Results 271 to 280 of about 478,505 (298)

On the interaction between single chain Fv antibodies and bacterial immunoglobulin-binding proteins

open access: yesJournal of Immunological Methods, 1994
Using four bacterial immunoglobulin-binding proteins, we have analyzed the binding characteristics of a panel of 34 human single chain Fv antibodies, expressed in E. coli and with known specificity and sequence.
Bo Åkerström   +2 more
exaly   +3 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   +6 more
openaire   +3 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   +2 more
openaire   +1 more source

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   +5 more
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   +7 more
openaire   +2 more sources

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

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   +4 more
openaire   +2 more sources

Increased Stability and DNA Site Discrimination of “Single Chain” Variants of the Dimeric β-Barrel DNA Binding Domain of the Human Papillomavirus E2 Transcriptional Regulator

Biochemistry, 2007
Human papillomavirus infects millions of people worldwide and is a causal agent of cervical cancer in women. The HPV E2 protein controls the expression of all viral genes through binding of its dimeric C-terminal domain (E2C) to its target DNA site. We engineered monomeric versions of the HPV16 E2C, in order to probe the link of the dimeric beta-barrel
Mariano, Dellarole   +3 more
openaire   +2 more sources

Targeting retrovirus to cancer cells expressing a mutant EGF receptor by insertion of a single chain antibody variable domain in the envelope glycoprotein receptor binding lobe

Journal of Immunological Methods, 2000
We have investigated targeting of retroviral vectors to a mutant EGF receptor (EGFRvIII) that is expressed in cancers of the brain, breast, lung and ovary, but is not found in any normal tissues. An expression plasmid was made in which a single chain Fv antibody specific for EGFRvIII was inserted at a novel position within a disulphide-bonded surface ...
I A, Lorimer, S J, Lavictoire
openaire   +2 more sources

Backbone and side-chain 1H, 13C and 15N resonance assignments of the OB domain of the single stranded DNA binding protein from Sulfolobus solfataricus and chemical shift mapping of the DNA-binding interface

Biomolecular NMR Assignments, 2013
Single stranded DNA binding proteins (SSBs) are present in all known cellular organisms and are critical for DNA replication, recombination and repair. The SSB from the hyperthermophilic crenarchaeote Sulfolobus solfataricus (SsoSSB) has an unusual domain structure with a single DNA-binding oligonucleotide binding (OB) fold coupled to a flexible C ...
Gamsjaeger, Roland (R16936)   +5 more
openaire   +2 more sources

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