Innovative Tools for Molecular and Cell Biology

Innovative Tools for Molecular and Cell Biology

Products

IgA Protease (Igase Pro-Pro-Y-Pro)

Highly efficient specific Endoprotease

Cleavage site of IgA Protease

Schematic view of cleavage site

Features

  • Cleaves amino acid sequence N-X-Z-Pro-Pro/-Y-Pro-C (X = preferably Pro or Ser;Y = Thr,Ser or Ala; Z = preferably Arg or Thr)
  • Also cleaves insoluble aggregates derived from inclusion bodies
  • Used for cleavage of fusion proteins
  • Natural substrate is IgA1
  • Since the endoproteinase cleaves the proline-rich hinge region of IgA1 the enzyme is also referred to as Igase or IgA protease 4

Description

  • In recombinant protein technology sequence-specific enzymatic cleavage of fusion proteins has become an important application. IgA Protease (Igase Pro-Pro-Y-Pro), a protein of 106 kDa, efficiently processes polypeptides at authentic or engineered sites. Since the endoproteinase cleaves the proline-rich hinge region of IgA1 the enzyme is also referred to as Igase or IgA protease 4. IgA Protease (Igase Pro-Pro-Y-Pro) recognizes the amino acid sequence N-X-Z-Pro-Pro/-Y-Pro-C (X = preferably Pro or Ser;Y = Thr,Ser or Ala; Z = preferably Arg or Thr). The highly specific proteolysis can be obtained not only with soluble and purified protein fusions but also with insoluble aggregates derived from cytoplasmic inclusion bodies.

ORDER INFORMATION

  • For shipping and storage information please click on Order#.
Order# Description Amount Price Data Sheet
EP0205 IgA Protease (Igase Pro-Pro-Y-Pro), recombinant 50 µg 457,00 PDF
  • All prices are in EURO excl. VAT and shipping. For further pricing and order information please ask your local distributor.

Literature

  • J. Pohlner et al., Nature 325 (1987), 458 – 462
  • R. Halter et al., EMBO J. 8 (1989), 2737 - 2744
  • W. Bachovchin et al., J. Biol. Chem. 265 (1990), 3738 - 3743
  • J. Pohlner et al., Biotechnology Vol. 10 (1992)
  • R. Jaenicke et al., ‘Protein Structure, a practical approach’, chapter ‘Folding Proteins’ pg. 191-223, ed. Creighton, IRL Press Oxford