Overview

Description

  • Nature
    Recombinant
  • Source
    HEK 293 cells
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      DVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIE KNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVAN NGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPE DDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDG YTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLR QKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLN ANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTE PKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVS PMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEA NNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQ KSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALT DCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAG LLPSHLPE
    • Molecular weight
      67 kDa including tags
    • Amino acids
      108 to 715
    • Tags
      His tag C-Terminus

Specifications

Our Abpromise guarantee covers the use of ab167741 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Biological activity
    Measured by its ability to cleave the fluorogenic peptide substrate p – Glu – Arg – Thr – Lys – Arg – AMC. The bioactivity was measured in 100µL reaction mixture containing 4 µg/ml of rhFurin, 50 µM substrate, 25 mM Tris, 1 mM CaCl2, 0.5% (w/v) Brij­35, pH 9.0. The specific activity is >130 pmol/min/µg.
  • Applications

    Functional Studies

    SDS-PAGE

  • Endotoxin level
    < 1.000 Eu/µg
  • Purity
    >95% by SDS-PAGE .
    ab167741 was lyophilized from 0.22 µm filtered solution.
  • Form
    Lyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

    Constituents: MES, Trehalose

    Typically between 5-10% trehalose is used for freeze drying, and after reconstitution, the trehalose is approximately 3-5%.

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

  • Reconstitution
    It is recommended to reconstitute the lyophilized protein in sterile deionized water to a final concentration of 200 ug/ml. Solubilize for 30 to 60 minutes at room temperature with occasional gentle mixing. Carrier protein (0.1% HSA or BSA) is strongly recommended for further dilution and long term storage.

General Info

  • Alternative names
    • Dibasic processing enzyme
    • Dibasic-processing enzyme
    • FES upstream region
    • FUR
    • FURIN
    • Furin membrane associated receptor protein
    • FURIN_HUMAN
    • PACE
    • Paired basic amino acid residue cleaving enzyme
    • Paired basic amino acid residue-cleaving enzyme
    • PCSK3
    • Proprotein convertase subtilisin/kexin type 3
    • SPC1
    see all
  • Function
    Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.
  • Tissue specificity
    Seems to be expressed ubiquitously.
  • Sequence similarities
    Belongs to the peptidase S8 family. Furin subfamily.
    Contains 1 homo B/P domain.
  • Domain
    Contains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface.
  • Post-translational
    modifications
    The inhibition peptide, which plays the role of an intramolecular chaperone, is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and furin activation.
    Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms.
  • Cellular localization
    Golgi apparatus > trans-Golgi network membrane. Cell membrane. Shuttles between the trans-Golgi network and the cell surface. Propeptide cleavage is a prerequisite for exit of furin molecules out of the endoplasmic reticulum (ER). A second cleavage within the propeptide occurs in the trans Golgi network (TGN), followed by the release of the propeptide and the activation of furin.
  • Information by UniProt

Images

  • SDS-PAGE analysis of reduced ab167741 and staining overnight with Coomassie Blue. DTT-reduced Protein migrates as 55-66 kDa.

References

ab167741 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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