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- Regulatory Status
- RUO
- Other Names
- Fibroblast growth factor 12, Fibroblast growth factor homologous factor 1 (FHF-1), Myocyte-activating factor.
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- Product Citations
- publications
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Human FGF-12 binds to immobilized human FGFR4 at 5 µg/ml. The ED50 = 0.01 -0.05 µg/ml
| Cat # | Size | Price | Quantity Check Availability | Save | ||
|---|---|---|---|---|---|---|
| 767704 | 25 µg | £182 | ||||
| 767708 | 500 µg | £1283 | ||||
FGF-12 is a member of the fibroblast growth factor family, belonging to the FGF-11 subfamily. FGF-12 is expressed in central nervous system. Two alternative splicing forms were identified, called FGF12A and FGF12B. FGF12B lacks the first N-terminal 66 amino acids and is substituted by only four residues. Unlike most of FGF members, FGF-12 lacks a signal peptide but contains a NLS sequence (nuclear localization signal) (a.a. 11-38). In the transfected cells, FGF-12 was accumulated in the nucleus and not secreted. Though FGF-12 can bind to heparin, FGF-12 fails to activate FGFRs, determined by a proliferation assay of FGFRs-expressing Baf3 cells. FGF-12 directly interacts with mitogen-activated protein kinase scaffolding protein islet brain 2 (IB2) in adult brain. Some evidences demonstrated that FGF-12 interacts with voltage-gated sodium channels (Nav) and modulates its activity. A single missense mutation of FGF-12, reducing the binding of the Nav, was identified in some patients of Brugada syndrome. Gain of function of FGF-12 mutation causes early-onset epileptic encephalopathy. In addition, FGF-12 negatively regulates NF-κB signaling in neurons via interacting with IKKγ/NEMO. Although FGF-12 is considered as an intracellular FGF, exogenesis FGF-12 can be internalized into the cytoplasm of intestinal epithelial cells, decreasing the radiation-induced apoptotic effect in mice. Recent study reports that mutations of FGF12 gene associates with pathogenesis of chronic disabled osteochondropathy, Kashin-Beck diseases.
Product DetailsProduct Details
- Source
- Human/Mouse FGF-12, amino acid Met1-Thr181 (Accession# NP_004104.3/ AAH30485.1) was expressed in E. coli.
- Molecular Mass
- The 181 amino acid recombinant protein has a predicted molecular mass of approximately 21 kD. The DTT-reduced protein migrates at approximately 21 by SDS-PAGE. The predicted N-terminal amino acid is Met.
- Purity
- > 98%, as determined by Coomassie stained SDS-PAGE.
- Formulation
- 0.22 µm filtered protein solution is in 20 mM MOPS, 150 mM Na2SO4, 1 mM EDTA, 10 mM DTT, pH 7.5.
- Endotoxin Level
- Less than 0.1 EU/µg cytokine as determined by the LAL method.
- Concentration
- 10 and 25 µg sizes are 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
- The activity was measured by the binding to human FGFR4-Fc using functional ELISA. The ED50 is 0.01-0.05 µg/ml when human FGFR4-Fc (cat # 752502) is immobilized at 5 µg/ml (100 µl/ well).
- Application
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Bioassay
- Application Notes
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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 verified 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
- Structure
- Growth factor
- Distribution
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Brain, eye, testis.
- Function
- FGF-12 modulates the activity of voltage-gated sodium channels and is involved in neuron development.
- Interaction
- Voltage-gated sodium channel, IB2
- Biology Area
- Angiogenesis, Cell Biology, Cell Motility/Cytoskeleton/Structure, Cell Proliferation and Viability, Immunology
- Molecular Family
- Cytokines/Chemokines, Growth Factors
- Antigen References
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- Ornitz DM, et al. 2015. Wiley Interdiscip Rev Dev Biol. 4:215.
- Smallwood PM, et al. 1996. Proc Natl Acad Sci USA. 93:9850.
- Olsen SK, et al. 2003. J Biol Chem. 278: 34226.
- Wang C, et al. 2011. J Biol Chem. 286: 24253.
- Nakayama F, et al. 2011. J Biol Chem. 286: 25823.
- Hartung H, et al. 1997. Mech Dev. 64:31.
- König HG, et al. 2012. J Cell Sci. 125:6058.
- Zhang F, et al. 2016. Funct Integr Genomics. 16: 13.
- Hennessey JA, et al. 2013. Heart Rhythm. 10: 1886.
- Siekierska A, et al. 2016. Neurology. 86: 2162.
- Gene ID
- 2257 View all products for this Gene ID 14167 View all products for this Gene ID
- UniProt
- View information about FGF-12 on UniProt.org
Related FAQs
- Why choose BioLegend recombinant proteins?
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• 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?
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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?
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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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