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AB290104

Recombinant Human Furin Protein

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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.

View Alternative Names

FUR, PACE, PCSK3, FURIN, Furin, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme

1 Images
SDS-PAGE - Recombinant Human Furin Protein (AB290104)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Furin Protein (AB290104)

SDS-PAGE analysis of ab290104

Key facts

Purity

>95% HPLC

Expression system

HEK 293 cells

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P09958

Animal free

Yes

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 10.26% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"DLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPE","proteinLength":"Fragment","predictedMolecularWeight":"62.9 kDa","actualMolecularWeight":"62.9 kDa","aminoAcidEnd":715,"aminoAcidStart":131,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P09958","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Furin is a serine endoprotease that plays critical role in the cleavage of precursor proteins into their active forms. It belongs to the proprotein convertase family and is also known as furin protease. The molecular weight of furin is approximately 54 kDa. Furin is ubiquitously expressed in various tissues in the body with high expression levels in the liver and the central nervous system. Furin is mainly located in the trans-Golgi network where it processes many precursor proteins involved in various cellular functions.
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.

Furin is implicated in several conditions including cardiovascular diseases and certain cancers. In cardiovascular diseases furin's role in processing proteins such as pro-BNP may have implications in cardiac function and disease progression. In cancer altered furin activity can lead to the inappropriate activation of growth factors and receptors contributing to tumor progression. Furin inhibitors are researched for their potential to modulate furin activity in these diseases and provide therapeutic benefits.
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Specifications

Form

Liquid

Additional notes

SDS-PAGE >= 95%

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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

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Product protocols

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Target data

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.
See full target information FURIN
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