Human TNF alpha recombinant protein (Active) (His-tagged, C-ter)
Human TNF alpha recombinant protein (Active) (His-tagged, C-ter) for SDS-PAGE
|产品描述||E. coli expressed, His-tagged (C-ter) Active Human TNF alpha recombinant protein|
|靶点名称||TNF alpha recombinant protein|
|A.A. 序列||MVRSS SRTPS DKPVA HVVAN PQAEG QLQWL NRRAN ALLAN GVELR DNQLV VPSEG LYLIY SQVLF KGQGC PSTHV LLTHT ISRIA VSYQT KVNLL SAIKS PCQRE TPEGA EAKPW YEPIY LGGVF QLEKG DRLSA EINRP DYLDF AESGQ VYFGI IAL with polyhistidine tag at the C-terminus.|
|活性说明||Determined by its ability to induce cytotoxicity in L929 cells in the presence of actinomycin D. The ED50 for this effect is < 0.2 pg/ml.|
|別名||Tumor necrosis factor ligand superfamily member 2; DIF; Cachectin; ICD2; ICD1; N-terminal fragment; TNF-a; TNFA; TNFSF2; TNF-alpha; Tumor necrosis factor; NTF|
|纯化说明||Endotoxin level is less than 0.1 EU/µg of the protein, as determined by the LAL test.|
|纯度||> 98% (by SDS-PAGE)|
|缓冲液||PBS (pH 8.0)|
|复溶||It is recommended to reconstitute the lyophilized protein in sterile water to a concentration not less than 100 µg/ml and incubate the stock solution for at least 20 min at room temperature to make sure the protein is dissolved completely.|
|存放说明||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.|
|注意事项||For laboratory research only, not for drug, diagnostic or other use.|
|全名||tumor necrosis factor|
|背景介绍||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]|
|生物功能||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. Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line.
The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells. [UniProt]
|细胞定位||Cell membrane; Single-pass type II membrane protein. Tumor necrosis factor, membrane form: Membrane; Single-pass type II membrane protein. Tumor necrosis factor, soluble form: Secreted. C-domain 1: Secreted. C-domain 2: Secreted. [UniProt]|
TNF alpha antibodies; TNF alpha ELISA Kits; TNF alpha Duos / Panels; TNF alpha recombinant proteins;
HMGB1 in inflammation
|翻译后修饰||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. [UniProt]
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