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Now showing items 1-10 of 12
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2010)
Background
Whereas T cell receptors (TCRs) detect peptide/major histocompatibility complexes (pMHCs) with exquisite specificity, there are challenges regarding their expression and use as soluble detection ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2011)
Background: Phage display is a leading technology for selection of binders with affinity for specific target molecules. Polypeptides are normally displayed as fusions to the major coat protein VIII (pVIII) or the minor ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2011)
Human IgG3 displays the strongest effector functions of all IgG subclasses but has a short half-life for unresolved reasons. Here we show that IgG3 binds to IgG-salvage receptor (FcRn), but that FcRn-mediated transport and ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2012)
Phage display has been instrumental in discovery of novel binding peptides and folded domains for the past two decades. We recently reported a novel pIX phagemid display system that is characterized by a strong preference ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2010)
Background
Efficient expression systems exist for antibody (Ab) molecules, which allow for characterization of large numbers of individual Ab variants. In contrast, such expression systems have been lacking ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2011)
The success of Fc-fusion bio-therapeutics has spurred the development of other Fc-fusion products for treating and/or vaccinating against a range of diseases. We describe a method to modulate their function by converting ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2011)
Background: Phage display is a platform for selection of specific binding molecules and this is a clear-cut motivation for increasing its performance. Polypeptides are normally displayed as fusions to the major coat protein ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2012)
Serum half-life of IgG is controlled by the neonatal Fc receptor (FcRn) that interacts with the IgG Fc region and may be increased or decreased as a function of altered FcRn binding. Preclinical evaluations of modified ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2012)
Albumin is the most abundant protein in blood where it has a pivotal role as a transporter of fatty acids and drugs. Like IgG, albumin has long serum half-life, protected from degradation by pH-dependent recycling mediated ...
(Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2010)
The neonatal Fc receptor (FcRn) regulates the serum half-life of both IgG and albumin through a pH-dependent mechanism that involves salvage from intracellular degradation. Therapeutics and diagnostics built on IgG, Fc, ...