Recombinant Human TNF alpha

Recombinant Human TNF alpha  (CG90)

 

产品说明(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

Known as: Tumor Necrosis Factor; Cachectin; TNF-Alpha; Tumor Necrosis Factor Ligand Superfamily Member 2; TNF-a; TNF; TNFA; TNFSF2

 

制剂（Formulation）

Lyophilized from a 0.2 μm filtered solution of 20mM Tris HCl,150mMNaCl,pH8.0.

 

质量控制（Quality Control）

Purity:            Greater than 95% as determined by reducing SDS-PAGE.    

Endotoxin:    Less than 0.1 ng/ug (1 EU/ug) as determined by LAL test.

 

Bioactivity:   Measured in a cytotoxicity assay using L-929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D.

                       The ED50 for this effect is 10-40 pg/mL.

 

复溶（Reconstitution）

Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.    

 

保存（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.     

 

背景（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.

 

电泳(SDS-PAGE)

 

FOR RESEARCH USE ONLY