| Source: |
Escherichia coli. |
| Molecular Weight: |
Approximately 18.3 kDa, a single, non-glycosylated polypeptide chain containing 164 amino acids with Met and 6 × His at N-terminus. |
| AA Sequence: |
MHHHHHHVRS SSRTPSDKPV AHVVANPQAE GQLQWLNRRA NALLANGVEL RDNQLVVPSE GLYLIYSQVL FKGQGCPSTH VLLTHTISRI AVSYQTKVNL LSAIKSPCQR ETPEGAEAKP WYEPIYLGGV FQLEKGDRLS AEINRPDYLD FAESGQVYFG IIAL |
| Purity: |
> 97% 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 × 107IU/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 rHuTNF-α/TNFSF2, His 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: |
TNF-α, known as cachectin, is a prominent member of the TNF family that induces cell death. It is secreted by various cells, including neutrophils, activated lymphocytes, macrophages, and others. TNF-α exists in both a secreted, soluble form and a membrane-bound form, each biologically active. While the natural TNF-α is glycosylated, the non-glycosylated recombinant version is similarly effective. The active native structure of TNF-α is a trimer. Human and mouse TNF-α share a high degree of similarity and can cross-react. Two receptor types for TNF-α have been identified, and most studied cells express at least one of them. |
