Alternative names:
TNFSF2

Data and images for Human TNF-α

Figures

Figure 1

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Human TNF-α activity assay.
The biological activity of Human TNF-α, premium grade was determined by inhibition assay using L-929 cells.

Figure 1

Human TNF-α activity assay.
The biological activity of Human TNF-α, premium grade was determined by inhibition assay using L-929 cells.

Figure 2

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SDS-PAGE of Human TNF-alpha, premium grade under reduced (R) and non reduced (NR) conditions.

Figure 2

SDS-PAGE of Human TNF-alpha, premium grade under reduced (R) and non reduced (NR) conditions.

Figure 3

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Mass spectrometry analysis (ESI-MS) of Human TNF-α, premium grade. The peak corresponds to the calculated molecular mass of 17353 Da.

Figure 3

Mass spectrometry analysis (ESI-MS) of Human TNF-α, premium grade. The peak corresponds to the calculated molecular mass of 17353 Da.

Specifications for Human TNF-α

Overview

TNF-α stands for tumor necrosis factor α, also termed TNFSF2 (TNF ligand superfamily member 2). Human TNF-α is a recombinant protein optimized for use in cell culture, differentiation studies, and functional assays.

Applications

TNF-α can be used for a variety of applications, including:
  • Induction of Mo-DC maturation.
  • Cytotoxicity and cell proliferation assays.
  • Assessment of apoptosis and viral protection.
  • Investigation of TNF-α–induced signaling pathways.

Alternative names

TNFSF2

Detailed product information

Background information

Tumor necrosis factor α (TNF-α) is a proinflammatory cytokine mainly produced by activated monocytes and macrophages in response to infection, injury, and tumor burden. TNF-α production has also been reported for a variety of other cell types involved in inflammatory responses, including T cells, NK cells, and neutrophils as well as a number of non-immune cells, such as keratinocytes and astrocytes. TNF-α has a broad spectrum of biological activities. In addition to its central role in inflammation, TNF-α is noted for its cytotoxic and tumoricidal abilities either by necrosis or induction of apoptosis. Further functions include antiviral activity, growth modulation, and induction of cellular differentiation. Despite its various beneficial actions, TNF-α also plays a detrimental role in, for example, septic shock syndrome, tissue injury, inflammation, cachexia, and diabetes.

Biological activity

  • Inhibition of L-929 cells (NIBSC 88/786)
  • research grade: ≥ 2×
    10
    7
    IU/mg
  • premium grade: ≥ 4×
    10
    7
    IU/mg
    (Typical specific activity: ≥ 6×
    10
    7
    IU/mg
    )
  • We measure the biological activity of each batch of MACS Premium-Grade Cytokines and state the results in the Certificate of Analysis (CoA). Based on the lot-specific activity, exact doses of active cytokine can be applied to cell culture experiments. This allows for reproducible cell culture conditions without the need for time-consuming lot-to-lot testing.

Quality description

Research-grade
cytokines are suitable for a wide variety of cell culture applications. They are sterile-filtered prior to lyophilization. Generally, endotoxin levels are <0.1 ng/μg (<1 EU/μg), and purities are >95%. The biological activity is tested in appropriate bioassays.
Premium-grade
cytokines offer the convenience of high and well-defined biological activities and allow exact unit dosing for demanding applications. The biological activity is determined after lyophilization and reconstitution, and normalized to WHO/NIBSC standards whenever available. In general, endotoxin levels are <0.01 ng/μg (<0.1 EU/μg), and purities are >97%. Lot-specific activities are stated in the Certificate of Analysis (www. miltenyibiotec.com/certificates).

Resources for Human TNF-α

Documents and Protocols

Certificates

Please follow this
link
to search for Certificates of Analysis (CoA) by lot number.

