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
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.
Quality description
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 certificates of analysis are available on request (macstec@miltenyibiotec.de).
SDS-PAGE of Human TNF-alpha, premium grade under reduced (R) and non reduced (NR) conditions.
SDS-PAGE of Human TNF-alpha, premium grade under reduced (R) and non reduced (NR) conditions.
Selected references
Black, R. A. et al. (1997) A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385: 729-733
Islam, S. A. et al. (2013) Identification of human CCR8 as a CCL18 receptor. J. Exp. Med. 210(10): 1889-1898
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
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
Simo, R. et al. (2012) Potential role of tumor necrosis factor-α in downregulating sex hormone-binding globulin. Diabetes 61(2): 372-382
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
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
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
Schipper H. S. et al. (2010) A multiplex immunoassay for human adipokine profiling. Clin. Chem. 56(8): 1320-1328
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