Synthetic peptide corresponding to Human Furin (N terminal). (Peptide available as ab41397)
Furin is ubiquitously expressed at low levels, but found in highest concentration in the liver and kidneys, lower levels in brain, spleen, thymus, and smaller levels in most other tissues. Endogenous furin was detected in lysates from LNCaP and DU145 prostate carcinoma cell lines.
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
1/1,000 when using colorimetric substrates such as BCIP/NBT and 1/5,000 for chemiluminescent substrates. Glycosylation and other post-translational modifications make the pre-pro furin run at 110-104 kDa, the mature furin at 98-95 kDa and shed furin at 90 kDa. Dilution optimised using Chromogenic detection.
Use at an assay dependent concentration. PubMed: 20454619
Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.
Seems to be expressed ubiquitously.
Belongs to the peptidase S8 family. Furin subfamily. Contains 1 homo B/P domain.
Contains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface.
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.
Golgi apparatus > trans-Golgi network membrane. Cell membrane. Shuttles between the trans-Golgi network and the cell surface. 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.
Proprotein convertase subtilisin/kexin type 3 antibody
Anti-Furin antibody - Aminoterminal end 画像
Western blot - Anti-Furin antibody - Aminoterminal end (ab28547)
All lanes : Anti-Furin antibody - Aminoterminal end (ab28547) at 1/1000 dilution
Lane 1 : Furin at 0.05 µg Lane 2 : Furin at 0.01 µg Lane 3 : Furin at 0.001 µg
Predicted band size : 88 kDa Observed band size : 88 kDa
Immunohistochemistry (Frozen sections) - Furin antibody - Aminoterminal end (ab28547)Image from Hajdin K et al, PLoS One. 2010 May 3;5(5):e10445 Fig 4.
ab28547 staining Furin (red) in mouse endothelial tissue by Immunohistochemistry (Frozen sections). Mice were perfused, tumor and control organs were dissected and frozen in O.C.T. embedding medium. 10 µm cryosections were washed with PBS, fixed for 15 minutes in ice-cold methanol and air-dried. Primary antibody was used at a dilution of 1/1500. The secondary antibody was an Alexa Fluor 594-labeled IgG at a 1/300 dilution. Nuclei are visualized by DAPI staining (blue).
Anti-Furin antibody - Aminoterminal end (ab28547) 使用論文
This product has been referenced in:
Jaaks P et al. The proprotein convertase furin is required to maintain viability of alveolar rhabdomyosarcoma cells. Oncotarget7:76743-76755 (2016).
Read more (PubMed: 27572312) »
Sathyamurthy M et al. Characterization and expression of proprotein convertases in CHO cells: Efficient proteolytic maturation of human bone morphogenetic protein-7. Biotechnol BioengN/A:N/A (2014).
Read more (PubMed: 25219685) »