TNF-α (Variant), Human

(Recombinant Human Tumor Necrosis Factor TNF-α, TNF-alpha, Cachectin, Cachexin)

Purity: >98% by SDS-PAGE and HPLC analyses

Source: Escherichia coli

Tumor necrosis factor (or TNF-α), also called cachectin, is produced by neutrophils, activated lymphocytes, macrophages, NK cells, LAK cells, astrocyte endothelial cells, smooth muscle cells and some transformed cells. TNF occurs as a secreted, soluble form and as a membrane-anchored form, both of which are biologically active. The naturally-occurring form of TNF is glycosylated, but non-glycosylated recombinant TNF has comparable biological activity. The biologically active native form of TNF is reportedly a trimer. Human and murine TNF has approximately 79% homology at the amino acid level and there is crossreactivity between the two species. Two types of receptors for TNF, p55 and p75, have been described and virtually all cell types studied show the presence of one or both of these receptor types.

The clinical use of the potent antitumor activity of TNF has been limited by the proinflammatory side effects including fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF mutants with low systemic toxicity has been an intense pharmacological interest. Human TNF variants, which bind to the murine TNF-R55 but not to the murine TNF-R75, exhibit retained antitumor activity and reduced systemic toxicity in mice compared with murine TNF, which binds to both murine TNF receptors. Based on these results, many TNF mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro, and exhibited lower systemic toxicity in vivo.

rHuTNF-Variant General Information
Amino Acid Sequence (151 aa):
MRKRKPVAHV VANPQAEGQL QWLNRRANAL LANGVELRDN QLVVPSEGLY LIYSQVLFKG QGCPSTHVLL THTISRIAVS YQTKVNLLSA IKSPCQRETP EGAEAKPWYE PIYLGGVFQL EKGDRLSAEI NRPDYLDFAE SGQVYFGIIA F

Reconstitution:
The sample should be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in aqueous buffer containing 10mM HAc to a concentration of 0.1-1.0 mg/mL. Reconstituted solutions are stable for up to one week at 2-8°C. Stock solutions should be aliquoted and stored at -80°C. Further dilutions should be made in appropriate buffered solutions..

Storage:
The lyophilized sample is stable at 2-8°C, but should be kept desiccated at -20°C for long term storage. The reconstituted sample can be apportioned into working aliquots and stored -80°C for maximal stability. Avoid repeated freeze/thaw cycles.

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