Results 261 to 270 of about 478,505 (298)
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Journal of Molecular Recognition, 1999
The humoral immune response of camels, dromedaries and llamas includes functional antibodies formed by two heavy chains and no light chains. The amino acid sequence of the variable domain of the naturally occurring heavy-chain antibodies reveals the necessary adaptations to compensate for the absence of the light chain.
Serge Muyldermans, Marc Lauwereys
exaly +5 more sources
The humoral immune response of camels, dromedaries and llamas includes functional antibodies formed by two heavy chains and no light chains. The amino acid sequence of the variable domain of the naturally occurring heavy-chain antibodies reveals the necessary adaptations to compensate for the absence of the light chain.
Serge Muyldermans, Marc Lauwereys
exaly +5 more sources
Matrix-Assisted Refolding of Single-Chain Fv– Cellulose Binding Domain Fusion Proteins
Protein Expression and Purification, 1999We describe a method for the isolation of recombinant single-chain antibodies in a biologically active form. The single-chain antibodies are fused to a cellulose binding domain as a single-chain protein that accumulates as insoluble inclusion bodies upon expression in Escherichia coli.
Yevgeny Berdichevsky +2 more
exaly +3 more sources
Enzyme and Microbial Technology, 1997
Trichoderma reesei cellobiohydrolase I (CBHI) and Cellulomonas fimi cellulase-xylanase (Cex) both have distinct C-terminal cellulose-binding domains which belong to different CBD sequence families. Two fusion proteins comprising a single-chain antibody fragment (OxscFv) against 2-phenyloxazolone fused to the two CBDs (CBDCBHI or CBDCex) were ...
Tapani Reinikainen +2 more
exaly +5 more sources
Trichoderma reesei cellobiohydrolase I (CBHI) and Cellulomonas fimi cellulase-xylanase (Cex) both have distinct C-terminal cellulose-binding domains which belong to different CBD sequence families. Two fusion proteins comprising a single-chain antibody fragment (OxscFv) against 2-phenyloxazolone fused to the two CBDs (CBDCBHI or CBDCex) were ...
Tapani Reinikainen +2 more
exaly +5 more sources
Analytical Chemistry, 2010
Single domain antibodies are the recombinantly expressed binding fragments derived from heavy chain antibodies found in camels and llamas. These unique binding elements offer many desirable properties such as their small size ( approximately 15 kDa) and thermal stability, which makes them attractive alternatives to conventional monoclonal antibodies ...
George P Anderson +2 more
exaly +3 more sources
Single domain antibodies are the recombinantly expressed binding fragments derived from heavy chain antibodies found in camels and llamas. These unique binding elements offer many desirable properties such as their small size ( approximately 15 kDa) and thermal stability, which makes them attractive alternatives to conventional monoclonal antibodies ...
George P Anderson +2 more
exaly +3 more sources
Protein Expression and Purification, 2000
The expression of single-chain Fv fragments (scFv) targeted to the periplasm of Escherichia coli often results in very low yields of soluble protein frequently accompanied by host cell growth arrest and sometimes lysis. Single-chain antibody fragments (scAb) are scFv with a human kappa light chain constant (HuCkappa) domain attached C-terminally and ...
Andrew Hayhurst
exaly +3 more sources
The expression of single-chain Fv fragments (scFv) targeted to the periplasm of Escherichia coli often results in very low yields of soluble protein frequently accompanied by host cell growth arrest and sometimes lysis. Single-chain antibody fragments (scAb) are scFv with a human kappa light chain constant (HuCkappa) domain attached C-terminally and ...
Andrew Hayhurst
exaly +3 more sources