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FURIN Protein

Recombinant FURIN protein expressed in Hi-5 Cells.
Catalog No. ABIN2468449

Quick Overview for FURIN Protein (ABIN2468449)

Target

See all FURIN Proteins
FURIN (Furin (Paired Basic Amino Acid Cleaving Enzyme) (FURIN))

Protein Type

Recombinant

Biological Activity

Active

Origin

  • 12
  • 3
  • 2
Human

Source

  • 12
  • 2
  • 2
  • 1
Hi-5 Cells

Purity

< 95 % by SDS-PAGE gel and HPLC analyses.
  • 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 CAPC

    Characteristics

    Biological activity was measured by its ability to cleave the fluorogenic peptide substrate Boc-Arg-Val-Arg-Arg-AMC (Bachem Catalog# I-1645.0025).

    Endotoxin Level

    Endotoxin level is less than 0.1 ng per μg (1 EU/μg).
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  • Restrictions

    For Research Use only
  • Format

    Lyophilized

    Handling Advice

    As with any protein, exposing Furin recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.

    Storage

    -20 °C

    Storage Comment

    The recombinant protein is stable for at least 2 years from date of receipt at -20 °C. Reconstituted Furin stable for at least 3 months when stored in working aliquots with a carrier protein at -20 °C.

    Expiry Date

    24 months
  • Target

    FURIN (Furin (Paired Basic Amino Acid Cleaving Enzyme) (FURIN))

    Alternative Name

    Furin

    Background

    Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Furin is a calcium dependent serine endoprotease that processes numerous proproteins of different secretory pathways into their mature forms by cleaving at the carboxyl side of the recognition sequence, R-Xaa-(K/R)-R, where Xaa can be any amino acid. Recombinant human Furin is a 63.9 kDa protein, corresponding to residues 131 through 715 of the Furin precursor plus a C-terminal His tag.

    Gene ID

    5045

    NCBI Accession

    NP_001276752

    OMIM

    577019578

    UniProt

    P09958

    Pathways

    Notch Signaling, Neurotrophin Signaling Pathway
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