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.

Data and images for Human TGF-β1 (CHO)

Figures

Figure 1

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Human TGF-β1 activity assay.
The biological activity of Human TGF-β1, premium grade was determined by inhibition assay using IL-5-induced TF-1 cells.

Figure 1

Human TGF-β1 activity assay.
The biological activity of Human TGF-β1, premium grade was determined by inhibition assay using IL-5-induced TF-1 cells.

Figure 2

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SDS-PAGE of Human TGF-β1 (CHO), premium grade
under reduced (R) and non-reduced (NR) conditions.

Figure 2

SDS-PAGE of Human TGF-β1 (CHO), premium grade
under reduced (R) and non-reduced (NR) conditions.

Figure 3

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Mass spectrometry analysis (ESI-MS) of Human TGF-β1, premium grade (CHO). The Peak corresponds to the calculated molecular mass of 25572 Da.

Figure 3

Mass spectrometry analysis (ESI-MS) of Human TGF-β1, premium grade (CHO). The Peak corresponds to the calculated molecular mass of 25572 Da.

Specifications for Human TGF-β1 (CHO)

Overview

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.

Applications

Human TGF-β1 can be used for a variety of applications, including:
  • In vitro differentiation of naive CD4+ T cells towards Th17 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.

Detailed product information

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 a 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-β to its specific cell surface receptor. Several extracellular factors such as matrix metalloproteases, low pH, reactive oxygen species and thrombospondin-1 can induce release of the active mature TGF-β dimer from the inactive complex. This sophisticated mechanism of activation is important for a fine-tuning of TGF-β signaling. Human TGF-β1 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-β1 is commonly used also for mouse cell culture.

Biological activity

  • Inhibition of IL-5 induced TF-1 cells (NIBSC 89/514)
  • premium grade: ≥ 5×
    10
    6
    U/mg
    (typical activity: ≥ 8×
    10
    6
    U/mg
    )

Resources for Human TGF-β1 (CHO)

Documents and Protocols

Background information

Premium-grade cytokine benefits

Certificates

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References for Human TGF-β1 (CHO)

Publications

  1. Randall, L. A. et al. (1993) A novel, sensitive bioassay for transforming growth factor β. J. Immunol. Methods 164: 61-67

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