Results 301 to 310 of about 282,766 (336)

Recombinant fusion proteins A and protein G with glutathione S-transferase as reporter molecules

Journal of Immunological Methods, 1991
The regions encoding the IgG-binding domains of protein A (PA) and protein G (PG) were cloned into the bacterial expression vector pGEX. Both proteins were expressed in Escherichia coli as fusion proteins with glutathione S-transferase (PA-GST and PG-GST) and were found to be soluble, abundant and easily purified in one step from the bacterial lysate ...
Lynda M. Thomas, Andrew M. Lew, Dianne J. Beck   +2 more
openaire   +3 more sources

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).
Haiyan Jiang, Mark Rogge, Shuanglian Li, Ivan Nestorov, Srividya Neelakantan, Thomas M. Ludden   +5 more
openaire   +3 more sources

Recombinant rubella E1 fusion proteins for antibody screening and diagnosis

Clinical and Diagnostic Virology, 1994
Until rubella is eradicated there will be a continuing need for rubella antibody surveillance. Antigen production using recombinant DNA technology may be a viable alternative to traditional techniques of producing antigens for enzyme immunoassays (EIAs).To investigate the potential of bacterial fusion proteins containing rubella E1 protein sequences ...
Angus I. Knight, Jane Newcombe, Jennifer M. Best, Sabah Al-Mumin, William G. Starkey, Peter G. Sanders   +5 more
openaire   +3 more sources

Oleosin fusion expression systems for the production of recombinant proteins [PDF]

Biologia, 2007
For the production of recombinant proteins, product purification is potentially difficult and expensive. Plant oleosins are capable of anchoring onto the surface of natural or artificial oil bodies. The oleosin fusion expression systems allow products to be extracted with oil bodies.
openaire   +1 more source

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 ...
Jeremy B. M. Jowett, Ian M. Jones, Anthony H. Davies   +2 more
openaire   +3 more sources

Production of Recombinant Oxytocin Through Sulfitolysis of Inteincontaining Fusion Protein

Protein & Peptide Letters, 2012
An artificial gene consisting of seven copies of an oxytocinoyl-lysine encoding sequence arranged in a tandem was synthesized and inserted downstream of the SspDnaB intein gene in a pTWIN1 plasmid. The corresponding fusion protein Dnab-7oxy contained 16 cysteine residues and formed inclusion bodies when expressed in E. coli.
Anatoly I. Miroshnikov, Vasily N. Stepanenko, Roman S. Esipov, L. A. Chupova   +3 more
openaire   +2 more sources

Architecting Multicompartmentalized, Giant Vesicles with Recombinant Fusion Proteins

Biomacromolecules
We 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, Biswajit Saha, Hoyong Chung, Yeongseon Jang   +3 more
openaire   +2 more sources

Pathogenicity and immunogenicity of recombinant human retinal S-antigen fusion protein

Current Eye Research, 1992
A full-length cDNA clone to human S-antigen (HS-ag) was isolated from lambda gt 10 human retinal library and expressed as a fusion protein with glutathione S-transferase (GST) in E. Coli. Uveitogenicity and immunogenicity of recombinant GST-HS-ag fusion protein and native HS-ag were compared in EAU-susceptible Lewis rats.
R. Whiston, A. J. Roberts, Dudley C. Dumonde, J. P. Banga, E Kasp, Miles Stanford   +5 more
openaire   +3 more sources

The FLAG™ peptide, a versatile fusion tag for the purification of recombinant proteins

Journal of Biochemical and Biophysical Methods, 2001
A fusion tag, called FLAG and consisting of eight amino acids (AspTyrLysAspAspAspAspLys) including an enterokinase-cleavage site, was specifically designed for immunoaffinity chromatography. It allows elution under non-denaturing conditions [Bio/Technology, 6 (1988) 1204]. Several antibodies against this peptide have been developed.
A. Einhauer, Alois Jungbauer
openaire   +3 more sources

Protein body-inducing fusions for recombinant protein production in plants.

2014
Abstract This chapter focuses on the use of plants as bioreactors for the production of recombinant proteins. The feasibility and promise of the use of protein body-inducing fusion tags in transient expression and in stable transgenic plants (i.e. tobacco) are also discussed.
Rima Menassa, S. Gutiérrez, K. L. Hefferon   +2 more
openaire   +2 more sources