Furin (E2Y2F) Rabbit mAb #64709
- WB
- IHC
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 90 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunohistochemistry (Paraffin) | 1:100 - 1:400 |
Storage
Protocol
Specificity / Sensitivity
Furin (E2Y2F) Rabbit mAb recognizes endogenous levels of total furin protein. Non-specific diffuse staining was observed in pancreatic islets by immunohistochemistry.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala237 of human furin protein.
Background
The proprotein convertases (PCs) are enzymes that activate precursor proteins through proteolytic cleavage within the secretory pathway. PCs comprise several enzymes that are basic amino acid-specific proteinases (furin, PC1/3, PC2, PC4, PACE4, PC5/6, and PC7), as well as nonbasic amino acid convertases (S1P and PC9) (1). PCs have a common structure that includes an N-terminal signal peptide for secretory pathway targeting; a pro-domain that is thought to act as an intramolecular chaperone; a catalytic domain containing the active site; a P-domain that contributes to the overall folding of the enzyme by regulating stability and both calcium- and pH-dependence; and a C-terminal domain that interacts with the membrane (2). PCs act in a tissue- and substrate-specific fashion to generate an array of bioactive peptides and proteins from precursors, both in the brain and in peripheral tissues (3). The SARS-CoV-2 coronavirus contains an inactive precursor spike glycoprotein, with a distinct furin cleavage site at the S1/S2 domain junction. Cleavage by furin "primes" the spike protein for binding to the ACE2 receptor and subsequent viral entry to the host cell (4-6). Loss of the furin cleavage site has been shown to drastically reduce the virulence of the SARS-CoV-2 virus (6-8). Furin cleavage sites are seen in a variety of other viral pathogens as well, including other CoV family members, HIV, avian influenza strains, and Ebola (6,8). In addition, furin has been proposed as a therapeutic target in cancer, and in regard to NMDA receptor-associated pathologies in the brain (9,10).
- Scamuffa, N. et al. (2006) FASEB J 20, 1954-63.
- Fugère, M. and Day, R. (2005) Trends Pharmacol Sci 26, 294-301.
- Seidah, N.G. and Chrétien, M. (1999) Brain Res 848, 45-62.
- Peacock, T.P. et al. (2021) Nat Microbiol, doi: 10.1038/s41564-021-00908-w.
- Klimstra, W.B. et al. (2020) J Gen Virol 101, 1156-1169.
- Hoffmann, M. et al. (2020) Mol Cell 78, 779-784.e5.
- Johnson, B.A. et al. (2021) Nature 591, 293-299.
- Johnson, B.A. et al. (2020) bioRxiv, 2020.08.26.268854. doi: 10.1101/2020.08.26.268854.
- Scamuffa, N. et al. (2008) J Clin Invest 118, 352-63.
- Yamada, M. et al. (2018) Sci Rep 8, 5212.
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