Monoclonal Antibodies
Monoclonal Antibodies - Related Videos
13:21
Antibody Generation: Producing Monoclonal Antibodies Using Hybridomas
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2023
Source: Frances V. Sjaastad1,2, Whitney Swanson2,3, and Thomas S. Griffith1,2,3,4 1 Microbiology, Immunology, and Cancer Biology Graduate Program, University of Minnesota, Minneapolis, MN 55455 2 Center for Immunology, University of Minnesota, Minneapolis, MN 55455 3 Department of Urology, University of Minnesota, Minneapolis, MN 55455 4 Masonic Cancer Center, University of Minnesota, Minneapolis, MN 55455 Polyclonal antibodies are defined as a collection of antibodies directed against...
09:57
Passive Administration of Monoclonal Antibodies Against H. capsulatum and Others Fungal Pathogens
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Cited by 8 •
2011
C57BL/6 mice have been used to study Hc pathogenesis and provide the best model. We are exploring the potential benefits of humoral immunity against this fungus and generated several mAbs [to histone H2B and a heat shock protein 60kDa] that we tested for their protective efficacy after intraperitoneal administration.
04:51
A Hybridoma Technology for Producing Monoclonal Antibodies against a Metallopeptidase
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2025
This video demonstrates an assay to produce monoclonal antibodies against porcine aminopeptidase N (APN), a membrane-bound metallopeptidase, using a traditional hybridoma technology. Upon immunizing a mouse with APN, the spleen cells are harvested and fused with immortal myeloma cells to produce hybridomas. The hybridomas are then selected and proliferated using the HAT (hypoxanthine-aminopterin-thymidine) medium to produce monoclonal antibodies specific to different APN epitopes.
03:03
An Affinity Chromatography Technique for the Purification of Monoclonal Antibodies
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2025
This video demonstrates a technique for purifying monoclonal antibodies from the culture supernatant obtained from an antibody-producing cell culture. The process involves using a matrix of crosslinked agarose beads with conjugated Protein A, which immobilizes the antibodies in the supernatant on the beads, allowing for effective separation from contaminants. By applying an elution buffer with low pH, the protein A-antibody interaction is loosened, facilitating the collection of...
03:28
Labeling Murine T Helper Lymphocytes using Radiolabeled Monoclonal Antibodies
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2025
In this video, we demonstrate the intracellular radiolabeling of T helper cells using radioactive isotope-conjugated monoclonal antibodies for non-invasive positron emission tomography imaging.
FAQs
Binding a single molecular feature of a pathogen, toxin, or host-pathogen interface helps investigators connect an observed effect to target recognition rather than broad immune reactivity. In infection research, selecting antibodies against different epitopes can support detailed analysis of antigen structure, immune recognition, and changes in pathogen-host interactions.
The outcome depends on what happens after the antibody binds its target. Binding may directly neutralize a pathogen or toxin, block an interaction with a receptor, or label the antigen for immune-mediated clearance. These are distinct functional readouts, so researchers can use them to separate interference with infection from recognition that promotes removal.
Hybridoma and recombinant expression methods provide routes for producing antibodies with the desired target specificity, while engineering can modify their properties for a particular research purpose. This flexibility allows investigators to create tools suited to detection, mechanistic studies, passive immunization, or targeted therapy, rather than treating every antibody as interchangeable.
In a diagnostic assay, an antibody's defined target recognition can be used to label or detect an antigen associated with an infectious agent. The resulting signal links detection to the presence of that molecular target, helping researchers identify pathogens and assess antigen recognition. Their specificity is especially useful when the goal is precise detection rather than broad immune measurement.
These applications are relevant when investigators want antibody-mediated protection or intervention without relying solely on the subject's own antibody response. Passive immunization uses supplied antibodies to provide targeted protection, whereas targeted therapy uses binding to influence a pathogen, toxin, receptor interaction, or clearance pathway. In infection studies, this approach helps test whether a defined target is therapeutically actionable.
Researchers can use them to characterize immune responses directed against defined antigenic targets and to test whether those targets can be neutralized, blocked, or marked for clearance. Comparing these antibody-mediated activities with vaccine-induced responses helps connect antigen recognition to potential protective function. The same tools also clarify which host-pathogen interactions deserve closer study during candidate evaluation.