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Nanobodies: Natural Single-Domain Antibodies

Annual Review of Biochemistry, 2013
Sera of camelids contain both conventional heterotetrameric antibodies and unique functional heavy (H)-chain antibodies (HCAbs). The H chain of these homodimeric antibodies consists of one antigen-binding domain, the VHH, and two constant domains.
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

Engineering pH-Sensitive Single-Domain Antibodies

2022
There is increasing interest in expanding an antibody beyond high affinity and specificity. One such feature is custom regulation of the binding event, such as pH-dependent control. Here, we provide a methodology for generating single-domain antibodies (sdAbs) that bind their antigen in a pH-dependent fashion.
Tosha M, Laughlin, James R, Horn
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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
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Expression of single-domain antibody in different systems

Applied Microbiology and Biotechnology, 2017
Camelid single-domain antibodies (sdAbs, VHHs, or Nanobodies®) are types of antibody fragments that are composed of the heavy-chain variable domain only. These VHHs possess unique structural and functional features, as they are small in size and exhibit thermal stability and high solubility. Compared to conventional antibodies, VHHs can be manufactured
Ping Song
exaly   +3 more sources

Single-Domain Antibodies for Intracellular Toxin Neutralization

2022
Ricin 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
openaire   +2 more sources

Engineered antibody fragments and the rise of single domains

Nature Biotechnology, 2005
With 18 monoclonal antibody (mAb) products currently on the market and more than 100 in clinical trials, it is clear that engineered antibodies have come of age as biopharmaceuticals. In fact, by 2008, engineered antibodies are predicted to account for >30% of all revenues in the biotechnology market. Smaller recombinant antibody fragments (for example,
Philipp, Holliger, Peter J, Hudson
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

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 B, Turner   +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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