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Purification of the recombinant green fluorescent protein from tobacco plants using alcohol/salt aqueous two-phase system and hydrophobic interaction chromatography

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The green fluorescent protein (GFP) has been regarded as a valuable tool and widely applied as a biomarker in medical applications and diagnostics. | Purification of the recombinant green fluorescent protein from tobacco plants using alcohol/salt aqueous two-phase system and hydrophobic interaction chromatography

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Purification and analysis catalytic functions of recombinant influenza viral polymerases

Selection of purification condition for recombinant endoglucanase originated from goat rumen bacteria in Escherichia Coli

Expression, purification, and characterization of recombinant human paraoxonase 1 (rhPON1) in Pichia pastoris

Purification of recombinant human interleukin-3 expressed as inclusion bodies in Escherichi coli

Purification and characterization of a recombinant beta-glucosidase in Escherichia coli

Expression and purification of thioredoxin-his6 -ZmDREB2.7 fusion protein in Escherichia coli for raising antibodies

Expression, purification, and characterization of rhTyrRS

High yield production and purification of two recombinant thermostable phosphotriesterase-like lactonases from Sulfolobus acidocaldarius and Sulfolobus solfataricus useful as bioremediation tools and bioscavengers

Soluble expression of an amebic cysteine protease in the cytoplasm of Escherichia coli SHuffle Express cells and purification of active enzyme

Soluble expression, purification, and characterization of active recombinant human tissue plasminogen activator by auto-induction in E. coli