TGF-α was initially identified in the culture medium of several transformed cell lines. TGF-α is structurally and functionally related to the epidermal growth factor and belongs to the EGF subfamily that also includes amphiregulin (AR), heparin binding EGF-like growth factor (HB-EGF), betacellulin (BTC), epiregulin (EPR), and epigen (EPG). TGF-α is derived from a transmembrane precursor (20-22 kD); pro-TGFα undergoes several posttranslational modifications that include N- and O-linked glycosylation and palmitoylation. The pro-TGFα includes a glycosylated N-terminal domain, a TGF-α region with the EGF-like motif, a linker sequence that joins the ectodomain to the transmembrane domain, and an intracellular portion. TGF-α is proteolytically released from the membrane by tumor necrosis factor-α converting enzyme (TACE/ADAM-17). TGF-α is cleaved at the N- and C-terminus of the EGF motif; the proteolytic cleavage at the C-terminus is required to release the soluble form. The N-terminal cleavage of pro-TGFα occurs at the cell surface by TACE-independent activity. TGF-α plays a key role regulating follicle development and tumorigenesis. TGF-α and its receptor are highly expressed in papillary thyroid carcinoma. Also, TGF-α polymorphism has been associated with oral birth defects.Product Details
- Human TGF-α, amino acids (Val40-Ala89) (Accession# NM_003236) was expressed in E. coli.
- Molecular Mass
- The 55 amino acid recombinant protein has a predicted Molecular mass of 5.5 kD. The predicted N-terminal amino acid is Val.
- >98%, as determined by Coomassie stained SDS-PAGE and HPLC analysis.
- Lyophilized, carrier-free.
- Endotoxin Level
- Less than 0.1 ng per µg of protein.
- Storage & Handling
- Unopened vial can be stored at -20°C or -70°C. For maximum results, quick spin vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. It is recommended to further dilute in a buffer, such as 5% Trehalose, and store working aliquots at -20°C to -80°C. Avoid repeated freeze/thaw cycles.
- The expected ED50 is ≤ 0.2 ng/ml, corresponding to a specific activity of ≥ 5 x 106 units/mg, as determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells.
- Product Citations
- Expressed by many human tumors, human granulosa cells, theca cells, keratinocytes, and a number of epithelial cells.
- TGF-α has angiogenic properties. It is a potent mitogen, and it induces KGN (human granulosa cell tumor) cell proliferation, cell viability, cell cycle progression, and cell migration. Also, it induces cell proliferation and differentiation in epithelial and neuronal cells.
- Human granulosa cells and epithelial cells.
- Human TGF-α is able induce proliferation of Balb/c 3T3 cells.
- Cell Type
- Neural Stem Cells, Mesenchymal Stem Cells, Hematopoietic stem and progenitors, Embryonic Stem Cells
- Biology Area
- Cell Biology, Signal Transduction, Stem Cells
- Molecular Family
- Growth Factors, Cytokines/Chemokines
- Antigen References
1. Derynck R, et al. 1984. Cell 38:287.
2. Sunnarborg SW, et al. 2002. J. Biol. Chem. 277:12838.
3. Juanes PP, et al. 2005. Biochem. J. 389:161.
4. Sull JW, et al. 2009. Hum. Genet. 126:385.
5. Degl’Innocenti D, et al. 2010. PLoS One 5:e12701.
6. Wang C, et al. 2012. PLoS One 7:e48299.
- Gene ID
- 7039 View all products for this Gene ID
- View information about TGF-alpha on UniProt.org
- 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?
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?
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?
- Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)