Results 141 to 150 of about 1,618 (161)
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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
Immunology Letters, 2006
We have employed a novel mutagenesis system, which utilizes an error-prone RNA dependent RNA polymerase from Qbeta bacteriophage, to create a diverse library of single domain antibody fragments based on the shark IgNAR antibody isotype. Coupling of these randomly mutated mRNA templates directly to the translating ribosome allowed in vitro selection of ...
George, Kopsidas +4 more
openaire +2 more sources
We have employed a novel mutagenesis system, which utilizes an error-prone RNA dependent RNA polymerase from Qbeta bacteriophage, to create a diverse library of single domain antibody fragments based on the shark IgNAR antibody isotype. Coupling of these randomly mutated mRNA templates directly to the translating ribosome allowed in vitro selection of ...
George, Kopsidas +4 more
openaire +2 more sources
Molecular Immunology, 2003
The novel immunoglobulin isotype novel antigen receptor (IgNAR) is found in cartilaginous fish and is composed of a heavy-chain homodimer that does not associate with light chains. The variable regions of IgNAR function as independent domains similar to those found in the heavy-chain immunoglobulins of Camelids. Here, we describe the successful cloning
Helen, Dooley +2 more
openaire +2 more sources
The novel immunoglobulin isotype novel antigen receptor (IgNAR) is found in cartilaginous fish and is composed of a heavy-chain homodimer that does not associate with light chains. The variable regions of IgNAR function as independent domains similar to those found in the heavy-chain immunoglobulins of Camelids. Here, we describe the successful cloning
Helen, Dooley +2 more
openaire +2 more sources
Fish & Shellfish Immunology, 2019
Cartilaginous fish are the evolutionarily oldest group of animals which possess antibodies, T cell receptors and major histocompatibility complex (MHC). The immunoglobulin novel antigen receptor (IgNAR) found in cartilaginous fish is a heavy chain homodimer which lacks light chain.
D.P.N. De Silva +7 more
openaire +2 more sources
Cartilaginous fish are the evolutionarily oldest group of animals which possess antibodies, T cell receptors and major histocompatibility complex (MHC). The immunoglobulin novel antigen receptor (IgNAR) found in cartilaginous fish is a heavy chain homodimer which lacks light chain.
D.P.N. De Silva +7 more
openaire +2 more sources
IgNAR characterization and gene loci identification in whitespotted bamboo shark () genome
Fish and Shellfish Immunology, 2023Xiaofeng Jiang, Guodong Chen, Bo Zhong
exaly
Sequence structure character of IgNAR Sec in whitespotted bamboo shark ()
Fish and Shellfish Immunology, 2020Guiqian Chen +2 more
exaly