Results 91 to 100 of about 350 (116)
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Fish & Shellfish Immunology, 2023
The development of recombinant antibody fragments as promising alternatives to full-length immunoglobulins offers vast opportunities for biomedicine. Antibody fragments have important advantages compared with conventional monoclonal antibodies that make them attractive for the biotech industry: superior stability and solubility, reduced immunogenicity,
Karen, Manoutcharian, Goar, Gevorkian
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The development of recombinant antibody fragments as promising alternatives to full-length immunoglobulins offers vast opportunities for biomedicine. Antibody fragments have important advantages compared with conventional monoclonal antibodies that make them attractive for the biotech industry: superior stability and solubility, reduced immunogenicity,
Karen, Manoutcharian, Goar, Gevorkian
openaire +2 more sources
Cytoplasmic and periplasmic expression of recombinant shark VNAR antibody in Escherichia coli
Preparative Biochemistry and Biotechnology, 2019Shark variable new antigen receptors (VNARs) are known to possess excellent heat-stability, and the long complementarity determining region 3 (CDR3) has permitted it to penetrate into the cleft region of antigens. The number of cysteine (Cys) residues contained within VNAR is greater than in conventional antibodies, entailing disulfide bond formation ...
Herng C. Leow +5 more
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Journal of Biotechnology, 2014
A novel method for stepwise in vitro affinity maturation of antigen-specific shark vNAR domains is described that exclusively relies on semi-synthetic repertoires derived from non-immunized sharks. Target-specific molecules were selected from a CDR3-randomized bamboo shark (Chiloscyllium plagiosum) vNAR library using yeast surface display as platform ...
Stefan, Zielonka +13 more
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A novel method for stepwise in vitro affinity maturation of antigen-specific shark vNAR domains is described that exclusively relies on semi-synthetic repertoires derived from non-immunized sharks. Target-specific molecules were selected from a CDR3-randomized bamboo shark (Chiloscyllium plagiosum) vNAR library using yeast surface display as platform ...
Stefan, Zielonka +13 more
openaire +2 more sources
Generation of VNAR Libraries from Immunized Sharks and Selection of Target-Specific Clones
2021Cartilaginous fishes (sharks, skates, rays, and chimeras) are the most phylogenetically distant lineage relative to mammals in which somatically rearranging immunoglobulins (Igs or antibodies) have also been found. Alongside their conventional (heavy-light chain) isotypes, IgM and IgW, sharks produce the novel isotype, IgNAR, a heavy-chain homodimer ...
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In Vitro Maturation of a Humanized Shark VNAR Domain to Improve Its Biophysical Properties
2019VNAR domains are the binding regions of new antigen receptor proteins (IgNAR) which are unique to sharks, skates, and rays (Elasmobranchii). Individual VNAR domains can bind antigens independently and are the smallest reported adaptive immune recognition entities in the vertebrate kingdom.
John, Steven +6 more
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Methods in Molecular Biology, 2018
The adaptive immune system of sharks comprises a heavy chain-only antibody isotype, referred to as immunoglobulin new antigen receptor (IgNAR). Antigen binding in case of IgNAR antibodies is mediated by a single variable domain (vNAR). Due to their inherent beneficial biophysical properties, such as small size and high thermal stability combined with a
Stefan Zielonka +2 more
exaly +3 more sources
The adaptive immune system of sharks comprises a heavy chain-only antibody isotype, referred to as immunoglobulin new antigen receptor (IgNAR). Antigen binding in case of IgNAR antibodies is mediated by a single variable domain (vNAR). Due to their inherent beneficial biophysical properties, such as small size and high thermal stability combined with a
Stefan Zielonka +2 more
exaly +3 more sources
Abstract 576: Shark VNAR single domain-based CAR T cells targeting PD-L1 for cancer therapy
Cancer Research, 2022Abstract Background: Chimeric antigen receptor (CAR)-T therapy shows great potency against hematological malignancies, whereas it is difficult to transfer CAR T into solid tumors due to lack of appropriate antigenic targets and immunosuppressive tumor microenvironment.
Dan Li +6 more
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A shark VNAR-IL-15 fusion protein that suppresses TROP2+ tumor growth
International Journal of Biological MacromoleculesInterleukin-15 (IL-15) holds great promise for cancer immunotherapy because it selectively activates cytotoxic immune cells without expanding regulatory T cells. It also has the potential to convert "cold" tumors into more immunologically active ones. However, its clinical utility is limited by systemic toxicity.
Zhongqiu, Wu +5 more
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International Journal of Biological Macromolecules
Since recombinant biotherapeutics were accepted in the therapeutic drug market, one of the significant challenges has been the insufficient circulatory half-life of many protein and peptide-based drugs. To overcome this pharmacokinetic limitation, serum albumin has been widely utilized as a molecular carrier due to its intrinsic FcRn-mediated recycling
Yuchao Gu
exaly +3 more sources
Since recombinant biotherapeutics were accepted in the therapeutic drug market, one of the significant challenges has been the insufficient circulatory half-life of many protein and peptide-based drugs. To overcome this pharmacokinetic limitation, serum albumin has been widely utilized as a molecular carrier due to its intrinsic FcRn-mediated recycling
Yuchao Gu
exaly +3 more sources
Hybridoma, 2011
In addition to conventional antibodies, cartilaginous fish have evolved a distinctive type of immunoglobulin, designated as IgNAR, which lacks the light polypeptide chains and is composed entirely by heavy chains. IgNAR molecules can be manipulated by molecular engineering to produce the variable domain of a single heavy chain polypeptide (vNARs ...
Karla, Juarez +6 more
openaire +2 more sources
In addition to conventional antibodies, cartilaginous fish have evolved a distinctive type of immunoglobulin, designated as IgNAR, which lacks the light polypeptide chains and is composed entirely by heavy chains. IgNAR molecules can be manipulated by molecular engineering to produce the variable domain of a single heavy chain polypeptide (vNARs ...
Karla, Juarez +6 more
openaire +2 more sources

