Austral Biologicals GF-230 - Human transforming growth factor beta-1 (TGF beta-1) recombinant, 5 µg

Transforming Growth Factor Beta-1 (TGF beta-1), Human Recombinant

5 µg
$300.00
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Austral Biologicals GF-230 - Human transforming growth factor beta-1 (TGF beta-1) recombinant, 5 µg
  • Austral Biologicals GF-230 - Human transforming growth factor beta-1 (TGF beta-1) recombinant, 5 µg
  • Austral Biologicals GF-230 - Human transforming growth factor beta-1 (TGF beta-1) recombinant, 5 µg
Transforming Growth Factor Beta-1 (TGF beta-1), Human Recombinant

Transforming Growth Factor Beta-1 (TGF beta-1), Human Recombinant

Catalog no. GF-230-2
$300.00
Size5 µg

Human Transforming Growth Factor beta1 (TGF- beta1 ) is stimulatory for cells of mesenchymal origin and inhibitory for cells of epithelial or neuroectodermal origin. Mature TGF- beta1 is a disulfide-linked homodimer of two chains composed of 112 amino acid residues each. There is a 70% homology between human TGF- beta1 and human TGF- beta2. Human TGF- beta1 is produced in genetically engineered bacteria, and purified by sequential chromatography.

  • Molecular weight: 25 kDa (dimeric protein)
  • Purity: Over 98% pure by non-reduced SDS gel electrophoresis.
  • Storage: Store at +4°C.
  • Stability: Several months at +4°C.
  • Biological activity: The biological activity of human TGF-&# beta1 is determined by measuring the acidification of the culture medium (Rat-1 cells) exposed to the growth factor.
  • Formulation: 25 µL (0.20 mg/mL) in 5 mM HCl (pH 2.5). Some of the liquid in the vial could have been evaporated with changes in the final volume. However, the 5 µg of the protein are still inside the vial. We recommend, in order to control the proper concentration, to dilute the entire content to a known volume with 5mM HCl. Do not freeze this material.
  • References:

    1. Ichijo, H. et al.(1994) The Journal of Biological Chemistry, Vol 266, No. 33, May, 22459-22464
    2. Yan, Z., Winawer, S., and Friedman, E., (1994) The Journal of Biological Chemistry, Vol 269, No. 18, May, 13231-13237.

Publications using GF-230

The following scientific publications report use of this Austral Biologicals product:

