet, contrary to widespread belief, these antibodies are not always monospecific. As shown in a multicentric study8 of 185 monoclonal hybridoma sequences, a striking 30 % of these hybridomas expressed additional productive light chains, sometimes even additional heavy chains, resulting in the generation of an oligospecific mixture of antibodies in their supernatant.
So, hybridoma-derived monoclonals are not always as defined as we thought. Furthermore, hybridoma antibodies do not provide the epitope diversity of polyclonals, which can result in lower signals and a more narrow application profile. Finally, storage of hybridoma lines in liquid nitrogen constitutes a quite expensive and not flawless system, that already caused the loss of countless hybridoma clones, making a future reproduction of results with these antibodies impossible.
As a result, the only unequivocally monoclonal antibodies are sequence defined antibodies generated and produced with recombinant technologies, most prominently antibody phage display. Only these antibodies provide infinite reproducibility, since they can always be reconstituted from their electronically stored or printed amino acid sequence.
Versatility
Since the DNA encoding Abcalis® antibodies is always available from the start, we can fuse the antigen binding end to many other protein domains. Typically, Fc from other species than human can be used, to combine e.g. three different Abcalis® antibodies in a three colour staining, using three different secondary antibodies9.
ScFv-Fragments from human libraries can be detected by anti-mouse Fc, anti-rabbit Fc or other secondary antibodies if they have been fused accordingly. While we may not always have every possible combination on stock, we do produce respective versions on request – or even fuse other Fc parts or detection domains you may need for your particular experiment.
Beside these usual host species (human, mouse, rabbit, goat), Abcalis® develops and offers special antibody formats for different applications. Every Abcalis® antibody can be acquired in every available format due to our recombinant technology. These formats can also be made available for customer antibodies via our format conversion service.
Sustainability
The immunization of animals and the extraction of animal sera is a practice that was initially conceived by Emil von Behring in the year 1890 and has been around ever since.
However, new technologies today allow to generate antibodies without the use of immunized animals. The Nobel Prize honoured technology of Antibody Phage Display allows to select antibodies entirely in vitro.
By using our sequence defined recombinant antibodies, you can obtain superior quality of your results with animal-free reagents.
It is our mission and aspiration every single day to achieve this goal, both for a sustainable future and medical safety of this and every future generation to come.
SOURCES
1Bradbury A, Plückthun A. (2015). Getting to reproducible antibodies: the rationale for sequenced recombinant characterized reagents. Protein Eng Des Sel. 28(10):303–305.
2Berglund L et al. (2008). A genecentric Human Protein Atlas for expression profiles based on antibodies. Mol Cell Proteomics 7(10):2019-2027.
3Bradbury A, Plückthun A. (2015). Reproducibility: Standardize antibodies used in research. Nature 518(7537):27-29.
4Dove A. (2017). Technology Feature | Agreeable antibodies: Antibody validation challenges and solutions. Science 357(6356):1165-1167.
5Goodman, 2018. The antibody horror show: an introductory guide for the perplexed. New Biotechnol 45:9-13.
6Bradbury A, Plückthun A. (2015). Antibodies: Validate recombinants once. Nature 520(7547):295.
7Taussig MJ et al. (2018). Antibody validation: a view from the mountains. N Biotechnol 45:1-8.
8Bradbury et al. (2018). When monoclonal antibodies are not monospecific: Hybridomas frequently express additional functional variable regions. MAbs 10(4):539-546.
9Moutel et al. (2009). A multi-Fc-species system for recombinant antibody production. BMC Biotechnology 9:14.
