Product Information
Reconstitution:
With carrier: Add sterile 4 mM HCl containing 0.1% BSA to a final hTGF-β2 concentration of greater than 50 μg/ml. Solubilize for 30 minutes at room temperature with occasional gentle vortexing.
Carrier free: Add sterile 4 mM HCl, or 4 mM HCl containing protein to minimize absorption of hTGF-β2 to surfaces. Solubilize for 30 minutes at room temperature with occasional gentle vortexing. Stock hTGF-β2 should be greater than 50 μg/ml.
MW (kDa) | 12 |
Purity | >98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hTGF-β2. All lots are greater than 98% pure. |
Endotoxin | Less than 0.01 ng endotoxin/1 μg hTGF-β2. |
Activity | 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. |
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. |
Recombinant human TGF-β2 (hTGF-β2) Ala303-Ser414 (Accession #NP_003229) was expressed in human 293 cells at Cell Signaling Technology.
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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