| Source: |
Escherichia coli. |
| Molecular Weight: |
Approximately 16.9 kDa, a single non-glycosylated polypeptide chain containing 151 amino acids. Compared with the wild-type, rHuTNF-α Variant has an amino acid sequence (a.a.) deletion from a.a. 1-7, and the following a.a. substitutes Arg8, Lys9, Arg10 and Phe157 which is proven to have more activity and with less inflammatory side effect in vivo. |
| AA Sequence: |
MRKRKPVAHV VANPQAEGQL QWLNRRANAL LANGVELRDN QLVVPSEGLY LIYSQVLFKG QGCPSTHVLL THTISRIAVS YQTKVNLLSA IKSPCQRETP EGAEAKPWYE PIYLGGVFQL EKGDRLSAEI NRPDYLDFAE SGQVYFGIIA F |
| 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 0.01 ng/mL, corresponding to a specific activity of > 1.0 × 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 PBS, pH7.0. |
| Endotoxin: |
Less than 1 EU/μg of rHu TNF-α/TNFSF2, Variant as determined by LAL method. |
| Reconstitution: |
Centrifuge the vial briefly before opening to ensure that the contents settle at the bottom. Reconstitute the vial with sterile distilled water or an aqueous buffer containing 0.1% BSA to achieve a concentration of 0.1-1.0 mg/mL. Divide the resulting stock solution into working aliquots and store them at or below -20°C. For further dilutions, use 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. |
| Synonyms: |
Tumor Necrosis Factor, TNFSF2, Cachectin, Differentiation-inducing factor (DIF), Necrosin, Cytotoxin |
| Background: |
The therapeutic application of TNF-α's powerful anticancer properties is hindered by its inflammatory adverse effects, such as fever, severe low blood pressure, liver damage, blood clots, and bleeding. There is a significant pharmacological effort to create TNF-α variants that are clinically viable and exhibit minimal toxicity. Human TNF-α, which only attaches to the murine TNF-R55 receptor and not the TNF-R75, maintains its cancer-fighting abilities while being less toxic in mice than the murine version that binds to both receptors. Consequently, numerous TNF-α variants with a preference for TNF-R55 have been synthesized. These variants have shown to be toxic to cancer cells in test tubes and demonstrate reduced toxicity in living organisms. |
