Results 261 to 270 of about 852,815 (296)

Binding Kinetics of Antiricin Single Domain Antibodies and Improved Detection Using a B Chain Specific Binder

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, Rachael D, Bernstein, Marla D, Swain, Dan, Zabetakis, Ellen R, Goldman   +4 more
openaire   +4 more sources

Improved Expression Characteristics of Single-Chain Fv Fragments When Fused Downstream of the Escherichia coli Maltose-Binding Protein or Upstream of a Single Immunoglobulin-Constant Domain

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
openaire   +4 more sources

Matrix-Assisted Refolding of Single-Chain Fv– Cellulose Binding Domain Fusion Proteins

Protein Expression and Purification, 1999
We 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.
Y, Berdichevsky, R, Lamed, D, Frenkel, U, Gophna, E A, Bayer, S, Yaron, Y, Shoham, I, Benhar   +7 more
openaire   +2 more sources

Building novel binding ligands to B7.1 and B7.2 based on human antibody single variable light chain domains.

Journal of molecular biology, 2001
Ligands specific for B7.1 (CD80) and B7.2 (CD86) have applications in disease indications that require inhibition of T-cell activity. As we observed significant sequence and structural similarity between the B7-binding ligand, cytotoxic T-lymphocyte associated protein-4 (CTLA-4), and antibody variable light chain domains (VLs), we have explored the ...
T, van den Beucken, N, van Neer, E, Sablon, J, Desmet, L, Celis, H R, Hoogenboom, S E, Hufton   +6 more
openaire   +2 more sources

Single-chain repressors containing Engineered DNA-binding domains of the phage 434 repressor recognize symmetric or asymmetric DNA operators

Journal of Molecular Biology, 1997
Single-chain (sc) DNA-binding proteins containing covalently dimerized N-terminal domains of the bacteriophage 434 repressor cI have been constructed. The DNA-binding domains (amino acid residues 1 to 69) were connected in a head-to-tail arrangement with a part of the natural linker sequence that connects the N and C-terminal domains of the intact ...
A, Simoncsits, J, Chen, P, Percipalle, S, Wang, I, Törö, S, Pongor   +5 more
openaire   +2 more sources

Comparison of the adsorption properties of a single-chain antibody fragment fused to a fungal or bacterial cellulose-binding domain

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 ...
Reinikainen, Tapani, Takkinen, Kristiina, Teeri, Tuula   +3 more
openaire   +4 more sources

Nanobodies, Single-Domain Antigen-Binding Fragments of Camelid Heavy-Chain Antibodies

2009
Antibodies or immunoglobulins are glycoproteins produced by B-cells and play a central role in host immune defense. Antibodies can be elicited virtually against any substance. Moreover, the immune response to any given antigen can be diverse, comprising different antibodies exhibiting different affinities and/or epitope specificities.
Gholamreza Hassanzadeh Ghassabeh, Serge Muyldermans, Dirk Saerens   +2 more
openaire   +1 more source

Cloning, high-level expression, single-step purification, and binding activity of His6-tagged recombinant type B botulinum neurotoxin heavy chain transmembrane and binding domain

Protein Expression and Purification, 2004
Botulinum neurotoxins (BoNTs) are highly potent toxins that inhibit neurotransmitter release from peripheral cholinergic synapses and associate with infant botulism. BoNT is a approximately 150kDa protein, consisting of a binding/translocating heavy chain (HC; 100kDa) and a toxifying light chain (LC; 50kDa) linked through a disulfide bond.
Yu, Zhou, Bal Ram, Singh
openaire   +2 more sources

[Cloning and expression of a single human immunoglobulin heavy-chain variable domain with vascular endothelial growth factor binding activity].

Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2012
In the application of therapeutic antibodies, large molecular weight of antibodies is always a problem that prevents them from penetrating into tissues or binding to antigenic determinants. To overcome this problem, we investigated the function of the heavy chain variable domain of a monoclonal anti-VEGF human IgM antibody derived from the Five-Feature
Heng, Liu, Siguo, Liu, Yi, Wu, M, Zili, Yu, Liu, Aimin, Zhang, Jianquan, Chen, Guoxiang, Cheng   +7 more
openaire   +2 more sources

A recombinant single-chain HLA-A2.1 molecule, with a cis active β-2-microglobulin domain, is biologically active in peptide binding and antigen presentation

Human Immunology, 1996
We have constructed a recombinant single-chain human HLA-A2.1 molecule (from A*0201) with a covalently attached beta 2m. This molecule (MSC beta A2.1) can be detected on the surface of transfected beta 2m- human cells by conformational antibodies W6/32 and BB7.2 and by anti-human beta 2m mAb BM-63.
L, Lee, D, Loftus, E, Appella, D H, Margulies, M, Mage   +4 more
openaire   +2 more sources