Recombinant Furin protein is a Human Full Length protein, in the 1 to 713 aa range, expressed in Mammalian, suitable for WB.
View Alternative Names
FUR, PACE, PCSK3, FURIN, Furin, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme
Reactivity data
Product details
This 81 kDa recombinant protein was obtained from cytoplasmic extracts by centrifugation and lysis of BSC-40 cells infected with recombinant vaccinia virus (VV:hFUR713t). The preparation was subjected to UV irradiation for 5 minutes to inactivate any residual virus. Activity of 1 U/µl, where 1 U (a unit of activity) is defined as the amount of furin that can release 1 pmol of AMC from the fluorogenic peptide pERTKR-MCA in 1 min.
Furin is a membrane-associated, calcium-dependent, serine protease that belongs to the subtilisin-like prohormone convertase (PC) family. Members of this family of cellular enzymes cleave most prohormones and neuropeptide precursors. Numerous other cellular proteins, some viral proteins, and bacterial toxins that are transported by the constitutive secretory pathway are also targeted for maturation by PCs. Furin and other PC family members share structural similarities which include a heterogeneous ~10 kDa amino-terminal proregion, a highly conserved ~55 kDa subtilisin-like catalytic domain, and carboxyl-terminal domain that is heterogeneous in length and sequence. These enzymes become catalytically active following proregion cleavage within the appropriate cellular compartment. Furin is the only known PC to possess a transmembrane domain. Cleavage of target proteins occurs at the carboxyl-terminus of the furin consensus sequence, RX(K/R)R. It has been shown that the acidic peptide sequence, C771PSDSEEDEG780, localizes furin to the trans-Golgi-network. Phosphorylation of serine residues within this region modulates intracellular routing of furin protein. An additional signaling domain includes the tetrapeptide sequence, Y759KGL762, which directs internalization from the cell surface.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Furin processes precursor proteins by cleaving at specific sequence motifs. This activity is essential for the maturation of many hormones growth factors and receptors. Furin is not part of a larger complex; it functions independently in its proteolytic activity. The processing by furin ensures that proteins become functional affecting numerous biological processes across different cell types and tissues.
Pathways
The activity of furin impacts the regulation of the Notch signaling pathway and the MAPK/ERK pathway. In the Notch signaling pathway furin processes Notch receptors facilitating their activation and downstream signaling. In the MAPK/ERK pathway furin activates several key proteins including growth factors and receptors essential for cell proliferation and differentiation. Furin-related proteins such as convertase enzymes are part of a similar family having roles in overlapping or complementary pathways.
Specifications
Form
Liquid
General info
Function
Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif (PubMed : 11799113, PubMed : 1629222, PubMed : 1713771, PubMed : 2251280, PubMed : 24666235, PubMed : 25974265, PubMed : 7592877, PubMed : 7690548, PubMed : 9130696). Mediates processing of TGFB1, an essential step in TGF-beta-1 activation (PubMed : 7737999). Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-32) (PubMed : 20489134, PubMed : 21763278). By mediating processing of accessory subunit ATP6AP1/Ac45 of the V-ATPase, regulates the acidification of dense-core secretory granules in islets of Langerhans cells (By similarity).. (Microbial infection) Cleaves and activates diphtheria toxin DT.. (Microbial infection) Cleaves and activates anthrax toxin protective antigen (PA).. (Microbial infection) Cleaves and activates HIV-1 virus Envelope glycoprotein gp160.. (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin.. (Microbial infection) Able to cleave S.pneumoniae serine-rich repeat protein PsrP.. (Microbial infection) Facilitates human coronaviruses EMC and SARS-CoV-2 infections by proteolytically cleaving the spike protein at the monobasic S1/S2 cleavage site. This cleavage is essential for spike protein-mediated cell-cell fusion and entry into human lung cells.. (Microbial infection) Facilitates mumps virus infection by proteolytically cleaving the viral fusion protein F.
Sequence similarities
Belongs to the peptidase S8 family. Furin subfamily.
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.
Subcellular localisation
Endosome membrane
Target data
Alternative Products
Complementary Products
Primary Antibodies
AB281204
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Product promise
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