Recombinant human dipeotdidyl peptidase I (DPPI)

Cathepsin C (CTSCD) also known as dipeptideyl peptides I (DPP I) is a lyaosomal exo-cysteine protease beloning to the peptidase C1 family. DPPI catalyzes excision of dipeptides from the N-terminus of proteins and peptide substrates unless the N-terminal amino group is blocked, the cleavage site is on either side of a proline residue, the N-terminal residue is lysine or arginine, or the structure of the peptide or protein prevents further digestion from the N-terminus. 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.