Product nameAnti-Furin antibody
See all Furin primary antibodies
DescriptionRabbit polyclonal to Furin
SpecificityDetects Furin from canine and mouse cells as well as transfected human Furin. This antibody does not detect endogenous Furin from BSC-40, HeLa, J774A.1 BPAEC, or CHO cells nor from rat skeletal muscle, spleen, kidney, ovary, testes, heart, or brain tissue.
Tested applicationsSuitable for: ICC, Inhibition Assay, ICC/IF, IP, WB, IHC-Pmore details
Species reactivityReacts with: Mouse, Rat, Sheep, Hamster, Dog, Human, Pig, Non human primates
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Storage bufferPreservative: 0.05% Sodium azide
Constituents: 0.1% BSA, 99% PBS
Concentration information loading...
PurityImmunogen affinity purified
Primary antibody notesFurin is a membrane-associated, calcium-dependent, serine protease that belongs to the subtilisin-like prohormone convertase (PC) family. Members of this family of cellular enzymes cleave most prohormones and neuropeptide precursors. Numerous other cellular proteins, some viral proteins, and bacterial toxins that are transported by the constitutive secretory pathway are also targeted for maturation by PCs. Furin and other PC family members share structural similarities which include a heterogeneous ~10 kDa amino-terminal proregion, a highly conserved ~55 kDa subtilisin-like catalytic domain, and carboxyl-terminal domain that is heterogeneous in length and sequence. These enzymes become catalytically active following proregion cleavage within the appropriate cellular compartment. Furin is the only known PC to possess a transmembrane domain. Cleavage of target proteins occurs at the carboxyl-terminus of the furin consensus sequence, RX(K/R)R. It has been shown that the acidic peptide sequence, C771PSDSEEDEG780, localizes furin to the trans-Golgi-network. Phosphorylation of serine residues within this region modulates intracellular routing of Furin protein. An additional signaling domain includes the tetrapeptide sequence, Y759KGL762, which directs internalization from the cell surface.
Immunizing Peptide (Blocking)
Our Abpromise guarantee covers the use of ab3467 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|ICC||Use at an assay dependent concentration.|
|Inhibition Assay||Use at an assay dependent concentration.|
|ICC/IF||Use at an assay dependent concentration. PubMed: 18174282|
|WB||Use at an assay dependent concentration. Detects a band of approximately 100 kDa (predicted molecular weight: 87 kDa).Can be blocked with Furin peptide (ab4989).
Representing Furin in BSC-40 cells transfected with the human Furin gene.
|IHC-P||Use at an assay dependent concentration. PubMed: 23418414|
FunctionFurin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif.
Tissue specificitySeems to be expressed ubiquitously.
Sequence similaritiesBelongs to the peptidase S8 family. Furin subfamily.
Contains 1 homo B/P domain.
DomainContains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface.
modificationsThe 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.
Cellular localizationGolgi 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.
- Information by UniProt
- Dibasic processing enzyme antibody
- Dibasic-processing enzyme antibody
- FES upstream region antibody
Immunolocalization of endogenous furin in mouse 3T3 cells with ab3467.
All lanes : Anti-Furin antibody (ab3467) at 1 µg/ml
Lane 1 : HeLa (Human epithelial carcinoma cell line) Whole Cell Lysate
Lane 2 : A431 (Human epithelial carcinoma cell line) Whole Cell Lysate
Lysates/proteins at 10 µg per lane.
All lanes : Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (ab97080) at 1/5000 dilution
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size: 87 kDa
Observed band size: 63 kDa why is the actual band size different from the predicted?
Exposure time: 90 seconds
The band observed at 63 kDa could potentially be a cleaved form of Furin due to the presence of a 24 amino acid signal peptide and a 83 amino acid propeptide.
ab3467 staining Furin in human A549 cells by Immunocytochemistry/ Immunofluorescence.
Cells were fixed with paraformaldehyde, permeabilized using 0.1% Triton X-100, blocked with 1% BSA/ 5%FBS/PBS for 1 hour at 25°C and then incubated with ab3467 at a 1/100 dilution for 1 hour at 25°C. The secondary used was an Alexa-Fluor 546 conjugated goat anti-rabbit polyclonal used at a 1/500 dilution.
Cells were counterstained with DAPI (436nM, 5 mins) and Phalloidin-633 (1unit/coverslip) and mounted with prolong gold. No staining seen in secondary control and furin staining was punctate and throughout the cytoplasm.
This product has been referenced in:
- Chang JC et al. SOST/Sclerostin Improves Posttraumatic Osteoarthritis and Inhibits MMP2/3 Expression After Injury. J Bone Miner Res 33:1105-1113 (2018). Read more (PubMed: 29377313) »
- Zhao G et al. Influence of a Coronary Artery Disease-Associated Genetic Variant on FURIN Expression and Effect of Furin on Macrophage Behavior. Arterioscler Thromb Vasc Biol 38:1837-1844 (2018). Read more (PubMed: 29976768) »