- Regulatory Status
- RUO
- Other Names
- WNT Inhibitory Factor-1, Wnt Inhibitory Factor-1, WIF1 , Wnt/β-catenin signaling pathway
- Ave. Rating
- Submit a Review
- Product Citations
- publications
Cat # | Size | Price | Quantity Check Availability | Save | ||
---|---|---|---|---|---|---|
564504 | 25 µg | $205 | ||||
564506 | 100 µg | $350 |
Wnt Inhibitory Factor-1 (WIF-1) is an extracellular antagonist of the Wnt/β-catenin signaling pathway and is a critical mediator of tissue homeostasis and repair. Aberrant activation of the Wnt/β-catenin signaling pathway has been observed in numerous human diseases. In the presence of Wnt, a receptor complex is formed between Frizzled and LRP5/6 stabilized β-catenin activating Wnt-responsive genes. Wnt antagonists can be divided into two groups based on their action on Wnt/β-catenin signaling pathway. The first group of antagonists includes WIF-1, belonging to the secreted frizzled-related protein (sFRP) family, and Cerberus. They inhibit Wnt/β-catenin signaling pathway through directly binding to Wnt ligands to alter their ability to form the receptor complex. The second group, including the Dickkopf (DKK) family, inhibits Wnt signaling by binding to LRP5/6. WIF-1 was initially identified in the human retina, and highly conserved homologues have been described in various vertebrates, fishes, amphibians, and mammals. WIF-1 is abundant in brain, the nervous system, lungs, retina, cartilages, and heart. Human WIF-1 has 379 amino acid, an N-terminal signal sequence, a unique WIF domain (WD) between 38-178 amino acids, five epidermal growth factor (EGF)-like repeats, and a C-terminal hydrophilic domain. WIF-1 is expressed during early and late developmental stages. WIF-1 is upregulated during later phases of osteoblast differentiation. WIF-1 silencing, driven by promoter hypermethylation, has been associated with numerous cancers including colorectal, prostate, bladder, melanoma, lung, bone cancer and leukemia. Overexpression of WIF-1 inhibits the growth of lung and bladder cancers cells.
Product DetailsProduct Details
- Source
- Human WIF-1, amino acid (Gly29-Trp379) (Accession: #AAD25402), with carboxi terminus GGS-6H tag, was expressed in CHO cells.
- Molecular Mass
- The 360 amino acid recombinant protein has a predicted molecular mass of approximately 39.46 kD. The DTT-reduced and non-reduced protein migrate at approximately 48 kD by SDS-PAGE. The predicted N-terminal amino acid is Gly.
- Purity
- > 95%, as determined by Coomassie stained SDS-PAGE.
- Formulation
- 0.22 µm filtered protein solution is in PBS.
- Endotoxin Level
- Less than 0.1 EU per µg cytokine as determined by the LAL method.
- Concentration
- 25 µg size is bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
- Storage & Handling
- Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
- Activity
- Recombinant human WIF-1 inhibits the activity of recombinant mouse Wnt3a (Cat. No. 772301) in HEK293 Wnt TCF reporter cells. The ED50 for this effect is 3 – 15 µg/mL.
- Application
-
Bioassay
- Application Notes
-
BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are validated in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.
Antigen Details
- Distribution
-
Expressed in nervous system, lung, eye, intestine, heart, osteoclast
- Function
- Negative regulator of Wnt signaling pathway, embryonic development, mesoderm segmentation, and tumor suppressor; upregulated in osteoblast differentiation
- Ligand/Receptor
- Wnt3a, Wnt4, Wnt5a, Wnt7a, Wnt9a and Wnt11 through the WD. Olfactomedin 1 (neuronal differentiation-related protein in Zebrafish)
- Bioactivity
- Human WIF-1 inhibits the activity of Wnt3a.
- Cell Type
- Endothelial cells, Macrophages, NK cells, T cells
- Biology Area
- Neuroscience
- Molecular Family
- Tumor Suppressors
- Antigen References
-
- Deng X, et al. 2017. Mol Med Rep. 16:7497.
- Guo H, et al. 2017. Oncotarget. 8:2550.
- Hsieh JC, et al. 1999. Nature. 398:431.
- Hunter DD, et al. 2004. Molr and Cell Neurosc. 27:477.
- Kawano Y, et al. 2003. J Cell Science. 116:2627.
- Liu P, et al. 2017. Scientific Reports. 7:1580.
- Malinauskas T, et al. 2011. Nature Struc & Mole Biol. 18:886.
- Nakaya N, et al. 2008. J of Neurosc. 28:7900.
- Sanchez-Hernandez D, et al. 2012. Development. 139:3849.
- Vaes BL, et al. 2005. Bone. 36:803.
- Gene ID
- 11197 View all products for this Gene ID
- UniProt
- View information about WIF-1 on UniProt.org
Related FAQs
- Why choose BioLegend recombinant proteins?
-
• Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
• Greater than 95% Purity or higher, tested on every lot of product.
• 100% Satisfaction Guarantee for quality performance, stability, and consistency.
• Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
• Bulk and customization available. Contact us.
• Learn more about our Recombinant Proteins. - How does the activity of your recombinant proteins compare to competitors?
-
We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
- What is the specific activity or ED50 of my recombinant protein?
-
The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.
- Have your recombinants been tested for stability?
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Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
- Does specific activity of a recombinant protein vary between lots?
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Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
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Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)
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