ARG70041

Mouse TNF alpha recombinant protein (Active) (His-tagged, C-ter)

Mouse TNF alpha recombinant protein (Active) (His-tagged, C-ter) for SDS-PAGE

Overview

Product Description E. coli expressed, His-tagged (C-ter) Active Mouse TNF alpha recombinant protein
Tested Application SDS-PAGE
Target Name TNF alpha recombinant protein
Species Mouse
A.A. Sequence MLRSS SQNSS DKPVA HVVAN HQVEE QLEWL SQRAN ALLAN GMDLK DNQLV VPADG LYLVY SQVLF KGQGC PDYVL LTHTV SRFAI SYQEK VNLLS AVKSP CPKDT PEGAE LKPWY EPIYL GGVFQ LEKGD QLSAE VNLPK YLDFA ESGQV YFGVI AL with polyhistidine tag at the C-terminus.
Expression System E. coli
Activity Active
Activity Note Determined by its ability to induce cytotoxicity in L929 cells in the presence of actinomycin D. The ED50 for this effect is < 40 pg/ml. The specific activity of recombinant mouse TNF alpha is approximately > 2.5x 10^7 IU/mg.
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 Ni-NTA chromatography.
Purification Note Endotoxin level is less than 0.1 EU/µg of the protein, as determined by the LAL test.
Purity > 98% (by SDS-PAGE)
Buffer PBS (pH 8.0)
Reconstitution 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 ensure sufficient re-dissolved.
Storage Instruction Lyophilized protein should be stored at -20°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. 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]
Cellular Localization 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]
Highlight Related products:
TNF alpha antibodies; TNF alpha ELISA Kits; TNF alpha Duos / Panels; TNF alpha recombinant proteins;
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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. [UniProt]