Furin
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.
Product Specifications
Synonyms
FURIN; FUR; PACE; SPC1; PCSK3
NCBI Gene ID
5045
UniProt
P09958
Accession Number
NP_002560.1
Accession Number mRNA
NM_002569.2
Chromosomal Location
15q26.1
Reactivity
Human
Cross Reactivity
Human
Sequence
Endotoxin
< 0.1 ng/µg of protein (< 1EU/µg)
Purity
> 98% by SDS-PAGE & HPLC analyses
Bioactivity
Measured by its ability to cleave the fluorogenic peptide substrate Boc-Arg-Val-Arg-Arg-AMC (Bachem Catalog# I-1645.0025) .
Length
715
Form
Lyophilized
Molecular Weight
61.7 kDa
Host or Source
Insect cells
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