  1. Upregulation of long noncoding RNA AP003419.16 predicts high risk of aging-associated idiopathic pulmonary fibrosis. Hao et al., Molecular Medicine Reports 16 8085-8091 (2017).
  2. 7‐Dehydrocholesterol (7‐DHC), But Not Cholesterol, Causes Suppression of Canonical TGF‐β Signaling and Is Likely Involved in the Development of Atherosclerotic Cardiovascular Disease (ASCVD). Huang et al., Journal of Cellular Biochemistry 118 1387-1400 (2017).
  3. Betulinic acid enhances TGF-β signaling by altering TGF-β receptors partitioning between lipid-raft/caveolae and non-caveolae membrane microdomains in mink lung epithelial cells. Chen et al., Journal of Biomedical Science 23 30 (2016).
  4. DMSO Enhances TGF‐β Activity by Recruiting the Type II TGF‐β Receptor From Intracellular Vesicles to the Plasma Membrane. Huang et al., Journal of Cellular Biochemistry 117 1568-1579 (2016).
  5. TIEG1 enhances Osterix expression and mediates its induction by TGFβ and BMP2 in osteoblasts. Subramaniam et al., Biochemical and Biophysical Research Communications 470 528-533 (2016).
  6. Krüppel-like factor KLF10 regulates transforming growth factor receptor II expression and TGF-β signaling in CD8+ T lymphocytes. Papadakis et al., American Journal of Physiology-Cell Physiology 308 C362-C371 (2015).
  7. Claudin 1 Mediates TNFα-Induced Gene Expression and Cell Migration in Human Lung Carcinoma Cells. Shiozaki et al., PLoS ONE 7 e38049 (2012).
  8. TIEG1/KLF10 Modulates Runx2 Expression and Activity in Osteoblasts. Hawse et al., PLoS ONE 6 e19429 (2011).
  9. Targeting the Transforming Growth Factor-β pathway inhibits human basal-like breast cancer metastasis. Ganapathy et al., Molecular Cancer 9 122 (2010).
  10. Cancer-Associated Transforming Growth Factor β Type II Receptor Gene Mutant Causes Activation of Bone Morphogenic Protein-Smads and Invasive Phenotype. Bharathy et al., Cancer Research 68 1656-1666 (2008).
  11. Cholesterol modulates cellular TGF‐β responsiveness by altering TGF‐β binding to TGF‐β receptors. Chen et al., Journal of Cellular Physiology 215 223-233 (2008).
  12. Cholesterol suppresses cellular TGF-β responsiveness: implications in atherogenesis. Chen et al., Journal of Cell Science 120 3509-3521 (2007).
  13. Prevention of TGF-β-induced apoptosis by interlukin-4 through Akt activation and p70S6K survival signaling pathways. Lin et al., Apoptosis 12 1659-1670 (2007).
  14. Inhibition of growth and metastasis of mouse mammary carcinoma by selective inhibitor of transforming growth factor-beta type I receptor kinase in vivo. Ge et al., Clinical Cancer Research 12 4315-4330 (2006).
  15. TGF-beta1 down-regulates ICAM-1 expression and enhances liver metastasis of pancreatic cancer. Sawada et al., Advances in Medical Sciences 51 60-65 (2006).
  16. IGFBP-3 activates TGF-β receptors and directly inhibits growth in human intestinal smooth muscle cells. Kuemmerle et al., American Journal of Physiology-Gastrointestinal and Liver Physiology 287 G795-G802 (2004).
  17. Decreased Tumorigenicity In Vivo When Transforming Growth Factor β Treatment Causes Cancer Cell Senescence. Katakura et al., Bioscience, Biotechnology, and Biochemistry 67 815-821 (2003).
  18. Advanced Glycosylation End Products Up-Regulate Connective Tissue Growth Factor (Insulin-Like Growth Factor-Binding Protein-Related Protein 2) in Human Fibroblasts: A Potential Mechanism for Expansion of Extracellular Matrix in Diabetes Mellitus. Twigg et al., Endocrinology 142 1760-1769 (2001).
  19. Growth Inhibition by Insulin-like Growth Factor-binding Protein-3 in T47D Breast Cancer Cells Requires Transforming Growth Factor-β (TGF-β) and the Type II TGF-β Receptor. Fanayan et al., Journal of Biological Chemistry 275 39146-39151 (2000).
  20. Differential Regulation of Insulin-Like Growth Factor-Binding Protein-3 Protease Activity in MCF-7 Breast Cancer Cells by Estrogen and Transforming Growth Factor-β1. Salahifar et al., Endocrinology 141 3104-3110 (2000).
  21. Expression of Profilin, an Actin-Binding Protein, in Rat Experimental Glomerulonephritis and Its Upregulation by Basic Fibroblast Growth Factor in Cultured Rat Mesangial Cells. Tamura et al., Journal of the American Society of Nephrology 11 423-433 (2000).
  22. An Active Site of Transforming Growth Factor-β1 for Growth Inhibition and Stimulation. Huang et al., Journal of Biological Chemistry 274 27754-27758 (1999).
  23. Identification of Two Smad4 Proteins in Xenopus. Masuyama et al., Journal of Biological Chemistry 274 12163-12170 (1999).
  24. Interactions of high affinity insulin-like growth factor-binding proteins with the type V transforming growth factor-beta receptor in mink lung epithelial cells. Leal et al., J Biol Chem 274(10):6711-6717 (1999).
  25. Activated Thyroglobulin Possesses a Transforming Growth Factor-β Activity. Huang et al., Journal of Biological Chemistry 273 26036-26041 (1998).
  26. Transforming Growth Factor β Peptide Antagonists and Their Conversion to Partial Agonists. Huang et al., Journal of Biological Chemistry 272 27155-27159 (1997).
  27. Transforming Growth Factor-β Regulation of Bone Morphogenetic Protein-1/Procollagen C-proteinase and Related Proteins in Fibrogenic Cells and Keratinocytes. Lee et al., Journal of Biological Chemistry 272 19059-19066 (1997).
  28. Overexpression of the TGFbeta-regulated zinc finger encoding gene, TIEG, induces apoptosis in pancreatic epithelial cells. Tachibana et al., Journal of Clinical Investigation 99 2365-2374 (1997).
  29. Salicylate or Aspirin Inhibits the Induction of the Inducible Nitric Oxide Synthase in Rat Cardiac Fibroblasts. Saeid et al., Circulation Research 78 759-768 (1996).
  30. Pre- and Post-translational Regulation of Lysyl Oxidase by Transforming Growth Factor-β1 in Osteoblastic MC3T3-E1 Cells. Feres-Filho et al., Journal of Biological Chemistry 270 30797-30803 (1995).
  31. Effects of transforming growth factor beta-1 on growth-regulatory genes in tumour-derived human oral keratinocytes. Paterson et al., British Journal of Cancer 72 922-927 (1995).

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