Results 271 to 280 of about 262,160 (309)
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Purification of recombinant proteins by fusion with thermally-responsive polypeptides
Nature Biotechnology, 1999Elastin-like polypeptides (ELPs) undergo a reversible, inverse phase transition. Below their transition temperature (Tt), ELPs are soluble in water, but when the temperature is raised above Tt, phase transition occurs, leading to aggregation of the polypeptide. We demonstrate a method for purification of soluble fusion proteins incorporating an ELP tag.
D E, Meyer, A, Chilkoti
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Temperature-responsive membrane permeability of recombinant fusion protein vesicles
Soft Matter, 2023In this study, we investigate the changes in the permeability of the recombinant fusion protein vesicles with different membrane structures as a function of solution temperature.
Jackson Powers, Yeongseon Jang
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Cytotoxic Activity of Recombinant bFGF–rViscumin Fusion Proteins
Biochemical and Biophysical Research Communications, 2000A fusion protein (bFGF-rMLA), containing the mitogen basic fibroblast growth factor (bFGF) and the cytotoxic component of rViscumin (recombinant mistletoe lectin), the enzymatic A-chain (rMLA), was expressed in Escherichia coli, purified, and functionally characterized.
A, Schmidt +5 more
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Preparation of Recombinant RNase Single-Chain Antibody Fusion Proteins
Molecular Biotechnology, 2002This article describes the construction, expression, and purification of RNase single-chain antibody fusion proteins. To construct a fusion protein, the gene for each moiety, the RNase and the binding ligand, is modified separately to contain complementary DNA encoding a 13 amino acid spacer that separates the RNase from the binding moiety. Appropriate
D L, Newton, S M, Rybak
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Architecting Multicompartmentalized, Giant Vesicles with Recombinant Fusion Proteins
BiomacromoleculesWe present a straightforward strategy for constructing giant, multicompartmentalized vesicles using recombinant fusion proteins. Our method leverages the self-assembly of globule-zipper-elastin-like polypeptide fusion protein complexes in aqueous conditions, eliminating the need for organic solvents and chemical conjugation.
Jooyong Shin +3 more
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Different Approaches to Stabilize a Recombinant Fusion Protein
Nature Biotechnology, 1989We have used a fusion protein between staphylococcal protein A and E. coli β–galactosidase as a model system to investigate different approaches to stabilize recombinant gene products. First, growth conditions were adapted to preferentially produce insoluble inclusion bodies.
Halldis Hellebust +4 more
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Self-cleaving fusion tags for recombinant protein production
Biotechnology Letters, 2011Fusion expression is a common practice for recombinant protein production. Some fusion tags confer solubility on the target protein whereas others provide affinity handles that facilitate purification. However, the tag usually needs to be removed from the final product, which involves using expensive proteases or hazardous chemicals and requires ...
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Expression and Purification of Recombinant Proteins by Fusion to Maltose-Binding Protein
Molecular Biotechnology, 2000The pMAL vectors provide a method for purifying proteins from cloned genes by fusing them to maltose-binding protein (MBP, product of malE), which binds to amylose. The vectors use the tac promoter and the translation initiation signals of MBP to give high-level expression of the fusion, and an affinity purification for MBP to isolate the fusion ...
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A Polypeptide Fusion Designed for the Purification of Recombinant Proteins
Nature Biotechnology, 1984Recombinant DNA technology was used to produce human urogastrone with a C-terminal polyarginine fusion. This peptide fusion formed the basis of a two-step ion exchange purification that gave 64mg of urogastrone at >95% purity with 44% yield. In the first step, a substantial purification was obtained due to the unusual basicity of the polyarginine-fused
Helmut M. Sassenfeld, Stephen J. Brewer
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Research Progress Fusion Tags for Recombinant Protein Production
Biotechnology and Applied BiochemistryABSTRACTRecombinant proteins are obtained using genetic engineering techniques and are widely used in various fields. Some recombinant proteins are difficult to express, purify, or are unstable or insoluble due to their structural characteristics. In order to address such issues, additional tags are fused at either the N‐ or C‐terminal end of the ...
Jing‐jia Yuan +2 more
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