Recombinant human SUMO protease, His tag

SUMO protease, also known as ULP protease, is a cysteine protease with high activity. SUMO proteases cleave proteins with a very high specificity. It can specifically recognize the tertiary structure of UBL proteins, namely Small Ubiquitin-LikeModifier (SUMO), rather than the amino acid sequence. The optimal reaction temperature was 30°C, and the enzyme acted in a wide range of temperature and pH (pH7-9) . SUMO protease recognizes tertiary structure of SUMO tag: LQDSEVNQEAKPEVKPEVKPETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQAPEDLDMEDNDIIEAHREQIGG↓XX (Except P on first X) 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.