Specification
| Organism | Homo sapiens (Human) |
| Expression Host | E.coli |
| Tag Info | N-terminal 6xHis-tagged |
| Purity | Greater than 95% as determined by SDS-PAGE. |
| Uniprot ID | P01375 |
| Uniprot Entry Name | |
| Gene Names | TNF |
| Alternative Names | Tumor Necrosis Factor; Cachectin; TNF-Alpha; Tumor Necrosis Factor Ligand Superfamily Member 2; TNF-a; TNF; TNFA; TNFSF2 |
| Expression Region | Extracellular Domain (57-233aa) |
| Molecular Weight | 21.8 kDa |
| Endotoxin | Less than 1.0 EU/µg as determined by LAL method. |
| Sequence | GPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL |
| Product Form | Lyophilized powder (Lyophilized from a 0.2 μm filtered 20 mM PB, 100 mM NaCl, pH 7.2) |
| Reconstitution | We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference. |
Background
| Relevance | Tumor Necrosis Factor-α (TNF-α) is secreted by macrophages, monocytes, neutrophils, T-cells, and NK-cells following stimulation by bacterial LPS. Cells expressing CD4 secrete TNF-α while cells that express CD8 secrete little or no TNF-α. Synthesis of TNF-α can be induced by many different stimuli including interferons, IL2, and GM-CSF. The clinical use of the potent anti-tumor activity of TNF-α has been limited by the proinflammatory side effects such as fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-α mutants with low systemic toxicity has been of intense pharmacological interest. Human TNF-α that binds to murine TNF-R55 but not murine TNF-R7, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF-α, which binds to both murine TNF receptors. Based on these results, many TNF-α mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro and have exhibited lower systemic toxicity in vivo. Recombinant Human TNF-α High Active Mutant differs from the wild-type by amino acid subsitution of amino acids 1-7 with Arg8, Lys9, Arg10 and Phe157. This mutant form has been shown to have increased activity with less inflammatory side effects in vivo. |
| 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 |
| Involvement in disease | Psoriatic arthritis (PSORAS) |
| Subcellular Location | Cell membrane, Single-pass type II membrane protein, SUBCELLULAR LOCATION: Tumor necrosis factor, membrane form: Membrane, Single-pass type II membrane protein, SUBCELLULAR LOCATION: Tumor necrosis factor, soluble form: Secreted, SUBCELLULAR LOCATION: C-domain 1: Secreted, SUBCELLULAR LOCATION: C-domain 2: Secreted |
| Protein Families | Tumor necrosis factor family |
| Tissue Specificity | |
| Pathway | MAPKsignalingpathway |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |