TNF is secreted by macrophages, monocytes, neutrophils, T-cells and NK-cells following their stimulation by bacterial LPS. Cells expressing CD4 secrete TNF-alpha while CD8 cells secrete little or no TNF-alpha. The synthesis of TNF-alpha is induced by many different stimuli including interferons, IL-2 and GM-CSF. Recombinant human Tumor Necrosis Factor-alpha produced in E. coli is a single, non-glycosylated polypeptide chain of 158 amino acids (157 aa of the mature human TNF-alpha and an N-terminal methionine) and a molecular mass of 17,483.77 Dalton.
Human TNF expressed in E.coli
CAT# CSC-CTK0345-10 (10 μg); CAT# CSC-CTK0345-50 (50 μg)
Greater than 98% as determined by SDS-PAGE and HPLC analysis.
Recombinant Tumor Necrosis Factor-alpha is fully biologically active when compared to standards. The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is less than 0.05 ng/ml, corresponding to a specific activity of 2 x 10^7 IU/mg.
Less than 1 EU/μg.
Lyophilized from an sterile-filtered protein solution containing 3 mM Tris (pH 8.0).
Please centrifuge product briefly before opening the vial. The lyophilized rHu TNF- alpha should be reconstituted in sterile, ultra-pure water to a concentration of 0.1 - 1.0 mg/ml. For further dilution, carrier protein (0.1% HSA or BSA) should be added to avoid loss of bioactivity.
Storage & Stability
The lyophilized rHu TNF-alpha, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted rHu TNF-alpha should be used immediately or stored long-term in undiluted working aliquots at -20°C. Avoid repeated freeze / thaw cycles.
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