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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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Pathogenicity and immunogenicity of recombinant human retinal S-antigen fusion protein
Current Eye Research, 1992A 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+5 more
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Protein body-inducing fusions for recombinant protein production in plants.
2014Abstract 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+2 more
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Expression, Purification, and Immobilization of Recombinant Tamavidin 2 Fusion Proteins
2014Tamavidin 2 is a fungal avidin-like protein that binds biotin with high affinity. Unlike avidin or streptavidin, tamavidin 2 in soluble form is produced at high levels in Escherichia coli. In this chapter, we describe a method for immobilization and purification of recombinant proteins with the use of tamavidin 2 as an affinity tag.
Masako Tsunashima+2 more
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A recombinant fusion protein clears IgA deposits
Nature Reviews Nephrology, 2022openaire +2 more sources
International Archives of Allergy and Immunology, 2010
Laetitia Bussières+17 more
semanticscholar +1 more source
Laetitia Bussières+17 more
semanticscholar +1 more source
Recombinant fusion proteins TAT‐Mu, Mu and Mu‐Mu mediate efficient non‐viral gene delivery
Journal of Gene Medicine, 2007Rukkumani Rajagopalan+4 more
semanticscholar +1 more source