TNF-α (His-FLAG-Myc-Tag)

Tumor necrosis factor (TNF, cachexin, or cachectin, and formerly known as tumor necrosis factor alpha or TNF-α) is the prototype of the TNF superfamily and is involved in systemic inflammation.

Interacting protein(s): TNFR1 (P7020F), TNFR2 (P7022F)
Related products: Hexa-Ligand

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Description

Tumor necrosis factor (TNF, cachexin, or cachectin, and formerly known as tumor necrosis factor alpha or TNF-α) is the prototype of the TNF superfamily and is involved in systemic inflammation. TNF is produced a type II protein membrane protein folded in stable homotrimers which can be proteolyzed by TNF-α converting enzyme (TACE) and released as soluble protein. Interestingly, at a concentration of less than nM, the non-covalent linked soluble trimeric TNF tend to dissociate into monomers which is biologically inactive.

TNF can bind two receptors, TNFR1 and TNFR2. TNFR1 is expressed in most tissues, and can be fully activated by both the membrane-bound and soluble trimeric forms of TNF, whereas TNFR2 is found only in cells of the immune system, and respond to the membrane-bound form of the TNF homotrimer. TNF is produced primarily by activated macrophages, although it can be produced by many other cell types such as CD4+ lymphocytes, NK cells, neutrophils, mast cells, eosinophils, and neurons. TNF promotes the inflammatory responses that often lead to autoimmune disorders such as rheumatoid arthritis, inflammatory bowel disease, psoriasis, and asthma.

TNF blockers have been developed to treatment these diseases including, Adalimumab (Humira) and infliximab (Remicade) and certolizumab (Cimzia), all are monoclonal antibodies capable of inhibiting TNF binding to its receptor, as well as Etanercept (Enbrel) which is a decoy protein consisting of the TNFR2 extracellular domain fused an Ig Fc region.

Amino Acid Sequence

References

1. Huyghe J, Priem D, Bertrand MJM. Cell death checkpoints in the TNF pathway. Trends Immunol. 2023;44(8):628-43. Epub 20230623. doi: 10.1016/j.it.2023.05.007. PubMed PMID: 37357102.

2. Plantone D, Pardini M, Righi D, Manco C, Colombo BM, De Stefano N. The Role of TNF-α in Alzheimer's Disease: A Narrative Review. Cells. 2023;13(1). Epub 20231226. doi: 10.3390/cells13010054. PubMed PMID: 38201258; PubMed Central PMCID: PMC10778385.

3. Kriegler M, Perez C, DeFay K, Albert I, Lu SD (1988). A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF. Cell 53: 45–53.

4. Chen G, Goeddel DV, Goeddel (2002). TNF-R1 signaling: a beautiful pathway. Science 296: 1634–1635
3. Scott LJ. (2014) Etanercept: a review of its use in autoimmune inflammatory diseases. Drugs.74:1379-1410.

5. Lapadula G, Marchesoni A, Armuzzi A, Blandizzi C, Caporali R, et al. (2014) Adalimumab in the treatment of immune-mediated diseases. Int J Immunopathol Pharmacol. 27(1 Suppl):33-48