Furin peptide (ab4989)
Key features and details
- Purity: > 95% HPLC
- Suitable for: Blocking
Description
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Product name
Furin 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. -
Animal free
No -
Nature
Synthetic
Associated products
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Related Products
Specifications
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.
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Applications
Blocking
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Form
Lyophilized -
Additional notes
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.
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Concentration information loading...
Preparation and Storage
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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.
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Reconstitution>95% pure, lyophilized synthetic peptide. Reconstitute with 0.1 ml of distilled water.
General Info
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Alternative names
- Dibasic processing enzyme
- Dibasic-processing enzyme
- FES upstream region
see all -
Function
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. -
Tissue specificity
Seems to be expressed ubiquitously. -
Sequence similarities
Belongs to the peptidase S8 family. Furin subfamily.
Contains 1 homo B/P domain. -
Domain
Contains a cytoplasmic domain responsible for its TGN localization and recycling from the cell surface. -
Post-translational
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 localization
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. - Information by UniProt
Protocols
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.
Datasheets and documents
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Datasheet download
References (0)
ab4989 has not yet been referenced specifically in any publications.