The three mammalian isoforms of TGF-β, TGF-β1, β2, and β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. TGF-β2 has been shown to exert suppressive effects on IL-2-dependent T-cell growth, and may also have an autocrine function in enhancing tumor growth by suppressing immunosurveillance of tumor development. Recombinant Human TGF-β2 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.
Transforming Growth Factor-β2, Glioblastoma-derived T cell suppressor factor, BSC-1, Cetermin, Polyergin
AA Sequence (monomer):
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS
≥ 98% by SDS-PAGE gel and HPLC analyses.
Determined by its ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The ED50 was found to be ≤ 0.2 ng/ml, corresponding to a specific activity of ≥ 5 x 106 units/mg.
Calculated Molecular Weight:
Endotoxin level is < 0.1 ng/ug of protein (< 1 EU/ug)
250μg is the largest vial size for this product.
Larger sizes supplied as multiple 250μg vials.
Not for human use.