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Affinity fusion strategies for detection, purification, and immobilization of recombinant proteins.
Genetic engineering enables the construction of gene man Genome Project (5), efficient and robust production and purification strategies are necessary (6). For fusions resulting in fusion proteinsExpand
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Display of proteins on bacteria.
Display of heterologous proteins on the surface of microorganisms, enabled by means of recombinant DNA technology, has become an increasingly used strategy in various applications in microbiology,Expand
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All individual domains of staphylococcal protein A show Fab binding.
The interactions between the individual domains (E, D, A, B and C) of staphylococcal protein A (SPA) and Fc and Fab regions of human immunoglobulins were studied using real-time biospecificExpand
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Affinity maturation of a Taq DNA polymerase specific affibody by helix shuffling.
The possibility of increasing the affinity of a Taq DNA polymerase specific binding protein (affibody) was investigated by an alpha-helix shuffling strategy. The primary affibody was from a naiveExpand
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The serum albumin‐binding domain of streptococcal protein G is a three‐helical bundle: a heteronuclear NMR study
Streptococcal protein G (SPG) is a cell surface receptor protein with a multiple domain structure containing tandem repeats of serum albumin‐binding domains (ABD) and immunoglobulin‐binding domainsExpand
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The use of gene fusions to protein A and protein G in immunology and biotechnology.
This review describes the use of fusion proteins containing the immunoglobulin-binding domains of staphylococcal protein A (SpA) or the serum albumin-binding regions of streptococcal protein G (SpG),Expand
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Recombinant human factor VIII-specific affinity ligands selected from phage-displayed combinatorial libraries of protein A.
Factor VIII-specific affibodies were selected from phage displayed libraries constructed by combinatorial mutagenesis of an alpha helical bacterial receptor domain derived from staphylococcal proteinExpand
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A combinatorial library of an alpha-helical bacterial receptor domain.
The construction and characterization of a combinatorial library of a solvent-exposed surface of an alpha-helical domain derived from a bacterial receptor is described. Using a novel solid-phaseExpand
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Stabilization of recombinant proteins from proteolytic degradation in Escherichia coli using a dual affinity fusion strategy
A dual affinity fusion approach has been used to study the expression and secretion of labile recombinant proteins in Escherichia coli. Here we show that three small eukaryotic proteins (humanExpand
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Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain.
Small protein domains, capable of specific binding to different target proteins have been selected using combinatorial approaches. These binding proteins, called affibodies, were designed byExpand
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