نتایج جستجو برای: vhh antibody
تعداد نتایج: 166690 فیلتر نتایج به سال:
To date, no immunization of humans or animals has elicited broadly neutralizing sera able to prevent HIV-1 transmission; however, elicitation of broad and potent heavy chain only antibodies (HCAb) has previously been reported in llamas. In this study, the anti-HIV immune responses in immunized llamas were studied via deep sequencing analysis using broadly neutralizing monoclonal HCAbs as a guid...
New tools for amyloid plaques detection by MRI: Gadolinium-VHH antibody conjugates Matthias Vandesquille, Tengfei Li, Chrystelle Po, Christelle Ganneau, Christian Czech, Charles Duyckaerts, Benoît Delatour, Sylvie Bay, Pierre Lafaye, and Marc Dhenain MIRCen, CEA, Fontenay-aux-Roses, France, Institut Pasteur, Paris, France, ICM, Hôpital de la Pitié-Salpêtrière, Paris, France, Hoffmann-La Roche, ...
A series of expression cassettes which mediate secretion or surface display of antibody fragments was stably integrated in the chromosome of Lactobacillus paracasei. L. paracasei producing surface-anchored variable domain of llama heavy chain (VHH) (ARP1) directed against rotavirus showed efficient binding to rotavirus and protection in the mouse model of rotavirus infection.
Camelids produce functional antibodies devoid of light chains and CH1 domains .The antigen-binding fragment of such heavy-chain antibodies is therefore comprised in one single domain, the VHH. We report here on the structures of three dromadery VHH domains in complex with porcine pancreatic αamylase. Two VHHs bind outside the catalytic site and do not inhibit or inhibit only partially the amyla...
BACKGROUND The 16 kDa heat shock protein (HSP) is an immuno-dominant antigen, used in diagnosis of infectious Mycobacterium tuberculosis (M.tb.) causing tuberculosis (TB). Its use in serum-based diagnostics is limited, but for the direct identification of M.tb. bacteria in sputum or cultures it may represent a useful tool. Recently, a broad set of twelve 16 kDa specific heavy chain llama antibo...
Genetic Incorporation of Non-canonical Amino Acids in Anti-HER2 VHH: Expression and Characterization
Nanobodies– or VHH– are small proteins (~120 residues) issued from antibodies with an intact recognition for the original target of antibody. In present study, we show possibility incorporating non-canonical amino acids at precise location sequence via classical genetic techniques (Genetic Code Expansion). We demonstrate that amount recombinant protein obtained is compatible large production fo...
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. HCAbs fail to incorporate light (L) chains owing to the deletion of the first constant domain and a reshaped surface at the VHH side, which normally ...
BACKGROUND Recombinant antibodies are powerful tools in engineering of novel diagnostics. Due to the small size and stable nature of llama antibody domains selected antibodies can serve as a detection reagent in multiplexed and sensitive assays for M. tuberculosis. METHODOLOGY/PRINCIPAL FINDINGS Antibodies for Mycobacterium tuberculosis (M. tb) recognition were raised in Alpaca, and, by phage...
The soluble epoxide hydrolase (sEH) is a potential pharmacological target for treating hypertension, vascular inflammation, pain, cancer, and other diseases. However, there is not a simple, inexpensive, and reliable method to estimate levels of active sEH in tissues. Toward developing such an assay, a polyclonal variable domain of heavy chain antibody (VHH) sandwich immunoassay was developed. T...
Nanobodies (Nbs) are the smallest functional antibody fragments known in nature and have multiple applications in biomedicine or environmental monitoring. Nbs are derived from the variable segment of camelid heavy chain-only antibodies, known as VHH. For selection, libraries of VHH gene segments from naïve, immunized animals or of synthetic origin have been traditionally cloned in E. coli phage...
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