anti-TNF alpha antibody [B1E4] (HRP)
anti-TNF alpha antibody [B1E4] (HRP) for ELISA and Human
Cancer antibody; Cell Biology and Cellular Response antibody; Immune System antibody; Metabolism antibody; Signaling Transduction antibody
HRP-conjugated Mouse Monoclonal antibody [B1E4] recognizes Human TNF-alpha
|Target Name||TNF alpha|
|Immunogen||Purified recombinant human TNF-α|
|Full Name||tumor necrosis factor|
|Alternate Names||Tumor necrosis factor ligand superfamily member 2; DIF; Cachectin; ICD2; ICD1; N-terminal fragment; TNF-a; TNFA; TNFSF2; TNF-alpha; Tumor necrosis factor; NTF|
|Application Note||ELISA: This HRP-conjugated monoclonal antibody can be used as a tracer/detection antibody in sandwich ELISA applications for human TNF-alpha detection in combination with capture antibody CH8820 (Cat. No.: ARG10001).
* The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.
|Purification||Protein G affinity purified|
|Buffer||0.01M PBS (pH 7.2) and 50% Glycerol|
|Storage instruction||For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Keep the antibody in the dark and keep protected from prolonged exposure to light. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.|
|Note||For laboratory research only, not for drug, diagnostic or other use.|
|Background||Tumor Necrosis Factor alpha (TNF-α) is a multifunctional pro-inflammatory cytokine, mainly secreted by activated macrophages. TNF-α was named for its remarkable ability to cause hemorrhagic necrosis of tumors in mice. It is implicated with a variety of biological procedures including systemic inflammation, cell proliferation, apoptosis, lipid metabolism, and coagulation. The pleiotropic attribute of TNF-α regulation is associated with its ability to trigger multiple signalling pathways simultaneously. It is well documented that TNF-α functions through its receptors, TNFR1 (p55) and TNFR2 (p75). TNF-α not only contributes to the immune response to bacterial, fungal, viral and parasitic invasions, but also functions in tissue remodeling, autoimmune-diseases and the necrosis of specific tumors. TNF-α hyper-expression in response to some bacterial components such as LPS can cause life threatening septic shock. Recombinant TNF-α, in combination with chemotherapy, has been applied for treatment of soft sarcomas, melanomas and other irresectable tumors. Anti-TNF-α therapy has been used for treatment of rheumatoid arthritis.|
|Function||Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is 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. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Upregulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208).
The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells. [UniProt]
|Resrarch Area||Cancer antibody; Cell Biology and Cellular Response antibody; Immune System antibody; Metabolism antibody; Signaling Transduction antibody|
|PTM||The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secreted into the extracellular space.
The membrane form, but not the soluble form, is phosphorylated on serine residues. Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1.
O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid.