Publications

Synthesis of lipophilic genistein derivatives and their regulation of IL-12 and TNF-? in activated J774A.1 cells.

Genistein modulates inflammatory responses in part by reducing the production of the pro-inflammatory cytokines IL-12, TNF-? and nitric oxide (NO), by activated macrophages in response to lipopolysaccharide (LPS) stimulus. Previous studies have shown that synthetic lipophilic genistein glycosides were significantly more active than hydrophilic glycosides. The aim of this study was to synthesize and evaluate the effect of novel lipophilic genistein derivatives on IL-12, TNF-? and NO production by J774A.1 cells. The results show that the modification of genistein enables the generation of non-cytotoxic compounds with increased IL-12 inhibition. However, these derivatives failed to inhibit TNF-?. The NO production was notably inhibited by the monoester (2, 3) and monoether (6, 7) compounds in a dose-dependent manner. © 2011 John Wiley & Sons A/S.

2011 Dec 15,.

Protein Name:TNF-α (Mutant)
Gene Name:TNF TNFA TNFSF2

Cat.No.Price/SizeQtyCart
C036

Recombinant Human Recombinant Human TNF Alpha, Tumor Necrosis Factor Alpha | Novoprotein
(CatNo. C036)

Recombinant Human TNF Alpha, Tumor Necrosis Factor-α/TNF-α Mutant produced in E. coli is a single non-glycosylated polypeptide chain containing 151 amino acids with a molecular mass of 16,886 Daltons.

Recombinant Human TNF Alpha: 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.