Human TGF-β1

Human TGF-β1

Recombinant human TGF-β1 is used for the cultivation of embryonic stem cells and induced pluripotent stem cells, but can also promote Th17 and Treg differentiation of T cells. The transforming growth factor (TGF) beta 1 is associated with diverse processes including chondrogenesis, wound healing, embryogenesis, proliferation, and apoptosis.


Human TGF-β1 can be used for a variety of applications, including:
  • In vitro differentiation of naive CD4+ T cells towards TH 17 cells.
  • In vitro generation of FoxP3+ inducible regulatory T cells (iTregs).
  • Embryonic stem cell differentiation models, for example, for vasculogenesis and angiogenesis.
  • In vitro chondrogenesis of mesenchymal progenitor cells and redifferentiation of expanded chondrocytes.

Background information

Transforming growth factor β1 (TGF-β1) belongs to a family of homologous, disulfide-linked, homodimeric proteins. These highly pleiotropic cytokines inhibit proliferation of most cells, but can promote the growth of mesenchymal cells and enhance extracellular matrix formation. The pivotal function of TGF-β1 in the immune system is to mediate immunosuppression and maintain tolerance by regulating lymphocyte proliferation, differentiation, and survival. In addition, TGF-β1 controls inflammatory responses through chemotactic attraction and activation of inflammatory cells and fibroblasts. TGF-β1 is produced by many cell types, but is reported to be most abundant in mammalian platelets and bone. All three TGF-β members are synthesized as an homodimeric precursor of 390 residues, which is intracellularly processed by proteolysis into a 112 aa form. The resulting N-terminal latency-associated peptide (LAP) remains non-covalently associated with the TGF-β dimer, and the complex binds to another protein called Latent TGF-β-Binding Protein (LTBP), forming a larger complex called Large Latent Complex (LLC). The LLC is secreted into the extracellular matrix, and prevents the binding of TGF-b to its specific cell surface receptor. Several extracellular factors such as matrix metalloproteases, low pH, reactive oxigen species and thrombospondin-1 can induce release of the active mature TGF-b dimer from the inactive complex. This sophisticated mechanism of activation is important for a fine-tuning of TGF-β signaling. Human TGF-b1 is a recombinant homodimer corresponding to the fully mature form of TGF-β1 without LAP. The amino acid sequence of human TGF-β1 shares 99% identity with TGF-β1 from mouse and rat, therefore human TGF-b1 is commonly used also for mouse cell culture.

Quality description

cytokines offer the convenience of high and well-defined biological activities and allow exact unit dosing for demanding applications. The biological activity is determined after lyophilization and reconstitution, and normalized to WHO/NIBSC standards whenever available. In general, endotoxin levels are <0.01 ng/μg (<0.1 EU/μg), and purities are >97%. Lot-specific certificates of analysis are available on request (

Biological activity

  • Inhibition of IL-5 induced TF-1 cells (NIBSC 89/514)
  • premium grade: ≥ 5×
    (typical activity: ≥ 8×
  • Selected references

    1. Nguyen, T. L. et al. (2011) Antigen-specific TGF-β-induced regulatory T cells secrete chemokines, regulate T cell trafficking, and suppress ongoing autoimmunity. J. Immunol. 187(4): 1745-1753
    2. Souza-Fonseca-Guimaraes, F. et al. (2012) NK cell tolerance to TLR agonists mediated by regulatory T cells after polymicrobial sepsis. J. Immunol. 188(12): 5850-5858
    3. Randall, L. A. et al. (1993) A novel, sensitive bioassay for transforming growth factor β. J. Immunol. Methods 164: 61-67
  • Certificates

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Product options: 4
HEK293 cells
5 µg
CHF  287.00
HEK293 cells
25 µg
CHF  630.00
HEK293 cells
100 µg
CHF  1'773.00
HEK293 cells
µg (liquid)
CHF  7'892.00

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