Floadianase (recombinant trypsin like enzyme)

Floadianase is an animal origin-free recombinant enzyme alternative to porcine or bovine trypsin for the dissociation of attachment-dependent cell lines from plasticware. Floadianase cleaves peptide bonds on the C-terminal side of lysine and arginine but with greater specificity than native trypsin preparations due to the superior purity of Floadianase. Floadianase has demonstrated the ability to dissociate cells cultured both in serum-free and serum supplemented systems. Floadianase products are formulated in 1x PBS/1 mM EDTA, are room-temperature stable, and are convenient to use. 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.