rHu TGF-β1 PLUS™ Protein

Product Summary

• High purity optimized TGF-β1 protein (Uniprot: P01137)
• 24 kDa (dimer)
• >98%, by SDS-PAGE quantitative densitometry
• Expressed in E. coli
• Animal origin-free (AOF) and carrier protein-free
• Manufactured in Cambridge, UK at Qkine laboratories
• Lyophilized from acetonitrile, TFA

Alternative Names

• Transforming growth factor-beta 1, TGF-beta 1, TGFβ1, TGFB1, TGF B1, tgf-b1, Qk10

Reconstitution

Resuspend in 10 mM HCl (Reconstitution solution A) at >50 µg/ml, add carrier protein if desired, prepare single-use aliquots and store frozen at -20 °C (short-term) or -80 °C (long-term)

For Use Statement

For research use only. This product is not for human use or for direct clinical use as a drug, therapeutic, biologic or medical device.

Certificate of Analysis (CoA)
Certificate of Origin (CoO)
Safety Data Sheet (SDS)
Product Page

Transforming growth factor-beta 1 (TGF-β1) is a pleiotropic cytokine part of the TGF-β superfamily. TGF-β1 regulates various cellular processes, including cell proliferation, growth, differentiation, motility, and apoptosis [1]. It plays a crucial role in the immune response, tissue repair, and the epithelial-mesenchymal transition. Transforming growth factor-beta 1 is produced by various cell types, including immune cells, fibroblasts, and epithelial cells. It is synthesized and secreted as an inactive or latent complex, associated with latency-associated proteins (LAP), and targeted to the extracellular matrix [2]. It is released from latency by TGF-β activators including plasmin, matrix metalloproteases, integrins. Once the LAP cleaved, the mature transforming growth factor-beta 1 is a homodimeric protein composed of two identical subunits linked by a disulfide bond. Its amino acid sequence is composed of 390 amino acids. TGF-β1 signals through complexes of cell surface receptors including TGF-βRII/TGF-βRI and ALK-5/ALK-1. This triggers downstream signaling cascades, such as the Smad-dependent and Smad-independent pathways.

In cell culture, recombinant TGF-β1 protein is an essential growth factor in many embryonic and induced pluripotent stem cell maintenance media, including the commonly used chemically-defined E8, StemPro, and mTeSR medias [3–5]. Transforming growth factor-beta 1 supports the survival and maintenance of pluripotency of stem cells [1]. TGF-β1 is used to promote the differentiation of various cell types such as fibroblasts, epithelial cells, and immune cells. It is used in combination with other growth factors such as BMP-2 to regulate bone marrow stromal cell differentiation or with IL-2 and IL-6 to regulate T reg and Th17 cells differentiation [6–8].

To date, recombinant human TGF-β1 has only been produced from mammalian cell protein expression systems (HEK or CHO), where endogenous protein contaminants, cost and animal-free status is a challenge. As part of the ongoing mission to redefine industry standards for growth factor and cytokine biochemical quality, Qkine introduced the first optimized, animal-free, and highly bioactive recombinant human TGF-β1.

[1] D. James, A. J. Levine, D. Besser, and A. Hemmati-Brivanlou, ‘TGFβ/activin/nodal signaling is necessary for the maintenance of pluripotency in human embryonic stem cells’, Development, vol. 132, no. 6, pp. 1273–1282, Mar. 2005, doi: 10.1242/dev.01706.

[2] J. P. Annes, J. S. Munger, and D. B. Rifkin, ‘Making sense of latent TGFβ activation’, J. Cell Sci., vol. 116, no. 2, pp. 217–224, Jan. 2003, doi: 10.1242/jcs.00229.

[3] J. Beers et al., ‘Passaging and colony expansion of human pluripotent stem cells by enzyme-free dissociation in chemically defined culture conditions’, Nat. Protoc., vol. 7, no. 11, pp. 2029–2040, 2012, doi: 10.1038/nprot.2012.130.

[4] T. E. Ludwig, V. Bergendahl, M. E. Levenstein, J. Yu, M. D. Probasco, and J. A. Thomson, ‘Feeder-independent culture of human embryonic stem cells’, Nat. Methods, vol. 3, no. 8, Art. no. 8, Aug. 2006, doi: 10.1038/nmeth902.

[5] A. Wang et al., ‘Induced Pluripotent Stem Cells for Neural Tissue Engineering’, Biomaterials, vol. 32, no. 22, pp. 5023–5032, Aug. 2011, doi: 10.1016/j.biomaterials.2011.03.070.

[6] Y. Tang et al., ‘TGF-β1–induced migration of bone mesenchymal stem cells couples bone resorption with formation’, Nat. Med., vol. 15, no. 7, Art. no. 7, Jul. 2009, doi: 10.1038/nm.1979.

[7] M. Elsafadi et al., ‘Convergence of TGFβ and BMP signaling in regulating human bone marrow stromal cell differentiation’, Sci. Rep., vol. 9, no. 1, Art. no. 1, Mar. 2019, doi: 10.1038/s41598-019-41543-0.

[8] M. Veldhoen, R. J. Hocking, C. J. Atkins, R. M. Locksley, and B. Stockinger, ‘TGFβ in the Context of an Inflammatory Cytokine Milieu Supports De Novo Differentiation of IL-17-Producing T Cells’, Immunity, vol. 24, no. 2, pp. 179–189, Feb. 2006, doi: 10.1016/j.immuni.2006.01.001.