References for Human TNF-α

Publications

  1. Zhou, R. et al. (2020) Acute SARS-CoV-2 Infection Impairs Dendritic Cell and T Cell Responses Immunity 53(4): 864-877
  2. Kronenberg, D. et al. (2012) Circulating preproinsulin signal peptide-specific CD8 T cells restricted by the susceptibility molecule HLA-A24 are expanded at onset of type 1 diabetes and kill β-cells Diabetes 61(7): 1752-1759
  3. Garufi, A. et al. (2012) Targeting COX-2/PGE(2) pathway in HIPK2 knockdown cancer cells: impact on dendritic cell maturation PLoS One 7(11): e48342
  4. Mayordomo, A. C. et al. (2018) IL-12/23p40 overproduction by dendritic cells leads to an increased Th1 and Th17 polarization in a model of Yersinia enterocolitica-induced reactive arthritis in TNFRp55-/- mice PLoS One 13(3): e0193573
  5. Voskamp, A. et al. (2013) MHC class II expression in human basophils: induction and lack of functional significance PLoS One 8(12): e81777
  6. Clement, M. et al. (2016) Targeted suppression of autoreactive CD8 + T-cell activation using blocking anti-CD8 antibodies Sci Rep 6: 35332
  7. Meurer, T. et al. (2018) Dissecting Genetic Control of HLA-DPB1 Expression and Its Relation to Structural Mismatch Models in Hematopoietic Stem Cell Transplantation Front Immunol 9: 2236
  8. Paravati, R. et al. (2020) Differential regulation of osteopontin and CD44 correlates with infertility status in PCOS patients J. Mol. Med. 98(12): 1713-1725
  9. Boink, M. A. et al. (2017) Saliva-Derived Host Defense Peptides Histatin1 and LL-37 Increase Secretion of Antimicrobial Skin and Oral Mucosa Chemokine CCL20 in an IL-1 α-Independent Manner J Immunol Res 2017: 3078194
  10. Cantoni, C. et al. (2021) Stromal-like Wilms tumor cells induce human Natural Killer cell degranulation and display immunomodulatory properties towards NK cells Oncoimmunology 10(1): 1879530
  11. Nicoli, F. et al. (2021) Use of a Novel Peptide Welding Technology Platform for the Development of B- and T-Cell Epitope-Based Vaccines Vaccines (Basel) 9(5): 526
  12. Ferroni, L. et al. (2020) Fluorescent Light Energy (FLE) Acts on Mitochondrial Physiology Improving Wound Healing J Clin Med 9(2): 559
  13. Baarsch, M. J. et al. (1991) Detection of tumor necrosis factor alpha from porcine alveolar macrophages using an L929 fibroblast bioassay. J. Immunol. Methods 140: 15-22
  14. Barbara, J. A. et al. (1996) Tumour necrosis factor-alpha (TNF-alpha): the good, the bad and potentially very effective. Immunol. Cell Biol. 74: 434-443
  15. Yeung, M. C. et al. (1996) An essential role for the interferon-inducible, double-stranded RNA-activated protein kinase PKR in the tumor necrosis factor-induced apoptosis in U937 cells. Proc. Natl. Acad. Sci. U.S.A. 93: 12451-12455
  16. Black, R. A. et al. (1997) A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385: 729-733
  17. Simo, R. et al. (2012) Potential role of tumor necrosis factor-α in downregulating sex hormone-binding globulin. Diabetes 61(2): 372-382
  18. Schipper, H. S. et al. (2010) A multiplex immunoassay for human adipokine profiling. Clin. Chem. 56(8): 1320-1328
  19. Schweikert, E. M. et al. (2012) PON3 is upregulated in cancer tissues and protects against mitochondrial superoxide-mediated cell death. Cell Death Differ. 19(9): 1549-1560
  20. Islam, S. A. et al. (2013) Identification of human CCR8 as a CCL18 receptor. J. Exp. Med. 210(10): 1889-1898
  21. Bacher, P. et al. (2014) Antigen-specific expansion of human regulatory T cells as a major tolerance mechanism against mucosal fungi. Mucosal Immunol 7(4): 916-928

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