Recombinant Human TGF-α (Animal-Free)

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Other Names
TGFA
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717602 100 µg £147
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Description

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
Technical Data Sheet (pdf)

Product Details

Source
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.
Purity
>98%, as determined by Coomassie stained SDS-PAGE and HPLC analysis.
Formulation
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.
Activity
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.
Application

Bioassay

Antigen Details

Structure
Cytokine
Distribution
Expressed by many human tumors, human granulosa cells, theca cells, keratinocytes, and a number of epithelial cells.
Function
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.
Interaction
Human granulosa cells and epithelial cells.
Ligand/Receptor
EGFR
Bioactivity
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
UniProt
View information about TGF-alpha on UniProt.org

Related FAQs

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.

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.

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)
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.

Go To Top Version: 3    Revision Date: 05/06/2014

For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

BioLegend Inc., 8999 BioLegend Way, San Diego, CA 92121 www.biolegend.com
Toll-Free Phone: 1-877-Bio-Legend (246-5343) Phone: (858) 768-5800 Fax: (877) 455-9587

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