ARG70840
Human TNF alpha recombinant protein (Active) (His-tagged, C-ter)
Human TNF alpha recombinant protein (Active) (His-tagged, C-ter) for SDS-PAGE
Overview
| Product Description | CHO expressed, His-tagged (C-ter) Active Human TNF alpha recombinant protein |
|---|---|
| Tested Application | SDS-PAGE |
| Target Name | TNF alpha |
| Species | Human |
| Expression System | CHO |
| Activity | Active |
| Activity Note | Determinedd by its ability to induce cytotoxicity in L929 cells in the presence of actinomycin D, with the ED50 being less than 0.1 ng/mL. |
| 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 |
Properties
| Form | Powder |
|---|---|
| Purification Note | Endotoxin level is less than 0.1 EU/µg of the protein, as determined by the LAL test. |
| Purity | > 95% (by SDS-PAGE) |
| Buffer | PBS (pH 7.4) |
| Reconstitution | It is recommended to reconstitute the lyophilized protein in sterile water to a concentration not less than 200 μg/mL and incubate the stock solution for at least 20 min at room temperature to make sure the protein is dissolved completely. |
| Storage Instruction | For long term, lyophilized protein should be stored at -20°C or -80°C. After reconstitution, aliquot and store at -20°C or -80°C for up to one month. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. |
| Note | For laboratory research only, not for drug, diagnostic or other use. |
Bioinformation
| Gene Symbol | TNF |
|---|---|
| Gene Full Name | tumor necrosis factor |
| Background | This gene encodes a multifunctional proinflammatory cytokine that belongs to the tumor necrosis factor (TNF) superfamily. This cytokine is mainly secreted by macrophages. It can bind to, and thus functions through its receptors TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. This cytokine is involved in the regulation of a wide spectrum of biological processes including cell proliferation, differentiation, apoptosis, lipid metabolism, and coagulation. This cytokine has been implicated in a variety of diseases, including autoimmune diseases, insulin resistance, and cancer. Knockout studies in mice also suggested the neuroprotective function of this cytokine. [provided by RefSeq, Jul 2008] |
| 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] |
| 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. |
