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Recombinant human TNF-alpha protein

Soluble form of Tumor Necrosis Factor α, Cachectin

Human Tumor Necrosis Factor α, Recombinant, E.coli

Cat #: T-100
Alternative Name Soluble form of Tumor Necrosis Factor α, Cachectin
Lyophilized Powder yes
  • Bioassay Tested
  • Sterile & Endotoxin Free yes
    Origin Recombinant, E. coli
    MW: 17.4 kDa
    Endotoxin Level <0.1 EU per 1 µg of the protein by the LAL method.
    Purity: >98% (HPLC)
    Form Lyophilized from a 0.2 µm filtered solution.
    Effective concentration EC50 = 1.4 pM.
    Modifications Disulfide bonds between Cys145- Cys177.
    CAS No.: 94948-59-1
    Activity TNF-α plays a role in antitumor activity, inflammation, immune modulation, viral replication, septic shock, anorexia, cachexia, and hematopoiesis1.
    1. Ware, C. et al. (1998) Thomson, A.W. ed. The Cytokine Handbook 3rd ed., San Diego, CA, 549.
    Shipping and storage Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.
    Solubility Any aqueous buffer. Centrifuge all product preparations before use (10000 x g 5 min).
    Storage of solutions Up to one week at 4°C or three months at -20°C.
    Our bioassay
    • Alomone Labs Recombinant human TNF-alpha protein induces cytolysis in HeLa cells.
      Alomone Labs Recombinant human TNF-alpha protein induces cytolysis in HeLa cells.
      Cells were incubated with increasing Recombinant human TNF-alpha protein (#T-100) concentrations in the presence of 1µg/ml actinomycin D. Cell death was determined after 24 h by the XTT methods and plotted against Recombinant human TNF-alpha protein concentrations (ED50 = 12.5 pg/ml).
    References - Scientific background
    1. Pennica, D. et al. (1984) Nature 312, 724.
    2. Aggarwal, B.B. et al. (1985) J. Biol. Chem. 260, 2345.
    3. Carswell, E.A. et al. (1975) Proc. Natl. Acad. Sci. U.S.A. 72, 3666.
    4. Janeway, C. et al. (1999) Immunobiology, 5th edition. New York, N.Y: Garland Publishers.
    5. Murray, J. et al. (1997) Blood 90, 2772.
    6. Strieter, R. et al. (1993) Critical Care Medicine 21, S447.
    7. Madhusudan, S. et al. (2004) Clin. Cancer Res. 10, 6528.
    8. Madhusudan, S. et al. (2005) J. Clin. Oncol. 23, 5950.
    9. Harrison, M.L. et al. (2007) J. Clin. Oncol. 25, 4542.
    10. Brown, E.R. et al. (2008) Ann. Oncol. 19, 1340.
    Scientific background

    TNF-α is a cytokine that binds to TNFR-55 and TNFR-75 receptors which are expressed on all somatic cells. It is derived from several types of cells but especially by activated monocytes1-2 and can induce cell death of certain tumor cell lines3. It is a potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia. Under certain conditions it can stimulate cell proliferation and induce cell differentiation.

    The secretion of the acute phase protein TNF-α initiates a cascade of cytokines and increases vascular permeability, thereby recruiting macrophages and neutrophils to a site of bacterial, fungal, viral or parasitic infection. Without TNF-α, mice infected with gram negative bacteria experience septic shock4.

    The cytokine possesses both growth stimulating properties and growth inhibitory processes, and it appears to have self-regulatory properties as well. For instance, TNF-α induces neutrophil proliferation during inflammation, but it also induces neutrophil apoptosis upon binding to the TNF-R55 receptor5.

    TNF-α participates in both inflammatory disorders of inflammatory and non-inflammatory origin6. Originally, sepsis was believed to result directly from the invading bacteria itself, but it was later recognized that host system proteins, such as TNF-α induced sepsis in response.

    TNF-α seems to serve as a mediator in various pathologies. A few such examples include: septic shock, cancer, AIDS, transplantation rejection, multiple sclerosis, diabetes, rheumatoid arthritis, trauma, malaria, meningitis, ischemia-reperfusion injury, adult respiratory distress syndrome, ankylosing spondylitis, inflammatory bowel disease, psoriasis, hidradenitis suppurativa and refractory asthma. Since TNF-α plays a role in several diseases, a substantial amount of research has been conducted concerning TNF-α and anti-TNF-α therapies. TNF-α inhibition can be achieved with a monoclonal antibody or with a circulating receptor fusion protein. Clinical experience so far concludes that it is safe to give TNF antagonists to cancer patients since TNF antagonist treatment results in a period of disease stabilization or better in 20% of patients with advanced cancer7-10.

    Peptide Content: 100%
    Last update: 06/11/2022

    Recombinant human TNF-alpha protein (#T-100) is a highly pure, recombinant, and biologically active protein.

    For research purposes only, not for human use



    Scientific Background

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