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A tool to pulse-label yeast Nuclear Pore Complexes in imaging and biochemical experiments
Veldsink AC +4 more
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Small-Scale Secretory VHH Expression in Saccharomyces cerevisiae
2022After isolation of a single-domain antibody (VHH) binding to an antigen of interest, the soluble VHH is often produced in Escherichia coli. However, targeting VHH expression to the secretory pathway of Saccharomyces cerevisiae (baker's yeast) enables the secretion of correctly folded, soluble, disulfide-bonded, and N-glycosylated VHHs into the culture ...
Harmsen, Michiel M. +2 more
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Selection of VHHs Under Application Conditions
2012The successful application of antibody fragments such as VHHs in diagnostic assays, affinity purification, imaging, or therapy is not determined by the specificity and affinity of the antibody fragment alone. The ability to bind the target protein in the environment in which the antibody fragment is intended to functionally perform determines to a ...
Dolk, E. +2 more
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Construction of Synthetic VHH Libraries in Ribosome Display Format
2023Single-domain antibodies, or VHH, represent an attractive molecular basis to design affinity proteins with favorable properties. Beyond high affinity and specificity for their cognate target, they usually show high stability and high production yields in bacteria, yeast, or mammalian cells.
Guilbaud, Audrey, Pecorari, Frédéric
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Expression of VHHs in Saccharomyces cerevisiae
2012The production of VHHs in microorganisms is relatively straightforward, however the amount of VHH produced per volume unit can vary substantially from hardly detectable to hundreds of milligrams per liter. Expression in Escherichia coli is more commonly used at initial research phase, since production of VHHs for large-scale application in E.
Andrea, Gorlani +2 more
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Production of Designer VHH-Based Antibodies in Plants
2022Simplified monoclonal antibodies can be produced by fusing a VHH or nanobody, derived from camelid heavy-chain-only antibodies to the Fc domain of either IgG (VHH-IgG), IgA (VHH-IgA), or IgY (VHH-IgY). These recombinant antibodies are encoded by a single gene and their production can be easily scaled up in plants.
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2022
The present disclosure relates to field of immune checkpoints in onco-immunology and their identification as potential targets for the treatment of cancer patients : it provides VHHs (Single-domain antibody fragments, also known as 'heavy-chain variable domains' or 'nanobodies') to detect and quantify in a non-invasive way the immune checkpoint LAG-3.
Breckpot, Karine +5 more
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The present disclosure relates to field of immune checkpoints in onco-immunology and their identification as potential targets for the treatment of cancer patients : it provides VHHs (Single-domain antibody fragments, also known as 'heavy-chain variable domains' or 'nanobodies') to detect and quantify in a non-invasive way the immune checkpoint LAG-3.
Breckpot, Karine +5 more
openaire +4 more sources
Structure and Function of Camelid VHH
2016The humoral immune response of camels and llama’s is unique in containing two types of IgG antibodies: classical heterotetrameric and homodimeric heavy chain-only antibodies (HCAbs). Remarkably, these heavy chain antibodies are functional in antigen binding and reach high titers and affinities after immunizing a camelid. Antigen recognition by HCAbs is
Vincke, Cecile, Muyldermans, Serge
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