Overview

Description

  • Nature

    Recombinant
  • Source

    BTI-TN-5B1-4 cells
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Sequence

      DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHACSAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPEHHHHH HHH
    • Molecular weight

      64 kDa including tags
    • Amino acids

      131 to 715
    • Tags

      His tag C-Terminus

Specifications

Our Abpromise guarantee covers the use of ab126908 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 Boc-Arg-Val-Arg-Arg-AMC
  • Applications

    Functional Studies

    SDS-PAGE

    HPLC

  • Endotoxin level

    < 0.100 Eu/µg
  • Purity

    > 95 % SDS-PAGE.
    Greater than 95% by SDS-PAGE gel and HPLC analyses.
  • Form

    Lyophilised
  • Additional notes

    Measured by its ability to cleave the fluorogenic peptide substrate Boc-Arg-Val-Arg-Arg-AMC
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C.

    pH: 7.60
    Constituents: 0.05% Calcium chloride, 5% Trehalose, 0.24% Tris

  • Reconstitution
    Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20oC to -80oC

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

References

ab126908 has not yet been referenced specifically in any publications.

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