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Recombinant Human TNF alpha (C-6His)
Recombinant Human TNF alpha (C-6His)
Recombinant Human Tumor Necrosis Factor Alpha is produced by our E.coli expression system and the target gene encoding Val77-Leu233 is expressed with a 6His tag at the C-terminus.
Catalog No:
EPT101
Regular price
$89.00 USD
Regular price
Sale price
$89.00 USD
Unit price
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per
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Product Details
Accession
P01375
Molecular Weight
18.5 KDa
Apparent Molecular Weight
16 KDa, reducing conditions
Purity
Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin
Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Expression Host
E. coli
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.
Shipping Condition
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed in the Storage field.
Storage Condition and Shelf Life
Lyophilized protein should be stored at < -20C, 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 < -20C for 3 months.
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.
Analyte
TNF alpha
Regulatory Status
For Research Use Only
