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Immunoglobulin G (IgG) antibodies are an essential part of the immune system, defending against infections and maintaining immune memory. These antibodies recognize and neutralize pathogens, providing long-term immunity after infection or vaccination. Beyond their biological role, IgG antibodies are widely used in biomedical research, diagnostics, and therapeutic applications.

Monoclonal antibodies (mAbs) are the largest class of recombinant proteins used as therapeutics, playing a critical role in treating cancers, autoimmune diseases, and infectious conditions. Producing recombinant mAbs requires a host system that can efficiently express, fold, and modify these complex proteins while maintaining their efficacy and safety.

The development of monoclonal antibody (mAb) therapeutics began in 1975 when Köhler and Milstein developed hybridoma technology, a breakthrough that earned them the Nobel Prize in 1984. The first mAb approved for human use, Orthoclone OKT3 (muromonab-CD3), was licensed in 1986 for preventing kidney transplant rejection.

Monoclonal antibodies (mAbs) provide targeted treatments for cancer, immune-related disorders, infectious diseases, and hematological conditions. Since the approval of the first therapeutic mAb, muromonab-CD3 (OKT3), in 1986, the field has expanded significantly. As of June 2022, a total of 162 mAbs

Since the first monoclonal antibodies (mAbs) were approved by the FDA in 1986, the field of therapeutic antibodies has advanced significantly. Early hybridoma technology produced mouse-derived antibodies, but these were limited by human antibodies developing an immune response against them. By the late 1990s, chimeric, humanized, and fully human monoclonal antibodies were developed, improving efficacy and safety.

Antibody–drug conjugates (ADCs) now have multiple FDA approvals and hundreds of clinical trials exploring novel targets and indications. The success of ADCs stems from advancements in multiple areas.

Antibodies, also known as immunoglobulins (Ig), are Y-shaped glycoproteins produced by B-cells in jawed vertebrates. They play a key role in immune defense by recognizing and binding specific antigens. Each antibody consists of two heavy chains and two light chains, which together form the fundamental structure of the molecule.

Biointron has launched "Spotlight on Antibodies", a monthly podcast diving deep into the world of antibody innovation. Listen to our first episode on Podbean, Spotify, Apple, or Amazon Music!Spotlight on Antibodies by Biointron is your go-to monthly podcast exploring the latest trends, bre

Phage display is a widely used technique for selecting and engineering antibodies with high specificity and affinity for target antigens. By fusing antibody fragments to bacteriophage coat proteins, researchers can generate large libraries and screen for desired binding properties. Over the ye

Generative AI is redefining the life sciences landscape through its ability to synthesize large amounts of structured and unstructured data. Its multimodal capabilities, leveraging inputs such as omics, images, patient data, and molecular structures, are particularly useful for the pharmaceutical industry.

VHH antibodies, derived from camelid single-domain antibodies, have a small size, high stability, and high binding affinity, making them ideal candidates for a wide range of therapeutic and diagnostic applications.

Structure of antibody–drug conjugates that have reach clinical trials and their payloads. DOI: 10.1186/s13045-022-01397-yAntibody-drug conjugates (ADCs) combine the selectivity of monoclonal antibodies with the potency of cytotoxic agents, enabling the precise delivery of therapeutic payloads to ca