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Find out how we're addressing the reproducibility crisis with our recombinant monoclonal antibodies.
In a survey carried out by Nature on scientific reproducibility, 90% of respondents agreed that there was a reproducibility crisis, but only 33% had considered how it could be addressed1. The reproducibility crisis has long since been a challenge for the scientific community, but by selecting robust and reliable reagents for our research, we can start to overcome it.
A survey of 1,576 researchers by Nature revealed that over 70% of researchers cannot reproduce another scientist’s experiments1.Given how often our work relies on protocols or results from other labs, this is a major problem.
This irreproducibility correlates to an enormous amount of wasted time and money; a paper by Andrew Bradbury in 2015 estimated that $1.6 billion was spent on poorly characterized antibodies worldwide2. Since this paper was written, this estimate has more than doubled to $3.5 billion3.
Overcoming the reproducibility crisis will be both a group and individual effort, but there are some simple changes we can make to improve the reproducibility of our work.
Figure 2: Examples of how many papers are affected by non-specific antibodies from Abcam’s Reproducible Science Week webinars. Speakers: Andrew Bradbury, Pablo Engel, Peter McPherson, and Angelo De Marzo.
To achieve accurate, reproducible results, the antibodies we use in our research need to have high specificity and batch-to-batch consistency, but these factors differ between polyclonal, monoclonal, and recombinant monoclonal antibodies.
Polyclonal antibodies have a high degree of variability and the ability to bind to multiple epitopes, due to being derived from a natural immune response. The heterogeneity of polyclonal antibodies offers advantages in some applications6, but every time a new batch is created another group of animals needs to be reimmunized. This makes it difficult to obtain a consistent polyclonal mixture, resulting in variable specificity and inconsistencies from batch to batch.
Traditionally produced monoclonal antibodies are derived from a single B-parent clone, which ensures they detect a specific epitope. They’re invaluable for effective drug or biomarker discovery, used to quantify, localize, and modulate proteins of interest.
Although the use of a hybridoma allows the generation of identical monoclonal antibodies, over long periods, genetic drift can occur, which results in slight variations in antibody batches over time; 40% of hybridoma-produced monoclonal antibodies have been shown to express additional productive heavy or light chains, rendering these antibodies non-specific7.
Recombinant monoclonal antibodies can overcome the specificity and reproducibility issues experienced with polyclonal and hybridoma-derived monoclonal antibodies. By cloning antibody genes into high-yield expression vectors, the encoding sequences can be controlled, resulting in improved antibody specificity and sensitivity. This also enables the antibodies to be made against virtually any antigen, including non-immunogenic and toxic antigens. Plus, the recombinant production method avoids problems such as gene loss, gene mutations, and cell-line drift.
The use of recombinant antibodies in our research can therefore produce highly reproducible results due to batch-to-batch consistency.
Validating antibodies before use is essential to ensure application-specific performance. Our recombinantly manufactured antibodies offer high specificity and reproducibility, reducing the time and resources required for validation.
Testing antibodies on knock-out cell lines is the gold standard for determining antibody specificity. The western blots below compare the specificity of a monoclonal and a recombinant antibody in both wild-type and knockout samples. If the antibody has high specificity, the band or bands specific to the target protein will disappear in the knock-out sample. While this is the case for the recombinant antibody, the traditional monoclonal antibody displays additional cross-reactivity.
Over 3,800 of our recombinant antibodies are KO-validated – this confirmed specificity means you can move your project forward faster and achieve reproducible results.
Figure 3: Abcam's recombinant anti-TLE1 [EPR9386(2)] antibody (left) being tested on knock-out and wild-type samples against our monoclonal anti-TLE1 [OTI1F5] antibody (right).
Biophysical testing enables confirmation of antibody identity at a molecular level, delivering robust, reproducible, and quality results across a large portfolio of products for the best lot-to-lot consistency.
We use a variety of methods as part of our robust quality control process, including:
Taking small steps to improve reproducibility in our own experiments can have a large impact on the wider scientific community. Whether it’s ensuring correct validation of reagents in your application, optimizing data analysis, or making the switch to recombinant antibodies, by working together, we can tackle the reproducibility crisis.