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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Construction and expression of recombinant fusion protein of thioredoxin-ApoO.
Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences, 2011To construct human apolipoprotein O (apolipoprotein O, ApoO) expression vector and obtain recombinant fusion protein thioredoxin (Trx)-ApoO by pET prokaryotic expression system.The ApoO gene fragment from the human liver cDNA library was amplified by PCR. The resulting product was cloned into pET-32a(+) vector and sequenced.
Bi-lian Yu+3 more
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Recombinant fusion proteins A and protein G with glutathione S-transferase as reporter molecules
Journal of Immunological Methods, 1991The 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+2 more
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Population pharmacokinetics of recombinant factor VIII Fc fusion protein
Clinical Pharmacology in Drug Development, 2014AbstractPopulation 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+5 more
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Recombinant rubella E1 fusion proteins for antibody screening and diagnosis
Clinical and Diagnostic Virology, 1994Until 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+5 more
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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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Oleosin fusion expression systems for the production of recombinant proteins [PDF]
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.
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Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase.
Analytical Biochemistry, 1994An improved method for the production, cleavage, and purification of fusion proteins and peptides is described. The unique aspect of this method is dependent on the use of a proteinase from tobacco etch virus (TEV).
T. Parks+4 more
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Production of Recombinant Oxytocin Through Sulfitolysis of Inteincontaining Fusion Protein
Protein & Peptide Letters, 2012An 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+3 more
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Recombinant Baculovirus Vectors Expressing Glutathione–S–Transferase Fusion Proteins
Nature Biotechnology, 1993Recombinant 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+2 more
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