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antibody formats

Antibody formats refer to the different structural and functional configurations of antibodies, particularly in the context of therapeutic and diagnostic applications. Antibodies are naturally Y-shaped molecules composed of two heavy chains and two light chains, but in biotechnology, they can be engineered into various formats to enhance their performance for specific uses. Here are some of the key antibody formats:

1. Full-Length Antibodies: These are the conventional form of antibodies, consisting of two heavy chains and two light chains. They have a typical Y-shape with two antigen-binding sites and are capable of triggering immune effector functions.

2. Monoclonal Antibodies (mAbs): These antibodies are derived from a single B-cell clone and are homogeneous in structure and specificity. They are widely used in therapeutics and diagnostics.

3. Fragment Antigen-Binding (Fab): Fab fragments consist of one constant and one variable domain of both the heavy and light chains. They contain the antigen-binding site but lack the Fc region, which is responsible for binding to cell receptors and the complement system.

4. Single-Chain Variable Fragment (scFv): scFvs are smaller antibody fragments that consist of the variable regions of the heavy (VH) and light (VL) chains linked together by a short peptide linker. They have a single antigen-binding site and are smaller than Fab fragments.

5. Bispecific Antibodies: These antibodies have been engineered to bind to two different antigens or epitopes simultaneously. They are useful in cancer therapy, where one part of the antibody can target a tumor cell and the other can engage an immune effector cell.

6. Antibody-Drug Conjugates (ADCs): ADCs are antibodies linked to a drug or toxin. They use the antibody's targeting ability to deliver the drug directly to specific cells, such as cancer cells, thereby minimizing systemic toxicity.

7. Nanobodies: Derived from camelid antibodies, nanobodies consist of a single variable domain and are the smallest naturally occurring antibody fragments that can bind antigens. They are notable for their stability and ease of production.

8. F(ab')2 Fragments: These are generated by pepsin digestion of full-length antibodies and consist of two Fab units linked by disulfide bonds. They have two antigen-binding sites and are devoid of the Fc region.

9. Multivalent or Multispecific Antibodies: These are engineered antibodies that possess multiple antigen-binding sites, either for the same or different antigens. This increases their binding strength and specificity.

10. Chimeric and Humanized Antibodies: Chimeric antibodies combine portions from different species, typically human and mouse, whereas humanized antibodies are mostly human, with only the antigen-binding sites coming from mouse antibodies. These modifications are designed to reduce immunogenicity when used as therapeutics in humans.

Each antibody format has its own set of advantages and applications. The choice of format depends on the desired biological activity, target specificity, pharmacokinetics, and potential clinical use. These diverse formats have significantly expanded the therapeutic and diagnostic capabilities of antibodies in medicine and research.


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If you know of any terms that have been omitted from this glossary that you feel would be useful to include, please send detail to the Editorial Office at GenScript: [email protected]

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