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The development of antibody-drug conjugates (ADCs) has transformed cancer treatment by combining the specificity of monoclonal antibodies with the cytotoxic potency of chemotherapy agents. Gemtuzumab ozogamicin (GO) was the first ADC to receive FDA approval, marking a significant milestone in targeted oncology therapies. Initially approved in 2000 for relapsed/refractory acute myeloid leukemia (AML), GO was withdrawn in 2010 due to safety concerns.

The past 25 years have seen significant advancements in therapeutic antibodies for cancer treatment, driven by academic and industrial collaborations. From the approval of rituximab in 1997 to the development of immune checkpoint inhibitors and bispecific antibodies, oncology has witnessed a transformation in drug discovery and regulatory approvals.

Bispecific antibodies (bsAbs) represent an important advancement in cancer immunotherapy, enabling dual-targeting mechanisms that enhance tumor specificity, immune activation, and therapeutic efficacy. The structural and functional versatility of bsAbs allows for diverse formats tailored to different clinical needs.

Antibody-based therapies continue to play a pivotal role in the treatment of autoimmune diseases, infectious diseases, and cancer. Recent regulatory advancements highlight the progress of multiple investigational and approved therapies across various indications.

VHH antibodies, also known as nanobodies, have emerged as a transformative class of biologics with applications spanning oncology, neurology, and targeted drug delivery. Their small size, high stability, and unique binding properties allow them to overcome many limitations of conventional monoclonal antibodies (mAbs).

DOI: 10.3389/fimmu.2019.01598Monoclonal antibodies (mAbs) have transformed modern medicine by providing highly specific therapies for cancer, autoimmune diseases, and infectious diseases. Their development traces back to key immunological discoveries that laid the groundwork for antibody-based thera

Bispecific antibodies (bsAbs) represent a significant advancement in therapeutic antibody technology, simultaneously binding to two different antigens to enable novel treatment mechanisms across multiple disease areas, including oncology, hematology, ophthalmology, and diagnostics.

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.