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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| GRF0386-2 | 7 days | 2 µg | $120.00 |
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| GRF0386-10 | 7 days | 10 µg | $290.00 | |||
| GRF0386-1 | 7 days | 1 mg | $8,320.00 |
Product Overview | |
| Name | TGFB1 (113 a.a.) Human |
|---|---|
| Description | |
| Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant | |
| Accession (Primary) | P01137 |
| Synonyms | |
| Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1. | |
| Introduction | |
| Transforming growth factor betas (TGF Betas) 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. | |
| Source | |
| Human Platelets. | |
| Physical Appearance | |
| Sterile Filtered lyophilized powder. | |
| Formulation | |
| TGF-Beta1 protein was lyophilized from a solution containing 30% acetonitrile and 0.1% trifluoroacetic acid. | |
| Stability | |
| Lyophilized TGF-beta 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-beta 1 should be stored at 4°C between 2-7 days and for future use below -18°C. DO NOT RECONSTITE WITH NEUTRAL BUFFERS. DO NOT USE GLASS IMPLEMENTS OR EXTENSIVE MANIPULATIONS. PREVENT FREEZE THAW CYCLES. | |
| Purity | |
| Greater than 98.0% as determined by SDS-PAGE. | |
| Biological Activity | |
| Stimulates the growth of NRK-1 cells in soft agar at concentrations ranging from 0.1 to 5ng/ml corresponding to a specific activity of 200,000-10,000,000IU/mg. Effective concentration ranges must be experimentally determined. Purified EGF and/or TGF- must be present for observation of the biological activity. | |
| Solubility | |
| It is recommended to reconstitute lyophilized TGF-beta 1 in 0.5% BSA in 0.1N acetic acid, which can then be further diluted to the desired aliquot with 30% acetonitrile and 0.1% trifluoroacetic acid. | |
| Background | |
| Title: Transforming Growth Factor-Beta 1 Human: An Insight into its Role in Cellular Regulation Abstract: Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a critical role in various cellular processes, including cell growth, differentiation, apoptosis, and immune regulation. This research paper aims to provide a comprehensive overview of the structure, synthesis, signaling pathways, and biological functions of TGF-β1 in human cells. Additionally, this article highlights the relevance of TGF-β1 in various physiological and pathological conditions, including cancer, fibrosis, and immune disorders. Furthermore, potential therapeutic strategies targeting TGF-β1 signaling are also discussed. The information presented in this paper consolidates the current understanding of TGF-β1 and its significance in cellular regulation. Introduction: Transforming Growth Factor-Beta 1 (TGF-β1) belongs to a superfamily of growth factors that regulate various cellular processes. It is synthesized as a precursor protein and undergoes proteolytic cleavage to generate the biologically active form. TGF-β1 exerts its effects by binding to specific cell surface receptors, leading to the activation of downstream signaling cascades. These signaling pathways involve Smad-dependent and Smad-independent mechanisms, which ultimately regulate gene expression and cellular responses. Biological Functions: TGF-β1 regulates cell proliferation by exerting both stimulatory and inhibitory effects, depending on the cellular context. It plays a crucial role in tissue development, wound healing, and tissue repair by promoting extracellular matrix synthesis and modulating the immune response. TGF-β1 also has immunomodulatory functions, influencing the differentiation and function of immune cells. However, dysregulation of TGF-β1 signaling is associated with various pathologies, including cancer progression, fibrosis, and autoimmune disorders. Role in Cancer: TGF-β1 acts as a tumor suppressor in early stages of cancer by inhibiting cell proliferation and inducing apoptosis. However, in advanced stages, it promotes tumor progression by enhancing tumor cell migration, invasion, and angiogenesis. The dual role of TGF-β1 in cancer highlights its complex involvement in tumorigenesis. Therapeutic Implications: Given the significant role of TGF-β1 in various diseases, targeting its signaling pathways has emerged as a potential therapeutic strategy. Several approaches, including small molecule inhibitors, antibodies, and gene therapies, are being explored to modulate TGF-β1 activity in a controlled manner. These interventions hold promise in the treatment of cancer, fibrosis, and other TGF-β1-related disorders. Conclusion: Transforming Growth Factor-Beta 1 is a versatile cytokine with diverse functions in cellular regulation. Its role in physiological processes and disease pathogenesis underscores its importance as a therapeutic target. Further investigations into the precise mechanisms and downstream effects of TGF-β1 signaling will contribute to the development of novel therapies for various human disorders. | |
| References | |
| Bibliography: Massagué, J. (2012). TGFβ signalling in context. Nature Reviews Molecular Cell Biology, 13(10), 616-630. Derynck, R., & Budi, E. H. (2019). Specificity, versatility, and control of TGF-β family signaling. Science, 361(6403), eaay5355. Batlle, E., & Massagué, J. (2019). Transforming growth factor-β signaling in immunity and cancer. Immunity, 50(4), 924-940. Pickup, M. W., Mouw, J. K., & Weaver, V. M. (2014). The extracellular matrix modulates the hallmarks of cancer. EMBO Reports, 15(12), 1243-1253. Akhurst, R. J., & Hata, A. (2012). Targeting the TGFβ signalling pathway in disease. Nature Reviews Drug Discovery, 11(10), 790-811. | |
| Precautions | |
| TGFB1 (113 a.a.) Human is for research use only and not for use in diagnostic or therapeutic procedures. | |
Target Information: ( P01137 ) | |
Background |
Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential Abstract: Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance. Introduction: TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications. Production Process and Characteristics: TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses. Therapeutic Applications: TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion. Advantages and Challenges: The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability. Conclusion: TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins. |
References |
Bibliography: Derynck R, Jarrett JA, Chen EY, et al. Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells. Nature. 1985;316(6030):701-705. Massagué J. TGF-beta signal transduction. Annu Rev Biochem. 1998;67:753-791. Blobe GC, Schiemann WP, Lodish HF. Role of transforming growth factor beta in human disease. N Engl J Med. 2000;342(18):1350-1358. Akhurst RJ, Hata A. Targeting the TGFβ signaling pathway in disease. Nat Rev Drug Discov. 2012;11(10):790-811. Prud'homme GJ. Pathobiology of transforming growth factor beta in cancer, fibrosis, and immunologic disease, and therapeutic considerations. Lab Invest. 2007;87(11):1077-1091. |
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