We report a novel fusion tag for expressing recombinant proteins in E. coli. The fusion tag is the C-terminus part of the human GMCSF gene comprising 45 amino acids, which aid in over expression of otherwise non expressible genes. Expression of hIFN 2b with this fusion tag also escapes the requirement of rare codons for expression. This is also a first report of a small fusion tag of human orig...

BACKGROUND Animal venoms are large, complex libraries of bioactive, disulphide-rich peptides. These peptides, and their novel biological activities, are of increasing pharmacological and therapeutic importance. However, recombinant expression of venom peptides in Escherichia coli remains difficult due to the significant number of cysteine residues requiring effective post-translational processi...

BACKGROUND Thymosin α1 (Tα1), a 28-amino acid Nα-acetylated peptide, has a powerful general immunostimulating activity. Although biosynthesis is an attractive means of large-scale manufacture, to date, Tα1 can only be chemosynthesized because of two obstacles to its biosynthesis: the difficulties in expressing small peptides and obtaining Nα-acetylation. In this study, we describe a novel produ...

BACKGROUND Therapeutic angiogenesis with vascular endothelial growth factor (VEGF), delivered either via recombinant protein infusion or via gene therapy, has shown promise in preclinical models of various diseases including myocardial infarction, renovascular disease, preeclampsia, and neurodegenerative disorders. However, dosing, duration of expression, and tissue specificity are challenges t...

The cDNA encoding human glutathione S-transferase (GST) T1 has been expressed as two recombinant forms in Escherichia coli that could be purified by affinity chromatography on either IgG-Sepharose or nickel-agarose; one form of the transferase was synthesized from the pALP 1 expression vector as a Staphylococcus aureus protein A fusion, whereas the other form was synthesized from the pET-20b ex...

BACKGROUND Genetic fusion of the major birch pollen allergen (Bet v1) to bacterial surface-(S)-layer proteins resulted in recombinant proteins exhibiting reduced allergenicity as well as immunomodulatory capacity. Thus, S-layer/allergen fusion proteins were considered as suitable carriers for new immunotherapeutical vaccines for treatment of Type I hypersensitivity. Up to now, endotoxin contami...

Background and Aims: The novel approaches in influenza vaccination have targeted more conserved viral proteins such as nucleoprotein (NP) to provide cross protection against all serotypes of influenza A viruses. Influenza specific cytotoxic T lymphocytes (CTL) are able to lyse influenza-infected cells by recognition of NP, the major target molecule in virus for CTL responses. On the other hand,...

A bovine tropoelastin cDNA encoding exons 15-36 that includes the elastin-receptor binding site was expressed in Escherichia coli as a fusion protein with Protein A from Staphylococcus aureus. After isolation of the fusion protein by affinity chromatography on Ig-Sepharose, the tropoelastin domain was separated from plasmid-pR1T2T-encoded Protein A (Protein A') by CNBr cleavage. Cell-adhesion a...

background and aims: the novel approaches in influenza vaccination have targeted more conserved viral proteins such as nucleoprotein (np) to provide cross protection against all serotypes of influenza a viruses. influenza specific cytotoxic t lymphocytes (ctl) are able to lyse influenza-infected cells by recognition of np, the major target molecule in virus for ctl responses. on the other hand,...

Our long-term research goal is to understand and exploit the natural biochemical properties of the fibrinogen/fibrin system for greater control of fibrin polymerization and degradation. In R21EB008463, we hypothesized that a fibrin knob fusion with thermo-responsive elastin-like peptide repeats will bind to fibrinogen polymerization pockets and prevent polymerization in a temperature-dependent ...