Results 251 to 260 of about 391,068 (308)

Recombinant avidin and avidin–fusion proteins

Biomolecular Engineering, 1999
Both chicken egg-white avidin and its bacterial relative streptavidin are well known for their extraordinary high affinity with biotin (Kd approximately 10(-15) M). They are widely used as tools in a number of affinity-based separations, in diagnostic assays and in a variety of other applications. These methods have collectively become known as (strept)
K J, Airenne, V S, Marjomäki, M S, Kulomaa   +2 more
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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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Temperature-responsive membrane permeability of recombinant fusion protein vesicles

Soft Matter, 2023
In 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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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.
R A, Reisfeld, S D, Gillies
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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, Takashi, Hoshiba, Toshihiro, Akaike, Chong-Su, Cho   +4 more
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Cytotoxic Activity of Recombinant bFGF–rViscumin Fusion Proteins

Biochemical and Biophysical Research Communications, 2000
A 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, B, Möckel, J, Eck, M, Langer, M, Gauert, H, Zinke   +5 more
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Preparation of Recombinant RNase Single-Chain Antibody Fusion Proteins

Molecular Biotechnology, 2002
This 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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Population pharmacokinetics of recombinant factor VIII Fc fusion protein

Clinical Pharmacology in Drug Development, 2014
AbstractPopulation pharmacokinetics (PK) of FVIII activity‐time profiles following recombinant factor VIII Fc fusion protein (rFVIIIFc) and recombinant factor VIII (rFVIII) dosing were evaluated in previously treated patients with severe hemophilia A (from two clinical trials).
Ivan, Nestorov, Srividya, Neelakantan, Thomas M, Ludden, Shuanglian, Li, Haiyan, Jiang, Mark, Rogge   +5 more
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Recombinant Human Hb‐SOD Fusion Proteins

2013
Hemoglobin (Hb) can produce reactive oxygen species, including superoxide anions, which are intrinsically toxic. Superoxide dismutase (SOD) is present in red blood cells (RBCs) and provides important protection against such oxidative stress. Upon hemolysis, Hb becomes released from the RBCs and the normal protection systems involving SOD and catalase ...
Marie Grey, Khuanpiroon Ratanasopa, Leif Bülow   +2 more
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Recombinant Baculovirus Vectors Expressing Glutathione–S–Transferase Fusion Proteins

Nature Biotechnology, 1993
Recombinant baculoviruses are a popular means of producing heterologous protein in eukaryotic cells. Purification of recombinant proteins away from the insect cell background can, however, remain an obstacle for many developments. Recently, prokaryotic fusion protein expression systems have been developed allowing single-step purification of the ...
A H, Davies, J B, Jowett, I M, Jones
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