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Recombinant human TNF-alpha protein (Qk083)

Tumor necrosis factor-alpha (TNF-α) is a cytokine involved in cell signaling, primarily produced by immune cells like macrophages. It plays a central role in inflammation, immunity, and regulating cell survival and death. TNF-α binds to its receptors, TNF receptor 1 and TNF receptor 2, triggering pro-inflammatory responses, apoptosis, and immune cell activation.

Human TNF-α has a molecular weight of 17.3 kDa. This protein is carrier-free and protein tag-free to ensure its purity with exceptional lot-to-lot consistency. Qk083 TNF-alpha is suitable for the culture of reproducible and high-quality hematopoietic stem cells and other relevant cells.

Orders are typically shipped same or next day (except Friday).
Easy world-wide ordering, direct or through our distributors.

1000µg will be despatched as 2 x 500µg

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  • High purity human protein (Uniprot number: P01375)

  • >98%, by SDS-PAGE quantitative densitometry

  • Source: Expressed in E. coli 

  • 17.3 kDa (Non covalent trimer)

  • Animal-free (AOF) and carrier protein-free

  • Manufactured in Cambridge, UK

  • Lyophilized from Tris/NaCl

  • Resuspend in water at >100 µg/mL, prepare single-use aliquots, add carrier protein if desired, and store frozen at -20oC or -80oC

Featured applications

  • Inflammation regulation

  • Immune response modulation

  • Cell survival regulation

  • Apoptosis regulation

  • Metabolic function regulation

  • Autoimmune disease and inflammatory disorders

Tumor necrosis factor ligand superfamily member 2


Bioactivity graph for Qkine recombinant TNF-α protein

TNF-α activity is determined using the TNF-α-responsive firefly luciferase reporter assay. Transfected HEK293T cells are treated in triplicate with a serial dilution of TNF-α for 3 hours. Firefly luciferase activity is measured and normalised to the control Renilla luciferase activity. Data from Qk083 lot #204609.

EC50 = 1.1 ng/mL (63 pM)


SDS-PAGE gel showing the high purity reduced and non-reduced forms of TNF-α

Recombinant TNF-α migrates as a major band at approximately 17 kDa (monomer) in reduced (R) and non-reduced (NR) conditions. The dimeric and trimeric forms are also observed at approximately 33 and 55 kDa, respectively. No contaminating protein bands are present.The purified recombinant protein (3 µg) was resolved using 15% w/v SDS-PAGE in reduced (+β-mercaptoethanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250. Data from Qk083 lot #204609.

Further quality assays

  • Mass spectrometry, single species with the expected mass

  • Endotoxin: <0.005 EU/μg protein (below the level of detection)

  • Recovery from stock vial: >95%

We are a company founded and run by scientists to provide a service and support innovation in stem cell biology and regenerative medicine.  All our products are exceptionally high purity, with complete characterisation and bioactivity analysis on every lot.

Protein background

Tumor necrosis factor-alpha (TNF-alpha) is a multifunctional cytokine that plays a central role in inflammation, immunity, and various physiological processes [1]. It is primarily produced by activated macrophages and other immune cells, although it can also be synthesized by a variety of other cell types, including endothelial cells, fibroblasts, and adipocytes [2,3].

TNF-alpha exerts its effects by binding to two distinct receptors: TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Both receptors are widely expressed on many cell types throughout the body [4]. TNFR1 activation triggers pro-inflammatory responses, apoptosis, and immune cell recruitment, while TNFR2 signaling is involved in tissue regeneration, immune regulation, and cell survival [5,7].

One of the primary functions of TNF-alpha is its role in the initiation and regulation of inflammation. Upon activation, TNF-alpha stimulates the production of other pro-inflammatory cytokines, such as interleukin-1 (IL-1) and interleukin-6 (IL-6), as well as chemokines that attract immune cells to sites of infection or injury [6]. This pro-inflammatory cascade helps to eliminate pathogens and promote tissue repair. However, dysregulated TNF-alpha signaling can lead to chronic inflammation and tissue damage, contributing to the pathogenesis of various autoimmune diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis.

TNF-alpha plays a crucial role in the regulation of immune responses. It modulates the activation, proliferation, and differentiation of immune cells, including T cells, B cells, and natural killer (NK) cells. TNF-alpha is also involved in the regulation of adaptive immunity by influencing antigen presentation and T cell activation [1-3,8,9].

TNF-alpha has diverse effects on various physiological processes, including metabolism, angiogenesis, and tissue remodeling. It is implicated in the pathogenesis of obesity, insulin resistance, and cardiovascular diseases. TNF-alpha contributes to the host defence against tumors by promoting inflammation and activating immune responses against cancer cells [10]. TNF-alpha has emerged as an important therapeutic target in the treatment of inflammatory and autoimmune diseases. Biologic agents that inhibit TNF-alpha, such as monoclonal antibodies and soluble receptors, have revolutionized the management of conditions like rheumatoid arthritis, Crohn’s disease, and psoriasis, providing relief for patients who do not respond to conventional therapies. However, the blockade of TNF-alpha can also lead to adverse effects, including increased susceptibility to infections and the development of paradoxical inflammatory reactions [11,12].

  1. Abbas, A. K., Lichtman, A. H., & Pillai, S. (2017). Cellular and Molecular Immunology (9th ed.). Elsevier.
  2. Croft, M., & Siegel, R. M. (2017). Beyond TNF: TNF superfamily cytokines as targets for the treatment of rheumatic diseases. Nature Reviews Rheumatology, 13(4), 217-233.
  3. Tracey, D., Klareskog, L., & Sasso, E. H. (2019). Sounding the alarm: A primer on the immunobiology of the alert cytokine, TNF-α. Arthritis Research & Therapy, 21(1), 1-10.
  4. Aggarwal, B. B. (2003). Signalling pathways of the TNF superfamily: a double-edged sword. Nature Reviews Immunology, 3(9), 745-756.
  5. Locksley, R. M., Killeen, N., & Lenardo, M. J. (2001). The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell, 104(4), 487-501.
  6. Balkwill, F., & Mantovani, A. (2001). Inflammation and cancer: back to Virchow? Lancet, 357(9255), 539–545.
  7. Parameswaran, N., & Patial, S. (2010). Tumor necrosis factor-α signaling in macrophages. Critical Reviews in Eukaryotic Gene Expression, 20(2), 87–103.
  8. Tracey, D., Klareskog, L., Sasso, E. H., Salfeld, J. G., & Tak, P. P. (2008). Tumor necrosis factor antagonist mechanisms of action: a comprehensive review. Pharmacology & Therapeutics, 117(2), 244–279.
  9. Aggarwal, B. B. (2003). Signalling pathways of the TNF superfamily: a double-edged sword. Nature Reviews Immunology, 3(9), 745–756.
  10. Choy, E. H. (2002). Clinical significance of tumor necrosis factor α antagonists. Expert Opinion on Drug Safety, 1(3), 229–241.
  11. Popivanova, B. K., et al. (2008). Blocking TNF-α in mice reduces colorectal carcinogenesis associated with chronic colitis. Journal of Clinical Investigation, 118(2), 560–570.
  12. Feldmann, M., & Maini, R. N. (2003). Lasker Clinical Medical Research Award. TNF defined as a therapeutic target for rheumatoid arthritis and other autoimmune diseases. Nature Medicine, 9(9), 1245–1250.

Our products are for research use only and not for diagnostic or therapeutic use.  Products are not for resale.

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