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Single-Domain Antibodies for Intracellular Toxin Neutralization
2022Ricin is a plant-derived toxin with a history as a biothreat agent. The toxin's enzymatic subunit, ricin toxin A chain (RTA), is a ribosome-inactivating protein that, when delivered into the cytoplasm of mammalian cells, arrests protein synthesis with extraordinary efficiency.
Timothy F, Czajka, Nicholas J, Mantis
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Multivalent Display of Single-Domain Antibodies
2012Antigen-binding fragments, such as single-domain antibodies (sdAbs), can now be readily isolated by in vitro technologies. Antibody fragment libraries derived from immune or nonimmune sources are presented in a molecular display format, typically phage display, and binders to individual antigens are selected from the libraries by a so-called panning ...
Zhang, J., MacKenzie, C.R.
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Humanization of Camelid Single-Domain Antibodies
2022Humanization of therapeutic antibodies derived from animal immunizations is often required to minimize immunogenicity risks in humans, which can cause potentially harmful and serious side effects and reduce antibody efficacy. Humanization is typically applied to conventional monoclonal antibodies derived in rodents as well as single-domain antibodies ...
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Single domain camel antibodies: current status
Reviews in Molecular Biotechnology, 2001The antigen-binding capacity of the paired variable domains of an antibody is well established. The observation that the isolated heavy chains of anti-hapten antibodies retain some antigen-binding capacity in the absence of light chains led to attempts to obtain an even smaller antigen-binding unit in a VH format.
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Bispecific Single Domain Antibodies
2011Monoclonal antibodies are now widely recognized as therapeutic molecules and more than 25 molecules have been approved in the United States and other countries. Despite these successes, the clinical activity of these molecules is still far from optimal and new solutions have to be found, especially in the field of cancer therapy.
Patrick Chames, Daniel Baty
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Production of Single-Domain Antibodies in Pichia pastoris
2022Single-domain antibodies (sdAbs) are binders that consist of a single immunoglobulin domain. SdAbs have gained importance as therapeutics, diagnostic reagents, and research tools. Functional sdAbs are commonly produced in Escherichia coli, which is a simple and widely used host for production of recombinant proteins. However, there are drawbacks of the
Yusei, Matsuzaki +3 more
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Generation of Single-Domain Antibody-Based Recombinant Immunotoxins
2022The discovery of single-domain antibodies has opened new avenues for drug development. Single-domain antibodies, also known as nanobodies, can access buried epitopes that are inaccessible to conventional antibodies. These antigen-binding domains have a high level of solubility and stability, which makes them well suited for therapeutic development ...
Bryan D. Fleming, Mitchell Ho
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Single domain antibody templated nanoparticle resistors for sensing
Biosensors and Bioelectronics, 2010The diversity of biomolecules enables materials to be synthesized at ambient conditions into complex shapes and structures while affording improved control over nanoparticle synthesis, structures, properties, and functionality. Also, biomolecules can impart recognition and sensing capabilities to metal nanoparticles.
Joseph M, Slocik +5 more
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Expression of Single-Domain Antibodies in Bacterial Systems
2012In this chapter we describe in detail the current protocols that are used to express single-domain antibodies in bacteria. Bacteria are among the most common expression systems for expressing recombinant proteins. We present different approaches for carrying out periplasmic and cytoplasmic expression, as well as small-scale and large-scale expression ...
Baral, T.N., Arbabi-Ghahroudi, M.
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Application of Single-Domain Antibodies in Tumor Histochemistry
2012High avidity, pentameric, single-domain antibodies, oligomerized through the B subunit of verotoxin, are excellent immunohistochemical reagents. The resulting molecules are termed pentabodies. Here, we describe the immunostaining of tissue sections with ES1, a pentabody recognizing CEACAM6 which is overexpressed in several cancers.
Maik, K.T., MacKenzie, C.R.
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