General Information
| Short Description | Recombinant-Human Furin-protein was developed from hek293. For use in research applications. |
| Host | HEK293 |
| Note | STRICTLY FOR FURTHER RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Conjugation | Unconjugated |
| Dilution Range | Spin the vial and reconstite in distilled water to a concentration not less than 0.1 mg/mL. This can then be diluted into other buffers. |
| Formulation | Lyophilised from 0.2 Mu m filtered PBS solution, pH7.2, 5% Trehalose. |
| Storage Instruction | Can be stored in working aliquots at 2°C-8°C C for one month, or at-20°C to-70°C for 1 year. Avoid repeated freeze/thaw cycles. NA |
| Endotoxin | Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg (1EU/µg). NA |
| Immunoreactivity | The activity was tested by the ability of cleave the fluorogenic peptide substrate GATLA–AMC, and was measured to be >150 pMole/min/ug NA |
Target Information
| Gene Symbol | |
| Gene ID | |
| Uniprot ID | |
| Immunogen | Optimized DNA sequence encoding peptidase domain of Human Furin (ASP108-GLU715) including a C-terminal His tag was expressed in HEK293 cells. NA |
| Immunogen Region | ASP108-GLU715 |
Additional Info
| Tissue Specificity | Seems to be expressed ubiquitously. |
| 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. |
| Function | Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. Mediates processing of TGFB1, an essential step in TGF-beta-1 activation. Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-32). 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. (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. |
| Protein Name | FurinDibasic-Processing EnzymePaired Basic Amino Acid Residue-Cleaving EnzymePace |
| Database Links | |
| Cellular Localisation | Golgi ApparatusTrans-Golgi Network MembraneSingle-Pass Type I Membrane ProteinCell MembraneSecretedEndosome MembraneShuttles Between The Trans-Golgi Network And The Cell SurfacePropeptide Cleavage Is A Prerequisite For Exit Of Furin Molecules Out Of The Endoplasmic Reticulum (Er)A Second Cleavage Within The Propeptide Occurs In The Trans Golgi Network (Tgn)Followed By The Release Of The Propeptide And The Activation Of Furin |
| Alternative Protein Names | Furin proteinDibasic-Processing Enzyme proteinPaired Basic Amino Acid Residue-Cleaving Enzyme proteinPace proteinFURIN proteinFUR proteinPACE proteinPCSK3 protein |
Information sourced from Uniprot.org