Human Transforming Growth Factor β2 (hTGF-β2) #8406

Recombinant human TGF-β2 (hTGF-β2) Ala303-Ser414 (Accession #NP_003229) was expressed in human 293 cells at Cell Signaling Technology.

Purity:

>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hTGF-β2. All lots are greater than 98% pure.

Molecular Formula:

Recombinant hTGF-β2 contains no "tags" and the nonglycosylated protein has a calculated MW of 12,719. DTT-reduced protein migrates as a 12 kDa polypeptide and the non-reduced cystine-linked homodimer migrates as a 24 kDa protein. The expected amino-terminal ALDAA of recombinant hTGF-β2 was verified by amino acid sequencing.

Bioactivity:

The bioactivity of recombinant hTGF-β2 was was determined by assessing inhibition of IL-4 induced HT-2 cell proliferation. The ED₅₀ of each lot is between 0.1-0.3 ng/ml.

Endotoxin:

Less than 0.01 ng endotoxin/1 μg hTGF-β2.

Formulation:

With carrier: Lyophilized from a 0.22 μm filtered solution of 35% acetonitrile and 0.1% trifluoroacetic acid containing 20 μg BSA per 1 μg hTGF-β2. Carrier free: Lyophilized from a 0.22 μm filtered solution of 35% acetonitrile and 0.1% trifluoroacetic acid.

Storage:

Stable in lyophilized state at 4°C for 1 year after receipt. Sterile stock solutions reconstituted with carrier protein are stable at 4°C for 2 months and at -20°C for 6 months. Avoid repeated freeze-thaw cycles.Maintain sterility. Storage at -20°C should be in a manual defrost freezer.

TGF-β2 is produced by eosinophils, astrocytes, glioblastoma and other cancer derived cell types (1-6). TGF-β2 inhibits antigen-induced T-cell proliferation, inhibits epithelial cell proliferation, induces mesenchymal cell proliferation and has cell specific effects on apoptosis (1-8). TGF-β2 binds to TβRII and binding is promoted by TβRIII. TβRI then complexes with TβRII and TβRIII (3,5). Signaling involves phosphorylation of the SMAD proteins (2,3,9). TGF-β2 also activates Erk2, p38, and JNK pathways (9). Knockout of TGF-β2 in mice severely impacts heart, lung and eye development (10).

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2. Siegel, P.M. and Massagué, J. (2003) Nat Rev Cancer 3, 807-21.
3. Bierie, B. and Moses, H.L. (2006) Nat Rev Cancer 6, 506-20.
4. Hinz, S. et al. (2007) Cancer Res 67, 8344-50.
5. Damstrup, L. et al. (1993) Br J Cancer 67, 1015-21.
6. Constam, D.B. et al. (1992) J Immunol 148, 1404-10.
7. Zhang, H. et al. (2008) Immunology 124, 304-14.
8. Dufour, C. et al. (2008) Am J Physiol Endocrinol Metab 294, E794-801.
9. Moustakas, A. and Heldin, C.H. (2009) Development 136, 3699-714.
10. Dünker, N. and Krieglstein, K. (2000) Eur J Biochem 267, 6982-8.

Zuckerwise, L. et al. (2016) Oncotarget 7, 38398-38407.

• Data sheet (631KB)
• MSDS PDF