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VHH characterization. Comparison of recombinant with chemically synthesized anti‐HER2 VHH [PDF]
Protein Science, 2019 AbstractIn the continuous exploration of the VHH chemistry, biochemistry and therapeutic future use, we investigated two different production strategies of this small antibody‐like protein, using an anti‐HER2 VHH as a model. The total chemical synthesis of the 125 amino‐acid peptide was performed with reasonable yield, even if optimization will be ...
Thomas Botzanowski +2 more
exaly +5 more sources
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Construction of Synthetic VHH Libraries in Ribosome Display Format.
Methods in molecular biology, 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.
Audrey Guilbaud, F. Pecorari
semanticscholar +5 more sources
Cancer Research, 2023
Heterogeneous antigen expression is a key barrier influencing the activity of chimeric antigen receptor (CAR) T cells in solid tumors. Here, we developed CAR T cells targeting glypican-1 (GPC1), an oncofetal antigen expressed in pancreatic cancer.
Nan Li +7 more
semanticscholar +1 more source
Heterogeneous antigen expression is a key barrier influencing the activity of chimeric antigen receptor (CAR) T cells in solid tumors. Here, we developed CAR T cells targeting glypican-1 (GPC1), an oncofetal antigen expressed in pancreatic cancer.
Nan Li +7 more
semanticscholar +1 more source
Small-Scale Secretory VHH Expression in Saccharomyces cerevisiae.
Methods in molecular biology, 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 ...
M. Harmsen +2 more
semanticscholar +3 more sources
International Immunology, 2022 Abstract Antigen-combining sites of the camelid heavy-chain antibody variable domain (VHH) are constructed by three complementarity-determining regions (CDR1, CDR2 and CDR3). We prepared cDNA using mRNA extracted from peripheral lymphocytes of alpacas that had been non-immunized or immunized with human serum albumin (HSA).
Narutoshi Tsukahara +7 more
semanticscholar +3 more sources
Ultrasensitive and rapid colorimetric detection of paraquat via a high specific VHH nanobody.
Biosensors & bioelectronics, 2022Rapid and quantitative detection of paraquat is crucial because of its high toxicity. Here, we developed an ultrasensitive time-resolved fluorescence immunochromatographic assay (TRFICA) strip based on our synthesized variable domain of heavy chain ...
Yongyi Zhang +8 more
semanticscholar +1 more source
Quality assessment of VHH models
Journal of Biomolecular Structure and Dynamics, 2023Heavy Chain Only Antibodies are specific to Camelid species. Despite the lack of the light chain variable domain, their heavy chain variable domain (VH) domain, named VHH or nanobody, has promising potential applications in research and therapeutic ...
A. Nadaradjane +7 more
semanticscholar +1 more source
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
openaire +3 more sources