Species |
Mouse |
Protein Construction |
TNF-α (Ser84-Leu235) Accession # P06804 |
|
Purity |
> 95% as analyzed by SDS-PAGE |
Endotoxin Level |
< 1 EU/μg of protein by gel clotting method |
Biological Activity |
ED50 < 0.01 ng/ml, measured by cytotoxicity assay using L929 cells, corresponding to a specific activity of > 1.0 × 108 units/mg. |
Expression System |
P. pastoris |
Apparent Molecular Weight |
~17 kDa, on SDS-PAGE under reducing conditions. |
Formulation |
Lyophilized after extensive dialysis against PBS. |
Reconstitution |
It is recommended that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute the lyophilized powder in ddH₂O or PBS up to 100 μg/ml. |
Storage & Stability |
Upon receiving, this product remains stable for up to 6 months at lower than -70°C. Upon reconstitution, the product should be stable for up to 1 week at 4°C or up to 3 months at -20°C. For long term storage it is recommended that a carrier protein (example 0.1% BSA) be added. Avoid repeated freeze-thaw cycles. |
Target Background |
Tumor necrosis factor alpha (TNF-α) is produced by neutrophils, activated lymphocytes, macrophages, NK cells, LAK cells, astrocytes endothelial cells, smooth muscle cells and some transformed cells. Mouse TNF-α occurs as a membrane-anchored form. 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 mouse TNF-α show approximately 79% homology at the amino acid level and crossreactivity between the two species. |
Synonyms |
TNF-alpha; Tumor necrosis factor ligand superfamily member 2; TNF-a; Cachectin; DIF; TNFA; TNFSF2 |
For laboratory research use only. Direct human use, including taking orally and injection and clinical use are forbidden.