Recombinant Human TNF alpha (C-6His)

Recombinant Human TNF alpha (C-6His)

Vendor: ELK Biotechnology
Item number: EPT101
Availability: In Stock
$89.00
$89.00
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Manual
Size: 10ug
Subtotal: $89.00
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Terms and Conditions

Recombinant Human TNF alpha (C-6His)

Recombinant Human TNF alpha (C-6His)

$89.00
Recombinant Human TNF alpha (C-6His)

Recombinant Human TNF alpha (C-6His)

$89.00
Size: 10ug
Description
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.
Accession
P01375
Molecular weight
18.5 KDa
Apparent molecular weight
16 KDa, reducing conditions
Other names
Tumor Necrosis Factor; Cachectin; TNF-Alpha; Tumor Necrosis Factor Ligand Superfamily Member 2; TNF-a; TNF; TNFA; TNFSF2
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.
Redissolve
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.
Delivery condition
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Manual
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.

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