Research Progress Fusion Tags for Recombinant Protein Production
Biotechnology and Applied BiochemistryABSTRACTRecombinant proteins are obtained using genetic engineering techniques and are widely used in various fields. Some recombinant proteins are difficult to express, purify, or are unstable or insoluble due to their structural characteristics. In order to address such issues, additional tags are fused at either the N‐ or C‐terminal end of the ...
Jing‐jia Yuan +2 more
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Recombinant peptide fusion construction for protein‐templated catalytic palladium nanoparticles
Biotechnology Progress, 2020Abstract Although peptide‐enabled synthesis of nanostructures has garnered considerable interest for use in catalytic applications, it has so far been achieved mostly via Fmoc based solid phase peptide synthesis.
Rita Tejada‐Vaprio +9 more
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Staphylokinase as a Plasminogen Activator Component in Recombinant Fusion Proteins
Applied and Environmental Microbiology, 1999ABSTRACT The plasminogen activator staphylokinase (SAK) is a promising thrombolytic agent for treatment of myocardial infarction. It can specifically stimulate the thrombolysis of both erythrocyte-rich and platelet-rich clots.
S J, Szarka +3 more
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OPTIMIZING PROTEIN PURIFICATION FOR RNA-BINDING RECOMBINANT FUSION PROTEINS
2021There has been great interest in delivering short interfering RNA (siRNA) and microRNA (miRNA) for therapeutic applications. However, the delivery of small RNAs remains challenging due to its inefficient cellular uptake and instability under physiological conditions.
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Experimental Spinal Fusion With Recombinant Human Bone Morphogenetic Protein-2
Spine, 1995Lumbar intertransverse process arthrodesis using recombinant human bone morphogenetic protein-2 was performed in a previously established rabbit model for posterolateral spinal fusion and compared with fusions achieved using autogenous bone graft.To qualitatively compare different recombinant human bone morphogenetic protein-2 dosages and carriers and ...
J H, Schimandle, S D, Boden, W C, Hutton
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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 ...
J, Newcombe +5 more
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The Use of Recombinant Fusion Proteases in the Affinity Purification of Recombinant Proteins
Molecular Biotechnology, 1999In the affinity purification of recombinant fusion proteins, the rate-limiting step is usually the efficient proteolytic cleavage and removal of the affinity tail and the protease from the purified recombinant protein. We have developed a rapid, convenient, and efficient method of affinity purification that can overcome this limitation.
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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.
Roman S, Esipov +3 more
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Fusion tails for the recovery and purification of recombinant proteins
Protein Expression and Purification, 1991Several fusion tail systems have been developed to promote efficient recovery and purification of recombinant proteins from crude cell extracts or culture media. In these systems, a target protein is genetically engineered to contain a C- or N-terminal polypeptide tail, which provides the biochemical basis for specificity in recovery and purification ...
C F, Ford, I, Suominen, C E, Glatz
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Tag Removal by Site-Specific Cleavage of Recombinant Fusion Proteins
2010Where an affinity tag has served its purpose it may become desirable to remove it from the protein of interest. This chapter describes the removal of such fusion partners from the intended protein product by cleavage with site-specific endoproteases. Methods to achieve proteolytic cleavage of the fusion proteins are provided, along with techniques for ...
Adam, Charlton, Michael, Zachariou
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