Recombinant tobacco etch virus proteinase, MBP tag, His tag

TEV protease, also known as tobacco etch virus protease, is a highly specific cysteine protease, which can recognize the amino acid sequence Glu-Asn-Leu-Tyr-Phe-Gln- (Gly/Ser) and cleave between Gln and Gly/Ser. It is often used to remove affinity purification tags from fusion proteins, such as maltose-binding protein (MBP) or polyhistidine . We have directional protein refolding technology (LeaBioFOLD) and self-developed technology platforms for proteins covering screening and purification, engineering design, fixed-point coupling design, and dosage form development. Protein refolding is a process of recovering protein aggregates in inclusion bodies in the form of misfolded and inactive proteins expressed by prokaryotes such as Escherichia coli back into proteins with correct conformation and bioactivity under appropriate conditions in vitro. It is a key technology for biopharmaceutical companies but a major bottleneck in protein production in prokaryotic expression systems. Leading Biology has been specializing in protein refolding for many years, has a core team with over ten years of experience in this technology and rich experience in its industrialization. Our team is summarizing the experience to form an independent technological system of ours.

Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.