Efficient Expression of Soluble Recombinant Protein Fused with Core-Streptavidin in Bacterial Strain with T7 Expression System

Soluble Expression and Purification of Q59L Mutant L-asparaginase in the Presence of Chaperones in SHuffle™ T7 strain

Background and Aims: Q59L mutant of L-asparaginase enzyme from Escherichia coli (E. coli) has been introduced with lower side effects. This version of the enzyme might have potential applications in the treatment of leukemia patients. We utilized SHuffle T7 strain of E. coli, to produce the mutant enzyme in the presence of chaperone molecules. Materials and Methods: Q59LAsp gene was cloned in...

Optimized Cytoplasmic Expression of Water Soluble Human Thrombopoietin in Modified Bacterial Strain

Background: Thrombopoietin is a glycoprotein produced by liver and kidney which is responsible for regulating the platelet production. Thrombopoietin is a key ligand with impact on regulating the self-renewal of Hematopoietic stem cells and the regulation of Megakaryocytes progenitors. Previous studies have indicated that only N-terminal domain of this protein has receptor promoting ability. Th...

Expression and Purification of HCV Core and Core-E1E2 Proteins in Different Bacterial Strains

Background: Hepatitis C virus (HCV) is a main public health problem causing chronic liver infection and subsequently liver cirrhosis and lethal hepatocellular carcinoma (HCC). Vaccination based on HCV capsid proteins has attracted a special interest for prevention of viral infections. The core protein is a basic and evolutionary most conserved protein, which regulates the cellular processes rel...

Advances and challenges in recombinant protein expression in Escherichia coli

applications of autodisplay system for recombinant protein expression on the bacterial cell surface

protein secretory systems are found in all living organisms including gram negative bacteria, and eukaryotic cell’s organelles that are derived from these bacteria. unlike all other living organisms, gram negative bacteria have different protein secretory systems. at least there are four different independent secretory systems, which are responsible to transport the secreted proteins to the mil...