The mouse TNF-a ELISA is an enzyme-linked immunosorbent assay for the quantitative detection of mouse TNF-a. The mouse TNF-a ELISA is for research use only. Not for diagnostic or therapeutic procedures.
TNF-α is a multifunctional cytokine involved in many different pathways, in homeostasis and pathophysiology of mammals. It can show opposing biological effects suggesting complex regulatory mechanisms.
TNF-α, also known as cachectin, was first detected as a cytotoxic factor inducing lysis of certain tumor cells. The TNF-α gene is member 2 of the TNF-superfamily (consisting of at least 20 distinct members).
TNF-α release is mainly triggered by viral infections and endotoxins, lipopolysaccharides or other bacterial components, by tissue injury, DNA-damage and by IL-1, PDFG and TNF-α itself. It is primarily expressed in macrophages, but also in monocytes, neutrophils, NK-cells, mast-cells, endothelial cells and activated lymphocytes. TNF-α expression in endothelial cells and fibroblasts can be induced by IL-17.
The expression of other cytokines, chemokines, reactive oxygen intermediates, nitric oxide and prostaglandins is stimulated by TNF-α.
The initially membrane bound TNF-α is enzymatically cleaved by TACE (= ADAM17). The soluble monomers aggregate to homotrimers and are secreted into blood and other biological fluids. The membrane bound and the soluble form are biologically active and bind to the TNFreceptors TNFR1 ( = TNFRSF1A, p55-60) and TNFR2 ( = TNFRSF1B, TNFBR2, p75-80). Upon ligand binding, receptors form trimers leading to conformational changes, protein dissociation (SODD = silencer of death domains, BAG4, Bcl2-associated athanogene 4) and association (TRADD = TNF-R1 associated death domain protein) and yielding the following biological activities:
- transcription of anti-apoptotic factors and proteins involved in cell proliferation and inflammation via binding of TRAF2 (TNF-R associated factor 2) and RIPK1 (TNF-R interacting serine-threonine kinase 1) and activation of the transcription factor NF-κB.
- cell proliferation, differentiation but also apoptotisis via TRAF2 binding, kinases activation, activation of c-Jun and ATF2 (JNK-MAPK-pathway).
- apoptosis via the binding of FADD (Fas associating protein with death domain) to TRADD and activation of caspases (including caspase 8 = FLICE).
- necrosis, a caspase independent cell death, mediated by NADPH oxidases, which form a complex with TRADD and RIPK1, leading to the generation of oxygen species.
TNF-R2 contains no DD (death domain), but exhibits its function via direct TRAF binding.
Thus the multiple biological functions of TNF-α comprise cellular proliferation and differentiation, tumorigenesis, apoptotic or necrotic cell death (including certain tumor cell lines), immunoregulatory activities, lipid metabolism, coagulation and endothelial function. It promotes local or systemic inflammation (TNF-α is a potent pyrogen) and stimulates the acute phase response. Very high expressions of TNF-α after infection can lead to septic shock (TNF-α is highly cytotoxic.), whereas sustained low levels induce cachexia and inflammation.
Dysregulation of TNF-α is involved in many diseases.
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