| Field | Specification |
|---|---|
| Mfr No | |
| Biological Activity | |
| Endotoxin Level | |
| Formulation | |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Reconstitution | |
| Source | Escherichia coli |
| Storage |
Scientific Background
Tumor necrosis factor alpha (TNF-α), also called cachectin, 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. 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.
Product Description
E. coli ExpressionRecombinant Tumor Necrosis Factor-alpha Rat protein is produced using a validated E. coli expression system and supplied as lyophilized powder for long-term stability. Suitable for use in functional bioassays, ELISA standard curves, receptor binding studies, antibody validation, and related research applications.
Protein Specifications
| Expression System | E. coli |
|---|---|
| Molecular Weight | Approximately 17.3 kDa. a single, non-glycosylated polypeptide chain containing 157 amino acids. |
| Purity | >95% by SDS-PAGE and HPLC analyses. |
| Endotoxin | Less than 1EU/mg of rRtTNF-α as determined by LAL method. |
| Physical Form | Sterile Filtered White lyophilized (freeze-dried) powder. |
| Formulation | Lyophilized from a 0.2mm filtered concentrated solution in 20mM PB, pH7.2, 150mM… |
| 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. |
| Storage | This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, … |
Functional Activity
Fully biologically active when compared to standard. The Specific Activity is ≥5.0 × 107 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.
Safety & Handling
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE. Made in China
This protein was produced in E. coli expression system. Expression system selection determines glycosylation profile, folding, and post-translational modifications. For cell-based stimulation assays, verify the expression system matches the glycosylation requirements of your target receptor or pathway.
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. Reconstitute in sterile distilled water or PBS at 100 µg/mL as a standard starting concentration. Allow to dissolve at 4°C for 30 minutes without vortexing. Prepare working aliquots in 0.1% BSA carrier protein and store at −80°C.
This protein has been validated for functional bioactivity: Fully biologically active when compared to standard. The Specific Activity is ≥5.0 × 107 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.. Optimal working concentrations may vary depending on your cell type, assay format, and culture conditions. Titrate the protein in a dose-response experiment to determine the optimal concentration for your system.
Endotoxin level is Less than 1EU/mg of rRtTNF-α as determined by LAL method. as determined by the LAL method. Low endotoxin is critical for cell-based studies because endotoxin activates NF-κB and TLR4 signalling in immune cells, producing artefactual cytokine induction that can completely mask the true biological activity of the recombinant protein.
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. F Upon receipt, immediately store at −80°C. Prepare single-use working aliquots to avoid repeated freeze-thaw cycles. Lyophilized protein is stable for 6–12 months at −80°C from the date of receipt.
BioHippo offers flexible sourcing options for qualified research institutions and partners. The following may be available subject to supplier capabilities and order volume.
- Custom quantities: Bulk pricing or non-standard sizes available for high-throughput screening or scale-up projects.
- Custom formulation: Alternative reconstitution buffers or carrier proteins may be accommodated on request.
- Extended QC data: Additional bioactivity assay data, endotoxin reports, or SEC-HPLC purity profiles available on request.
Contact BioHippo customer support to discuss your requirements.
