TNF-alpha (Tumor necrosis factor alpha), a member of the TNF ligand superfamily, is among others, secreted by macrophages, activated monocytes, neutrophils, T-cells, B-cells and natural killer cells stimulated by bacterial lipopolysaccharides. TNF-alpha shows approximately 30% homology with TNF-beta. TNF-alpha plays an important role in the regulation of immune cells. TNF-alpha has many biological activites, including a cytotoxic effect to various tumor cells, causes inflammation, cellular proliferation and plays a critical role in mediating resistance to bacterial infections. Human and murine TNF-alpha show approximately 79% homolgy and human TNF- alpha is active on murine cells with a slightly reduced specific activity. Recombinant human TNF-alpha produced in plant is a 19.6 kDa protein containing 158 amino acid residues and a 16 a.a. histidine-based tag for a total length of 174 a.a. The recombinant protein migrates as two bands with an apparent molecular mass of 24 kDa in SDS-PAGE. Recombinant human TNF-alpha is produced in the endosperm tissue of barley grain (Hordeum vulgare), that exhibits up to 50 times less protease activity than E.coli or mammalian cells. Barley seed is void of any human or animal viral contaminants that could jeopardize your cell culture.
Human TNF expressed in Endosperm tissue of barley grain (Hordeum vulgare)
CAT# CSC-CTK0343-50 (50 μg); CAT# CSC-CTK0343-250 (250 μg)
Endosperm tissue of barley grain (Hordeum vulgare)
Greater than 95% as determined by SDS-PAGE analysis.
Each batch is tested for bioactivity and verified to have comparable activity to a commercial source. The bioactivity of recombinant human TNF-alpha was determined by its dose-dependent effects in a cytotoxicity assay using Actinomycin-D sensitized L929 cells. The ED50 value for this specific lot of TNF-alpha was found to be 0.3 ng/ml corresponding to specific activity of 3×10^6 units/mg. Optimal concentration should be determined for specific applications and cell lines.
Less than 0.05 EU/μg.
Sterile filtered through a 0.2 μm filter. Lyophilized from PBS (pH 7.2).
Please centrifuge the vial before opening. It is recommended to reconstitute the lyophilized protein in sterile, ultra-pure water to a concentration of no less than 100 μg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein should be used immediately or stored long-term in undiluted working aliquots at -20°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
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