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Search Results for "Refolding Hydrophobic Protein"

18:16 EDT 21st May 2013 | BioPortfolio

Original Source: Ion-exchange resins facilitate like-charged protein refolding: Effects of porous solid phase properties.

We have previously found that addition of charged particles in a refolding solution can greatly increase the refolding yield of like-charged proteins. Herein, porous anion exchangers of different charged group densities, ligand chemistries, pore sizes and particle sizes were prepared with Sepharose FF gel for studying their effects on the oxidative refolding of like-charged lysozyme. We found that charge density had significant contribution to the enhancing effects on lysozyme refolding. At low resin concen...

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Lonza signs deal to evaluate BaroFold PreEMT high pressure refolding technology

Lonza has signed an agreement to assess BaroFold's PreEMT high pressure protein refolding technology against traditional refolding methods used in biological development refolding processes.

Protein refolding using chemical refolding additives

In laboratories and manufacturing settings, a rapid and inexpensive method for the preparation of a target protein is crucial for promoting resesrach in protein science and engineering. Inclusion‐bo...

Lonza to Evaluate BaroFold’s Protein Refolding Technology

Lonza has agreed to evaluate BaroFold’s high-pressure refolding technology for difficult to express microbial products expressed as inclusion bodies.

BaroFold and Boehringer Ingelheim announce strategic alliance for protein refolding technology

BaroFold and Boehringer Ingelheim have entered into a non-exclusive technology and commercial license option agreement.Boehringer Ingelheim will acquire a laboratory-scale reactor of BaroFold’s Pres...

BaroFold and Lonza Announce a Technology Evaluation Agreement for PreEMT

AURORA, Colo. & BASEL, Switzerland--(BUSINESS WIRE)--Lonza, a leader in biological development, and BaroFold, Inc., an innovative protein technology developer, announced today a non-exclusive tech...

Boehringer Ingelheim and BaroFold Announce Strategic Agreement on PreEMT™ High Pressure Protein Refolding Technology

Boehringer Ingelheim to license PreEMT protein refolding technology

Will install a laboratory-scale reactor at its microbial facility in Vienna, Austria

BaroFold and Lonza sign evaluation agreement for protein refolding technology

Lonza will focus on effectiveness of PreEMT for difficult to express microbial recombinant proteins

Matching PubMed Articles

Efficient refolding of a hydrophobic protein with multiple S-S bonds by on-resin immobilized metal affinity chromatography.

The efficient refolding of recombinant proteins produced in the form of inclusion bodies (IBs) in Escherichia coli still is a complicated experimental problem especially for large hydrophobic highly d...

Protein Refolding by N-Alkylpyridinium and N-Alkyl-N-methylpyrrolidinium Ionic Liquids.

An important property of ionic liquids consisting of cations and anions is that the chemical structures can be easily tuned. To expand the repertoire of effective ionic liquid-based refolding additive...

Mechanism of Gemini Disulfide Detergent Mediated Oxidative Refolding of Lysozyme in a New Artificial Chaperone System.

Gemini surfactants are a new class of surfactants that consist of two hydrophilic head groups and two hydrophobic tails separated by a spacer group. As the properties of geminis are different to their...

Synergistic effects of detergents and organic solvents on protein refolding: Control of aggregation and folding rates.

This paper presents the synergistic enhancement of the refolding yield of denatured and reduced lysozyme by using detergents as aggregation inhibitors and water-miscible organic cosolvents as modulato...

Experimental optimization of protein refolding with a genetic algorithm.

Refolding of proteins from solubilized inclusion bodies still represents a major challenge for many recombinantly expressed proteins and often constitutes a major bottleneck. As in vitro refolding is...

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