Recombinant Human Furin Protein is a Human Fragment protein, in the 131 to 715 aa range, expressed in HEK 293 cells, with >95%, suitable for SDS-PAGE.
대체 명칭 보기
FUR, PACE, PCSK3, FURIN, Furin, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Furin Protein (AB290104)
SDS-PAGE analysis of ab290104
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Reagents, Controls & Accessories
AB325997
Prestained Protein Ladder - Extra broad molecular weight (3-250 kDa, 5-color)
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추가 정보
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.
일반 정보
기능
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.
서열 유사성
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
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