Key features and details
- Purity: > 95% HPLC
- Suitable for: Blocking
Product nameFurin peptide
See all Furin proteins and peptides
Purity> 95 % HPLC.
Peptides are analyzed by Reverse-Phase HPLC (RP-HPLC) in order to determine purity. Identities are confirmed by MALDI-MS.
Our Abpromise guarantee covers the use of ab4989 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
This peptide may be used for neutralization and control experiments with the polyclonal antibody that reacts with this product and furin convertase, catalog ab3467. Using a solution with equal weights per unit volume of peptide and corresponding antibody will yield a solution with a large molar excess of peptide that is able to competitively bind the antibody.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Reconstitution>95% pure, lyophilized synthetic peptide. Reconstitute with 0.1 ml of distilled water.
- Dibasic processing enzyme
- Dibasic-processing enzyme
- FES upstream region
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
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab4989 has not yet been referenced specifically in any publications.