Going further than ever before with a new generation of antibodies

Antibodies are widely used in medicine – and we are all likely to have benefited from an antibody-based test or treatment as part of our everyday lives. They are also an essential tool in biomedical research where they continue to play vital roles in countless discoveries.

Many diagnostic tests carried out in doctor’s surgeries or clinical laboratories rely on antibodies to identify specific diseases. They’re also found in over-the-counter kits like pregnancy tests, which contain antibodies that bind to human chorionic gonadotropin, the hormone that signals a pregnancy. And they are also used as therapeutics – for example, to treat certain cancers or autoimmune diseases including multiple sclerosis and rheumatoid arthritis.

In addition, biomedical researchers regard antibodies as essential laboratory reagents, with their high specificity and sensitivity making them ideal for use in a plethora of applications – from protein detection to cell separation.

But the traditional approaches used for antibody production could be improved – particularly as these often rely on the use of animals.

Antibodies are protein molecules around 10nm in size, which are produced exclusively by specialist white blood cells called B cells [1]. They play a vital role in our immune system, helping to protect us from infection.

When our immune system recognizes a foreign substance – or antigen – that enters our body, it triggers several responses, including antibody production.

When a B cell binds an antigen, it will divide and mature into a group of identical cells known as a clone. A mature B cell can produce 2,000 antibody molecules per second – that enter the circulation and bind to a specific antigen like a jigsaw piece, tagging it as a threat that needs eliminating by the immune system [2].

Collectively, our army of B cells has the potential to recognize countless antigens. But an individual B cell clone produces a unique antibody that binds to a single antigen.

Although the general structure of an antibody is similar from molecule to molecule, they contain structural variations within the region that binds with the antigen – the antigen-binding site.
 

In the past, scientists have had the choice of using polyclonal or monoclonal antibodies, which offer different advantages that are desirable for specific applications.

Polyclonal antibodies are a mixture of different antibodies, which are produced as a result of the activation of several different B cell clones in an animal. Each individual antibody recognizes and binds to a different part – or epitope – of the same antigen. This type of antibody is often used in research, but a major disadvantage is variability between batches, as they are produced in different animals at different times. And because these are derived from animal sources, their supply has traditionally been limited.

In contrast, monoclonal antibodies are made from a single B cell clone and only recognize a single epitope on an antigen. These are traditionally produced by the fusion of B cells with a tumor cell to produce a hybridoma - an immortal antibody-producing cell that can be used to produce a specific antibody indefinitely.

Monoclonal antibodies are usually the better choice for applications such as therapeutic drug development, which require large amounts of identical antibodies. Their high specificity makes them useful in highly targeted immunoassays, such as diagnostic applications – as they are less likely than polyclonal antibodies to cross-react with other proteins.

“Traditional antibodies have been around, but there haven’t been huge innovations made in production technologies – yet the demand from researchers for antibodies has grown, especially to study new targets and markers,” says Isaku Tanida, Head of Protein and Pathway Technologies at Merck KGaA, Darmstadt, Germany.

Our ZooMAb^® recombinant antibodies offer a new generation of monoclonal antibodies that are specifically engineered using our proprietary technology. 

The approach involves using recombinant technology – or genetic engineering – to produce large quantities of a monoclonal antibody in cells. The gene sequences for the antibody are cloned into a DNA vector and delivered into cells. These cellular factories make the antibody, which is then harvested and purified for use by researchers around the world.

The technology enables antibodies to be derived from a wide range of species and eliminates the need for arduous cell fusion and hybridoma construction. And once the gene sequence for the antibody is obtained, it is produced without the need to harm or sacrifice any animals – offering an essentially limitless supply of a monoclonal antibody with exceptional batch-to-batch consistency.

“So researchers no longer need to worry about the supply, but they still benefit from similar and even improved capabilities and functions,” says Isaku Tanida. “They also get the same product time after time, improving their chance of achieving reproducible results.”

Many countries have restrictions on importing traditional antibody products. But as ZooMAb^® antibodies are provided free of animal components, biocides such as sodium azide and preservatives – this can help to reduce red-tape, democratizing the use of antibodies.

“We are already seeing that regions that traditionally had challenges with importing antibodies now have access to this product,” says Isaku Tanida.

ZooMAb^® recombinant antibodies are also exceptionally stable and can be shipped and stored at room temperature.
 

With modern biotechnology facilitating the large-scale production of different types of antibodies, these tiny molecules have become crucial tools in medicine and research.

“For researchers, ZooMAb^® antibodies will enable further discoveries and eventually lead to the development of new tests for key disease markers,” says Isaku Tanida.

This novel platform demonstrates our leadership in the Life Science space and our deep technical capabilities to develop a new, more ethical and sustainable option for advancing research.

“We are already seeing the realization of the benefits since the launch of these antibodies,” Isaku Tanida. “Researchers are able to study targets that they couldn’t before – and countries that didn’t have access to antibodies before are now pushing the boundaries of possibility with this product.”

_{[1] https://www.agrisera.com/en/info/igg.html
[2] https://www.ncbi.nlm.nih.gov/books/NBK26884/}

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