Recombinant Human TNF alpha (C-6His)
- Cat. No.：EPT101
- Price：USD $ 540.00
- Clicks：1457
Product Detail
Basic Information
| Size | 10ug |
|---|
| Expression Host | E.coli |
|---|
| Tag | C-6His |
|---|
Physical Properties
| Molecular Weight | 18.5 KDa |
|---|
| Apparent Molecular Weight | 16 KDa, reducing conditions |
|---|
| Form | Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0. |
|---|
| Purity | Greater than 95% as determined by reducing SDS-PAGE. |
|---|
Activity & Endotoxin
| Endotoxin Level | Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
|---|
Storage & Shipping
| Reconstitution | Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
|---|
| Storage | Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months. |
|---|
| Shipping Condition | The product is shipped at ambient temperature.
Upon receipt, store it immediately at the temperature listed below. |
|---|
Detailed Description
| Background | Tumor Necrosis Factor-α (TNF-α) is secreted by macrophages, monocytes, neutrophils, T-cells, and NK-cells following stimulation by bacterial LPS. Cells expressing CD4 secrete TNF-α while cells that express CD8 secrete little or no TNF-α. Synthesis of TNF-α can be induced by many different stimuli including interferons, IL2, and GM-CSF. The clinical use of the potent anti-tumor activity of TNF-α has been limited by the proinflammatory side effects such as fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF-α mutants with low systemic toxicity has been of intense pharmacological interest. Human TNF-α that binds to murine TNF-R55 but not murine TNF-R7, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF-α, which binds to both murine TNF receptors. Based on these results, many TNF-α mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro and have exhibited lower systemic toxicity in vivo. Recombinant Human TNF-α High Active Mutant differs from the wild-type by amino acid subsitution of amino acids 1-7 with Arg8, Lys9, Arg10 and Phe157. This mutant form has been shown to have increased activity with less inflammatory side effects in vivo. |
|---|
