Rabbit Anti-FURIN Recombinant Antibody (
1C3) (V2LY-0725-LY1147)

Name: Rabbit Anti-FURIN Recombinant Antibody (1C3)
SKU: V2LY-0725-LY1147
Rating: 5 (1 reviews)

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Tested Data

Rabbit Anti-FURIN Recombinant Antibody (1C3) (V2LY-0725-LY1147) in WB

Western Blot
Positive WB detected in: A549 whole cell lysate, Hela whole cell lysate, A375 whole cell lysate, HT-29 whole cell lysate, HepG2 whole cell lysate, U-87 whole cell lysate
All lanes: Furin antibody at 1:1000
Secondary
Goat polyclonal to rabbit IgG at 1/50000 dilution
Predicted band size: 87 kDa
Observed band size: 87, 72 kDa

Rabbit Anti-FURIN Recombinant Antibody (1C3) (V2LY-0725-LY1147) in IHC

IHC image of V2LY-0725-LY1147 diluted at 1:100 and staining in paraffin-embedded human placenta tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit IgG polymer labeled by HRP and visualized using 0.05% DAB.

Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Rabbit

Clone

1C3

Application

ELISA, WB, IHC

Immunogen

A synthesized peptide derived from human Furin.

Host Species

Rabbit

Specificity

Human

Antibody Isotype

IgG

Clonality

Monoclonal Antibody

Application Notes

Application	Note
WB	1:500-1:5,000
IHC	1:50-1:200

Formulations & Storage [For reference only, actual COA shall prevail!]

Format

Liquid

Buffer

PBS, glycerol

Preservative

Sodium azide

Concentration

Batch dependent

Purity

> 95% Purity determined by SDS-PAGE.

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

More Infomation

Target

Full Name

Furin, Paired Basic Amino Acid Cleaving Enzyme

Entrez Gene ID

5045

UniProt ID

P09958

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).

(Microbial infection) Cleaves and activates diphtheria toxin DT.

(Microbial infection) Cleaves and activates anthrax toxin protective antigen (PA).

(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.

Biological Process

Amyloid fibril formation Source: Reactome
Blastocyst formation Source: Ensembl
Collagen catabolic process Source: Reactome
Dibasic protein processing Source: UniProtKB
Extracellular matrix disassembly Source: Reactome
Extracellular matrix organization Source: Reactome
Negative regulation of inflammatory response to antigenic stimulus Source: Reactome
Negative regulation of low-density lipoprotein particle receptor catabolic process Source: HGNC-UCL
Negative regulation of transforming growth factor beta1 production Source: BHF-UCL
Nerve growth factor production Source: BHF-UCL
Peptide biosynthetic process Source: BHF-UCL
Peptide hormone processing Source: BHF-UCL
Positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
Positive regulation of transforming growth factor beta1 activation Source: UniProtKB
Protein processing Source: UniProtKB
Regulation of cholesterol transport Source: Ensembl
Regulation of endopeptidase activity Source: BHF-UCL
Regulation of lipoprotein lipase activity Source: Reactome
Regulation of protein catabolic process Source: BHF-UCL
Regulation of signal transduction Source: Ensembl
Secretion by cell Source: BHF-UCL
Signal peptide processing Source: HGNC-UCL
Transforming growth factor beta receptor signaling pathway Source: Reactome
Viral life cycle Source: BHF-UCL
Viral protein processing Source: Reactome
Zymogen activation Source: UniProtKB
Zymogen inhibition Source: UniProtKB

Cellular Location

Trans-Golgi network membrane; Endosome membrane; Secreted; Cell membrane. Shuttles between the trans-Golgi network and the cell surface (PubMed:9412467, PubMed:11799113). Propeptide 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 (PubMed:11799113).

Topology

Lumenal: 108-715
Helical: 716-738
Cytoplasmic: 739-794

PTM

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.

Essalmani, R., Jain, J., Susan-Resiga, D., Andréo, U., Evagelidis, A., Derbali, R. M., ... & Seidah, N. G. (2022). Distinctive roles of furin and TMPRSS2 in SARS-CoV-2 infectivity. Journal of Virology, 96(8), e00128-22.

Peacock, T. P., Goldhill, D. H., Zhou, J., Baillon, L., Frise, R., Swann, O. C., ... & Barclay, W. S. (2021). The furin cleavage site in the SARS-CoV-2 spike protein is required for transmission in ferrets. Nature microbiology, 6(7), 899-909.

Johnson, B. A., Xie, X., Bailey, A. L., Kalveram, B., Lokugamage, K. G., Muruato, A., ... & Menachery, V. D. (2021). Loss of furin cleavage site attenuates SARS-CoV-2 pathogenesis. Nature, 591(7849), 293-299.

Osman, E. E. A., Rehemtulla, A., & Neamati, N. (2021). Why all the fury over furin?. Journal of Medicinal Chemistry, 65(4), 2747-2784.

Wu, Y., & Zhao, S. (2021). Furin cleavage sites naturally occur in coronaviruses. Stem cell research, 50, 102115.

Wu, C., Zheng, M., Yang, Y., Gu, X., Yang, K., Li, M., ... & Li, H. (2020). Furin: a potential therapeutic target for COVID-19. Iscience, 23(10), 101642.

Bestle, D., Heindl, M. R., Limburg, H., Pilgram, O., Moulton, H., Stein, D. A., ... & Böttcher-Friebertshäuser, E. (2020). TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells. Life science alliance, 3(9).

Braun, E., & Sauter, D. (2019). Furin‐mediated protein processing in infectious diseases and cancer. Clinical & translational immunology, 8(8), e1073.

Izaguirre, G. (2019). The proteolytic regulation of virus cell entry by furin and other proprotein convertases. Viruses, 11(9), 837.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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For research use only. Not intended for any clinical use.

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