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Cat. #:GMP-103-01
Recombinant Human Tumor Necrosis Factor-alpha/TNFSF2 GMP
rHuTNF-α/TNFSF2 GMP
Technical Parameters
SynonymsTumor Necrosis Factor, TNFSF2, Cachectin, Differentiation-inducing factor , DIF, Necrosin, Cytotoxin
AccessionP01375
GeneID7124
Source Escherichia coli.
Molecular Weight Approximately 17.5 kDa, a single non-glycosylated polypeptide chain containing 158 amino acids.
Quantity 5µg/100µg/1mg
AA Sequence MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA EAKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL
Purity > 98 % by SDS-PAGE and HPLC analyses.
Biological Activity Fully 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 × 107 IU/mg in the presence of actinomycin D.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation Lyophilized from a 0.2 μm filtered concentrated solution in 10 mM PB, 10 mM NaCl, pH 7.0.
Endotoxin Less than 0.01 EU/μg of rHuTNF-α/TNFSF2 GMP as determined by LAL method.
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 apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Usage This GMP product can be for research use or further manufacturing use.
Quality statement The manufacture and testing of this product is in compliance with ICH Q7a guidelines.
Reference1. 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.
BackgroundTumor 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.