Furine

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 61.7 kDa protein, corresponding to residues 124 through 715 of the Furin precursor plus a C-terminal His tag.

FURIN; FUR; PACE; SPC1; PCSK3

5045

P09958

NP_002560.1

NM_002569.2

15q26.1

Human

Human

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 WTTVAPQRKI IDILTEPKDI GKRLEVRKTV TACLGEPNHI TRLEHAQARL TLSYNRRGDL AIHLVSPMGT RSTLLAARPH DYSADGFNDW AFMTTHSWDE DPSGEWVLEI ENTSEANNYG TLTKFTLVLY GTAPEGLPVP PESSGCKTLT SSQACVVCEE GFSLHQKSCV QHCPPGFAPQ VLDTHYSTEN DVETIRASVC APCHACSATC QGPALTDCLS CPSHASLDPV EQTCSRQSQS SRESPPQQQP PRLPPEVEAG QRLRAGLLPS HLPEHHHHHH HH

< 0.1 ng/µg of protein (< 1EU/µg)

> 98% by SDS-PAGE & HPLC analyses

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

715

Lyophilized

61.7 kDa

Insect cells