Recombinant tobacco etch virus proteinase, His tag

CAT:
882-PO56024E1-01
Size:
100 µg
  • Availability: 24/48H Stock Items & 2 to 6 Weeks non Stock Items.
  • Dry Ice Shipment: No
Recombinant tobacco etch virus proteinase, His tag - image 1

Recombinant tobacco etch virus proteinase, His tag

  • Synonyms:

    Recombinant Tobacco Etch Virus (TEV) protease
  • Expression System:

    E.coli
  • Tag:

    His
  • Endotoxin:

    < 1.0 EU per μg of the protein as determined by the LAL method.
  • Purity:

    > 95% as determined by SDS-PAGE.
  • Length:

    255
  • Form:

    Liquid
  • Buffer:

    PBS, pH 8.0
  • Molecular Weight:

    27 kDa
  • Storage Conditions:

    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.
  • Symbol:

    TEV protease
  • Species:

    Tobacco Etch Virus
  • Overview:

    The recombinant TEV protease is a highly purified preparation encoded by the small nuclear protein A catalytic domain gene of tobacco Mosaic virus. The biological function of the enzyme is to hydrolyse multiple proteins into a single protein during virus production. The product is a genetically engineered protease that is stable and specific over a wide range of temperatures. This product is derived from recombinant Escherichia coli and is highly purified with high specific activity. The optimal digestion temperature was 30 °C, but the enzyme was also active at 4 °C. After digestion, it can be conveniently removed by Ni affinity column chromatography. 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.