Antibody Gene Assembly
Antibody Gene Assembly - Related Videos
12:02
Transient Gene Expression in Tobacco using Gibson Assembly and the Gene Gun
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Cited by 8 •
2014
This work describes a novel method for selectively targeting subcellular organelles in plants, assayed using the BioRad Gene Gun.
11:36
Assembly, Loading, and Alignment of an Analytical Ultracentrifuge Sample Cell
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Cited by 21 •
2009
The analytical ultracentrifuge (AUC) sample cell holds sample and reference buffer and during experiments and is exposed to high vacuum and rotor speeds up to 60,000 rpm. This video will demonstrate the rigorous attention to detail necessary for assembly, loading and alignment of this very important component of an AUC experiment.
12:55
Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
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Cited by 33 •
2015
A method is described with visual accompaniment for conducting scalable, high throughput selections from phage-displayed combinatorial synthetic antibody libraries against hundreds of antigens simultaneously. Using this parallel approach, we have isolated antibody fragments that exhibit high affinity and specificity for diverse antigens that are functional in standard immunoassays.
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...
04:47
A Method to Assess Fc-mediated Effector Functions Induced by Influenza Hemagglutinin Specific Antibodies
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Cited by 6 •
2018
We describe a method to measure the activation of Fc-mediated effector functions by antibodies that target the influenza virus hemagglutinin. This assay can also be adapted to assess the ability of monoclonal antibodies or polyclonal sera targeting other viral surface glycoproteins to induce Fc-mediated immunity.
FAQs
RAG1 and RAG2 act during B-cell development to join selected antibody-gene DNA segments. Their activity connects the variable, diversity, and joining regions in a rearranged sequence, creating the genetic template for an antibody chain. Because this step determines which segments become physically linked, it provides a central control point for generating different antigen specificities.
Different combinations of V, D, and J segments produce different assembled variable regions before the resulting genes are expressed. This segment-level variation means that B cells need not use the same DNA arrangement, allowing the immune system to generate receptors with diverse antigen specificities. The principle is distinct from junctional diversity, which arises at the boundaries where segments are joined.
Junction formation is not always exact, so the DNA sequence at the boundaries between joined segments can vary. These sequence differences create additional receptor variation beyond the choice of V, D, and J segments alone. Consequently, imprecise joining helps explain how antibody gene assembly supports recognition of a broad range of molecular targets.
After the gene segments are assembled, the resulting genes are transcribed and expressed as antibody chains. Those chains form the molecular basis of receptors produced by B cells, linking a DNA rearrangement to antigen recognition. Studying this transition connects gene assembly with immune-cell development and with the specificity of the receptors that B cells can generate.
Research on this process can illuminate how the immune system develops its B-cell repertoire and achieves receptor diversity. It also provides context for investigating immunodeficiency, autoimmune disease, and vaccine responses. Knowledge of the assembly process helps relate antibody-gene organization and expression to differences in immune recognition across these biological and medical settings.
Understanding how variable antibody genes are assembled provides a foundation for studying how antibody sequences encode antigen specificity. That knowledge is relevant to engineering therapeutic antibodies, where antibody genes and their expressed chains determine target recognition. The same framework also supports interpretation of vaccine responses and the diverse antibodies generated during immune development.