Registration for PeproTech.com is no longer available. To order your PeproTech products online, register or logon to ThermoFisher.com.

Growth Factors & Cytokines

Recombinant Human TGF-α

Detalles del Producto

Nùmero de Catalogo 100-16A
Descripcion
Recombinant Human TGF-α

TGF-α is an EGF-related polypeptide growth factor that signals through the EGF receptor, and stimulates the proliferation of a wide range of epidermal and epithelial cells. It is produced by monocytes, keratinocytes, and various tumor cells. TGF-α induces anchorage-independence transformation in cultured cells. Human, murine and rat TGF-α are cross-species reactive. Recombinant Human TGF-α is a 50 amino acid polypeptide (5.5 kDa) which shares approximately 40% sequence homology with EGF, including 6 conserved cysteine residues, which form 3 intramolecular disulfide bonds.

Source: E.coli

Synonyms: Transforming Growth Factor-α, Sacroma growth factor, TGF-type I, ETGF

AA Sequence: VVSHFNDCPD SHTQFCFHGT CRFLVQEDKP ACVCHSGYVG ARCEHADLLA

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BALB/c 3T3 cells is ≤ 0.2 ng/ml, corresponding to a specific activity of ≥ 5 x 106 units/mg.

Recombinant Human TGF-α Biological Activity Graph

Calculated Molecular Weight: 5.5 kDa

Accession Number: P01135

Gene ID: 7039

Endotoxin: Endotoxin level is < 0.1 ng/ug of protein (< 1 EU/ug)

crossreactivity:
Country Of Origin: USA

Not for human use.

Research Interest

product.subtitle.recentcitations

Primer autor
Yang, Q
Titulo
FOXM1 regulates glycolysis in nasopharyngeal carcinoma cells through PDK1.
Citar
Journal of Cellular and Molecular Medicine; 26(13) pg3783-3796
PudMed id
Primer autor
Zhang, B
Titulo
A new protocol for long-term culture of a specific subpopulation of liver cancer stem cells enriched by cell surface markers.
Citar
FEBS Open Bio; 10(9) pg1737-1747
PudMed id
Primer autor
Lundby, A
Titulo
Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites.
Citar
Cell; 179(2) pg543-560.e26
PudMed id

product.subtitle.productreviews

Comentarios existentes
High quality and better price
This product worked well for my project.  The price is reasonable and lower than most of vendors.
De:  Jin | Fecha:  26/08/2020