• Product NameRecombinant Human Tumor Necrosis Factor-a (rHu TNF-a)
• Brief DescriptionRecombinant Protein
• Host SpeciesE.coli
• Purification> 98 % by SDS-PAGE and HPLC analyses.
• Species ReactivityHu
• Biological ActivityFully biologically active when compared to standard. The ED50 as determined by a cytotoxicity assay using murine L929 cells is less than 0.05 ng ml, corresponding to a specific activity of > 2.0 ⅹ 107 IU mg in the presence of actinomycin D.
• EndotoxinLess than 1.0 EU/ng of rHuTNF-a/TNFSF2 as determined by LAL method.
• Target NamerHu TNF-a
• Alternative Names    Tumor Necrosis Factor, TNFSF2, Cachectin, Differentiation-inducing factor , DIF, Necrosin, Cytotoxin
• Accession No. accession:P01375
  GeneID:7124
• UniprotP01375
• Gene ID7124;
• Calculated MW Approximately 17.5 kDa, a sing
• SDS-PAGE MW Sterile Filtered White lyophil
• Target Sequence MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA EAKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL
• Formulation Lyophilized from a 0.2 ng m filtered concentrated solution in 20 mM PB, 10 mM Nacl, pH 7.0.
• Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg mL. Stock solutions should be apportio
• Storage This lyophilized preparation is stable at 2-8 ˚C, but should be kept at -20 ˚C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8 ˚C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20 ˚C to -70 ˚C. Avoid repeated freeze thaw cycles.

Tumor necrosis factor alpha (TNF-α), also called cachectin, is the best-know member of the TNF-family, which can cause cell death. This protein is produced by neutrophils, activated lymphocytes, macrophages, NK cells, LAK cells, astrocytes endothelial cells, smooth muscle cells and some transformed cells. TNF-α occurs as a secreted, soluble form and as a membrane-anchored form, both of which are biologically active. The naturally-occurring form of TNF-α is glycosylated, but non-glycosylated recombinant TNF-α has comparable biological activity. The biologically active native form of TNF-α is reportedly a trimer. Human and murine TNF-α show approximately 79 % homology at the amino acid level and cross-reactivity between the two species. Two types of receptors for TNF-α have been described and virtually all cell types studied show the presence of one or both of these receptor types.

1. Davenport C, Kenny H, Ashley DT, et al. 2012. Eur J Clin Invest, 42: 1173-9. 2. Cavalcanti YV, Brelaz MC, Neves JK, et al. 2012. Pulm Med, 2012: 745483. 3. Sheng WS, Hu S, Ni HT, et al. 2005. J Leukoc Biol, 78: 1233-41. 4. Berthold-Losleben MandHimmerich H. 2008. Curr Neuropharmacol, 6: 193-202.

• Flow Cytometry (FCM) General Protocol
• Immunofluorescence(IC)
• Immunohistochemistry(Polymer)
• Western Blotting