Results 281 to 290 of about 282,766 (336)

Overview of fusion tags for recombinant proteins

Biochemistry (Moscow), 2016
Virtually all recombinant proteins are now prepared using fusion domains also known as "tags". The use of tags helps to solve some serious problems: to simplify procedures of protein isolation, to increase expression and solubility of the desired protein, to simplify protein refolding and increase its efficiency, and to prevent proteolysis.
E. N. Kosobokova, K. A. Skrypnik, V. S. Kosorukov   +2 more
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Fusion tails for the recovery and purification of recombinant proteins

Protein Expression and Purification, 1991
Several fusion tail systems have been developed to promote efficient recovery and purification of recombinant proteins from crude cell extracts or culture media. In these systems, a target protein is genetically engineered to contain a C- or N-terminal polypeptide tail, which provides the biochemical basis for specificity in recovery and purification ...
Ilari Suominen, Clark Ford, Charles E. Glatz   +2 more
openaire   +3 more sources

Application of Recombinant Fusion Proteins for Tissue Engineering

Annals of Biomedical Engineering, 2010
Extracellular matrix (ECM) plays important roles in tissue engineering because cellular growth and differentiation, in the two-dimensional cell culture as well as in the three-dimensional space of the developing organism, require ECM with which the cells can interact. Also, the development of new synthetic ECMs is very important because ECMs facilitate
Masato Nagaoka, Hu-Lin Jiang, Chong-Su Cho, Takashi Hoshiba, Toshihiro Akaike   +4 more
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Antigenicity of a recombinant Ro (SS‐A) fusion protein

Arthritis & Rheumatism, 1990
AbstractThe antigenicity of the 60‐kd human Ro (SS‐A) synthesized in vitro from its complementary DNA as a β‐galactosidase fusion protein (β‐gal—Ro) was evaluated by Western blotting. In this analysis, almost all the anti‐Ro (SS‐A)‐positive sera that bound β‐gal‐Ro also bound affinity‐purified 60‐kd human Ro (SS‐A) (P > 0.005).
Judith A. James, Judith A. James, W. Daryl Dickey, W. Daryl Dickey, Charles A. O'Brien, Charles A. O'Brien, Susan L. Deutscher, Susan L. Deutscher, Atsushi Fujisaku, Atsushi Fujisaku, John B. Harley, John B. Harley, Jack D. Keene, Jack D. Keene   +13 more
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A Polypeptide Fusion Designed for the Purification of Recombinant Proteins [PDF]

Nature Biotechnology, 1984
Recombinant 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 Max Sassenfeld, Stephen James Brewer   +1 more
openaire   +1 more source

The solubility and stability of recombinant proteins are increased by their fusion to NusA

Biochemical and Biophysical Research Communications, 2004
The new bacterial vector pETM60 enables the expression of His-tagged recombinant proteins fused to the C-terminus of NusA through a TEV protease recognition sequence. Three sequences coding for two protein domains (Xklp3A and Tep3Ag) and one membrane-bound viral protein (E8R) could not be expressed in a soluble form in bacteria.
De Marco, V., Stier, G., Blandin, S., de Marco, A.   +3 more
openaire   +4 more sources

The Use of Recombinant Fusion Proteases in the Affinity Purification of Recombinant Proteins

Molecular Biotechnology, 1999
In the affinity purification of recombinant fusion proteins, the rate-limiting step is usually the efficient proteolytic cleavage and removal of the affinity tail and the protease from the purified recombinant protein. We have developed a rapid, convenient, and efficient method of affinity purification that can overcome this limitation.
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Recombinant Antibody Fusion Proteins for Cancer Immunotherapy

1996
The last decade has seen the extensive development of monoclonal antibodies (mAb) combined with rapid advances in recombinant DNA technologies. These developments have greatly accelerated and expanded research efforts to generate new approaches for cancer therapy.
Ralph A. Reisfeld, Stephen D. Gillies
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Different Approaches to Stabilize a Recombinant Fusion Protein

Nature Biotechnology, 1989
We 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.
Lars Abrahmsén, Halldis Hellebust, Sven-Olof Enfors, Mathias Uhlén, Maria Murby   +4 more
openaire   +2 more sources

Engineering of a recombinant colorimetric fusion protein for immunodiagnosis of insulin

Journal of Immunological Methods, 1996
A synthetic DNA encoding human proinsulin was inserted in frame in the bacterial alkaline phosphatase gene. A homogeneous recombinant human proinsulin-alkaline phosphatase conjugate was obtained directly from the periplasm of Escherichia coli transformed with a plasmid carrying the hybrid gene. The recombinant conjugate was stable and could be produced
Laurent Bellanger, André Ménez, Corinne Chanussot, Patrick Seguin, Caroline Ligny-Lemaire, Jean-Claude Boulain   +5 more
openaire   +3 more sources