Results 201 to 210 of about 610,444 (251)
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Single domain camel antibodies: current status

Reviews in Molecular Biotechnology, 2001
The 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.
Serge Muyldermans
exaly   +4 more sources

Improving the targeting of therapeutics with single-domain antibodies

Expert Opinion on Drug Delivery, 2016
The targeted delivery of therapeutic agents greatly increases their effectiveness while simultaneously reducing negative side effects. In the past, targeting of therapeutics has been accomplished with nucleic acids, peptides/proteins, and conventional antibodies. A promising alternative to the conventional antibodies often used in therapeutic targeting
Kendrick Turner   +2 more
exaly   +3 more sources

Single-Domain Antibody Theranostics on the Horizon

Journal of Nuclear Medicine, 2022
Single-domain antibody (sdAb) is among the most promising vectors for developing molecular imaging tracers. Several sdAb tracers targeting human epidermal growth factor receptor 2 or programmed death ligand 1 have entered clinical practice. However, radiolabeled single-valent sdAbs generally have high kidney retention, limiting their therapeutic ...
Weijun, Wei   +4 more
openaire   +2 more sources

Multivalent Display of Single-Domain Antibodies

2012
Antigen-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.
openaire   +3 more sources

Single-domain antibodies

2009
The antigen-binding entity of an antibody, reduced in size to one single domain, is referred to as a "single-domain antibody". Various strategies have been explored with variable success to arrive at functional sinlge-domain antibodies. The potential of single-domain antibodies, as research tools or in medicine, is reflected by the three companies ...
Muyldermans, Serge   +2 more
openaire   +3 more sources

Humanization of Camelid Single-Domain Antibodies

2022
Humanization 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 ...
openaire   +2 more sources

Production of Single-Domain Antibodies in Pichia pastoris

2022
Single-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
openaire   +2 more sources

Expression of Single-Domain Antibodies in Bacterial Systems

2012
In 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.
openaire   +3 more sources

Single-Domain Antibodies or Nanobodies: A Class of Next-Generation Antibodies

International Reviews of Immunology, 2018
Nanobodies for the first time were identified in the sera of Camelidae. Single-domain antibodies or nanobodies are a class of next-generation antibodies that have specific features: small size (in nanoscale), high penetration in various tissues, high stability in hard situations and ease production process in microbial systems.
Farnaz Khodabakhsh   +3 more
openaire   +2 more sources

Application of Single-Domain Antibodies in Tumor Histochemistry

2012
High 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.
openaire   +2 more sources

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