TGFB1 Human Recombinant

TGFB1 Human Recombinant

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  • TGFB1 Human Recombinant

  • Transforming Growth Factor-Beta 1 Human Recombinant
  • CYT-716
  • Shipped at Room temp.

Catalogue number



Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, LAP, TGFB1.


Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.


TGFB1 Human Recombinant produced in CHO cells is a glycosylated homodimeric polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.6kDa. The TGFB1 is purified by proprietary chromatographic techniques.


CHO cells.

Physical Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.


Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA) And trehalose (1:20 protein to Trehalose ratio).


It is recommended to reconstitute the lyophilized TGFB1 in sterile 10mM HCl at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions. 


Lyophilized TGFB1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB1 Human should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.


Greater than 95.0% as determined by SDS-PAGE.

Amino acid sequence


Biological Activity

The ED50 as determined by the dose-dependent inhibition of IL-4-induced proliferation of HT-2 cells is 0.0149ng/ml, corresponding to a specific activity of 6.7x107units/mg.


1.Title: attenuates skeletal muscle dystrophy in mdx mice .
Publication:Published online before print March 16, 2009, doi: 10.1096/fj.09-129833 August 2009 The FASEB Journal vol. 23 no. 8 2539-2548 .
Link:TGFB1 prospec publication

2.Title:Characterization of Non-Specific Cytotoxic Cell Receptor Protein 1: A New Member of the Lectin-Type Subfamily of F-Box Proteins.
Publication:Kallio H, Tolvanen M, J?nis J, Pan P-w, Laurila E, et al. (2011) Characterization of Non-Specific Cytotoxic Cell Receptor Protein 1: A New Member of the Lectin-Type Subfamily of F-Box Proteins. PLoS ONE 6(11): e27152. doi:10.1371/journal.pone.0027152
Link:TGF-beta-1 prospec publication

3.Title: Cancer-Associated Carbonic Anhydrases IX and XII: Effect of Growth Factors on Gene Expression in Human Cancer Cell Lines.
Publication: Journal of Cancer Molecules 5(3): 73-78, 2010.

Safety Data Sheet


ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.


Title: Transforming Growth Factor-Beta 1 Human Recombinant: A Promising Tool for Biomedical Research



Transforming Growth Factor-Beta 1 (TGF-β1) is a crucial cytokine involved in diverse cellular processes. This research paper provides an in-depth analysis of human recombinant TGF-β1, focusing on its production, purification, and applications in biomedical research. The paper discusses the significance of TGF-β1 in tissue engineering, regenerative medicine, and immunology. Furthermore, it elucidates the potential therapeutic implications of recombinant TGF-β1 in various diseases and highlights ongoing research in the field. The information presented in this paper aims to enhance the understanding of TGF-β1 and its utility as a research tool in biomedical sciences.



Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that regulates cellular processes such as cell growth, differentiation, and immune modulation. Human recombinant TGF-β1 is synthesized using genetic engineering techniques, enabling the production of large quantities of biologically active protein for research purposes.


Production and Purification:

Recombinant TGF-β1 is typically produced in expression systems such as bacteria, yeast, or mammalian cells. The protein is then purified using various chromatographic techniques to obtain a highly pure and active form. Quality control measures ensure the biological activity and integrity of the recombinant protein.


Biomedical Applications:

Human recombinant TGF-β1 has found broad applications in biomedical research. In tissue engineering and regenerative medicine, it plays a critical role in promoting cell proliferation, extracellular matrix production, and tissue repair. TGF-β1 is also involved in immune modulation, influencing immune cell differentiation and function. Recombinant TGF-β1 is a valuable tool for studying these processes and developing therapeutic interventions.


Therapeutic Implications:

The dysregulation of TGF-β1 signaling is associated with various diseases, including fibrosis, cancer, and autoimmune disorders. Recombinant TGF-β1 offers potential therapeutic applications through its ability to modulate cellular responses. Ongoing research aims to develop targeted therapies that specifically regulate TGF-β1 signaling for the treatment of these conditions.



Human recombinant TGF-β1 holds immense potential as a research tool in biomedical sciences. Its production, purification, and applications in tissue engineering, regenerative medicine, and immunology contribute to advancing our understanding of cellular processes and disease mechanisms. With ongoing research, recombinant TGF-β1 may pave the way for novel therapeutic strategies in various medical fields.




  1. de Caestecker, M., Piek, E., & Roberts, A. B. (2021). Role of transforming growth factor-betas in human disease. Handbook of Experimental Pharmacology, 267, 1-51.
  2. Akhurst, R. J., & Hata, A. (2012). Targeting the TGFβ signalling pathway in disease. Nature Reviews Drug Discovery, 11(10), 790-811.
  3. Chen, G., Deng, C., & Li, Y. P. (2019). TGF-β and BMP signaling in osteoblast differentiation and bone formation. International Journal of Biological Sciences, 15(11), 2132-2142.
  4. Varelas, X. (2014). The Hippo pathway effectors TAZ and YAP in development, homeostasis and disease. Development, 141(8), 1614-1626.
  5. Chen, C. C., & Lau, L. F. (2009). Functions and mechanisms of action of CCN matricellular proteins. International Journal of Biochemistry and Cell Biology, 41(4), 771-783.
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