Using Large Language Model to Optimize Protein Purification: Insights from Protein Structure Literature Associated with Protein Data Bank. [PDF]
Chen Z, Sivaraman J.
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Bacterial expression, purification and folding of exceptionally hydrophobic and essential protein: Surfactant Protein-B (SP-B). [PDF]
Asrat T, Jackman D, Booth V.
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Recovery of mouse growth hormone from E. coli inclusion bodies using a mild solubilisation and repeated freeze-thaw approach. [PDF]
Kim M, Langley RJ, Perry JK, Wang Y.
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Bacillus subtilis surface display technology: applications in bioprocessing and sustainable manufacturing. [PDF]
Bahrulolum H, Ahmadian G.
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M72 Fusion Proteins in Nanocapsules Enhance BCG Efficacy Against Bovine Tuberculosis in a Mouse Model. [PDF]
Blanco FC+8 more
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Application of Recombinant Fusion Proteins for Tissue Engineering
Annals of Biomedical Engineering, 2010Extracellular matrix (ECM) plays important roles in tissue engineering because cellular growth and differentiation, in the two-dimensional cell culture as well as in the three-dimensional space of the developing organism, require ECM with which the cells can interact. Also, the development of new synthetic ECMs is very important because ECMs facilitate
Masato Nagaoka+4 more
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Staphylokinase as a Plasminogen Activator Component in Recombinant Fusion Proteins
ABSTRACT 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.
Steven Szarka+3 more
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Overview of fusion tags for recombinant proteins
Biochemistry (Moscow), 2016Virtually all recombinant proteins are now prepared using fusion domains also known as "tags". The use of tags helps to solve some serious problems: to simplify procedures of protein isolation, to increase expression and solubility of the desired protein, to simplify protein refolding and increase its efficiency, and to prevent proteolysis.
E. N. Kosobokova+2 more
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Tag Removal by Site-Specific Cleavage of Recombinant Fusion Proteins
Methods in molecular biology, 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 ...
Michael Zachariou, Adam Charlton
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Recombinant avidin and avidin–fusion proteins
Biomolecular Engineering, 1999Both chicken egg-white avidin and its bacterial relative streptavidin are well known for their extraordinary high affinity with biotin (Kd approximately 10(-15) M). They are widely used as tools in a number of affinity-based separations, in diagnostic assays and in a variety of other applications. These methods have collectively become known as (strept)
Markku S. Kulomaa+2 more
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