||Recombinant mouse TGF-β1 (hTGF-β1) Ala279-Ser390 was expressed in human 293 cells.
||TGF-β1 activities include proliferation, angiogenesis, and promotion or inhibition of many immune events. TGF-β1 is produced by a number of cell types including regulatory T cells, fibroblasts, epithelial cells, and endothelial cells. TGF-β1 binds to TβRII homodimer, which then complexes with TβRI homodimer. The oligomeric receptor complex phosphorylates subsets of the Smad proteins that then act to induce and repress a number of target genes. TGF-β1 binding can also activate the Erk2, p38, and JNK pathways via TAK1. TGF-β1 appears to promote late stage progression and metastasis in some cancers.
||human 293 cells
||With carrier: Lyophilized from a 0.22 μm filtered solution of 20 mM citrate, pH 3.0 containing 100 mM NaCl and 20 μg BSA per 1 μg mTGF-β1. Carrier free: Lyophilized from a 0.22 μm filtered solution of 20 mM citrate, pH 3.0 containing 100 mM NaCl.
||The bioactivity of recombinant mTGF-β1 was determined by assessing inhibition of IL-4 induced HT-2 cell proliferation. The ED50 of each lot is between 40-200 pg/ml.
||Recombinant mTGF-β1 contains no "tags" and the nonglycosylated protein has a calculated MW of 12,810. DTT-reduced protein migrates as a 13 kDa polypeptide and the non-reduced cystine-linked homodimer migrates as a 25 kDa protein. The expected amino-terminal ALDTN of recombinant mTGF-β1 was verified by amino acid sequencing.
||Less than 0.01 ng endotoxin/1 μg mTGF-β1.
||>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant mTGF-β1.