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Amino Acid Sequence: VRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
Background: Tumor Necrosis Factor is secreted by macrophages, monocytes, neutrophils, T-cells, and NK- cells following their stimulation by bacterial lipopolysaccharides. Cells expressing CD4 secrete TNF-alpha while CD8(+) cells secrete little or no TNF-alpha. Stimulated peripheral neutrophilic granulocytes but also unstimulated cells and also a number of transformed cell lines, astrocytes, microglial cells, smooth muscle cells, and fibroblasts also secrete TNF. Human milk also contains this factor. The synthesis of TNF-alpha is induced by many different stimuli including interferons, IL-2, GM-CSF, SP, Bradykinin, Immune complexes, inhibitors of cyclooxygenase and PAF (platelet activating factor). Human TNF-alpha is a non-glycosylated protein of 17 kDa and a length of 157 amino acids. Murine TNF-alpha is N-glycosylated. Homology with TNF-beta is approximately 30%. TNF-alpha forms dimers and trimers.
Biological Activity: The ED50 was determined cytolysis of murine L929 cells in the presence of Actinomycin D is ≤ 0.05 ng/ml, corresponding to a specific activity of > 1.9 x 10^7 units/mg.
Description: Recombinant TNF-alpha is a disulfide-linked monomer protein, consisting of 158 amino acids and migrates as an approximately 17 kDa protein under reducing conditions. Optimized DNA sequence encoding Human Tumor Necrosis Factor-alpha chain was expressed in E. coli.
Endotoxin Level: <0.1 ng/µg (1 EU/µg), using the LAL gel clot method.
Format: lyophilized protein
Formulation: Lyophilized from a 0.2 µm filtered concentrated (1 mg/ml) solution in PBS, pH 7.2.
Genbank: P01375
Purity: ≥95% by SDS-PAGE and HPLC
Reconstitution: Reconstitute at 0.1-1.0 mg/ml in distilled water. This solution can then be diluted into other buffers. To maximize product collection from vial surface, vortex briefly and then spin down to recollect the liquid.
Storage Stability: The lyophilized protein is stable for at least 2 years from date of receipt when stored at -20°C. Upon reconstitution, store in working aliquots at +4°C for up to one month, or at -20°C for up to six months, in the presence of a carrier protein. Avoid repeated freeze/thaw cycles.
Uniprot: P01375
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: 1. Vermel' AE. Klin Med (Mosk). 2005,83(11):13-7.
2. Tracey KJ, Cerami A. Annu Rev Med. 1994,45:491-503
3. Sedgwick JD, et al. Immunol Today. 2000 Mar,21(3):110-3.
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