Recombinant Human TGF-α (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
TGFA
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Product Citations
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Human_TGF-a_CF_RECOM_1_070820_updated.png
Recombinant human TGF-α induces the proliferation of BALB/3T3 cells in a dose-dependent manner. The ED50 = 0.02 - 0.1 ng/mL.
  • Human_TGF-a_CF_RECOM_1_070820_updated.png
    Recombinant human TGF-α induces the proliferation of BALB/3T3 cells in a dose-dependent manner. The ED50 = 0.02 - 0.1 ng/mL.
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589902 10 µg $59
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589904 25 µg $101
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589906 100 µg $223
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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

Product Details

Source
Human TGF-α, amino acids (Val40-Ala89) (Accession# NM_003236) was expressed in E.coli.
Molecular Mass
The 50 amino acid recombinant protein has a predicted molecular mass of approximately 5.5 kD. The DTT-reduced and non-reduced protein migrate at approximately 8 and 6 kD by SDS-PAGE respectively. The N-terminal amino acid is Val.
Purity
>98%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in PBS.
Endotoxin Level
Less than 0.01 ng per 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
Recombinant human TGF-α induces the proliferation of BALB/3T3 in a dose-dependent manner. The ED50 = 0.02 - 0.1 ng/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 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.

Product Citations
  1. Mikuličić S, et al. 2019. Elife. 8. PubMed

Antigen Details

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, epithelial cells
Ligand/Receptor
EGFR
Cell Type
Embryonic Stem Cells, Hematopoietic stem and progenitors, Mesenchymal Stem Cells, Neural Stem Cells
Biology Area
Cell Biology, Signal Transduction, Stem Cells
Molecular Family
Cytokines/Chemokines, Growth Factors
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

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) = 10^6/ ED50 (ng/mL)

Go To Top Version: 2    Revision Date: 07/08/2020

For Research Use Only. Not for diagnostic or therapeutic use.

 

This product is supplied subject to the terms and conditions, including the limited license, located at www.biolegend.com/terms) ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.

 

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