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H8916 Sigma-Aldrich

Tumor Necrosis Factor-α human

TNF-α, recombinant, expressed in HEK 293 cells, suitable for cell culture

Synonym: TNF-α

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Properties

Related Categories Cell Culture, Growth Factors and Cytokines, Reagents and Supplements, Tumor Necrosis Factor (TNF) Superfamily
Quality Level   100
biological source   human
recombinant   expressed in HEK 293 cells
assay   ≥95% (SDS-PAGE)
form   lyophilized powder
potency   ≤1.0 ng/mL ED50
quality   endotoxin tested
mol wt   17 kDa (glycosylated)
  ~17.4 kDa
packaging   pkg of 10 μg
storage condition   avoid repeated freeze/thaw cycles
application(s)   cell culture | mammalian: suitable
impurities   ≤1 EU/μg
UniProt accession no.   P01375
storage temp.   −20°C
Gene Information   human ... TNF(7124)

Description

General description

The TNFα (tumor necrosis factor α) gene is mapped to human chromosome 6p21.33. TNFα is a member of TNF superfamily.

Application

Tumor Necrosis Factor-α (TNF-α) human has been used
• In induction of netting neutrophils by anti-neutrophil cytoplasmic antibody and to study its effect on platelet activation and formation of monomeric C-reactive protein.
• To study the effect of TNF-α on miR-221 and fractalkine expression.
• To induce inflammatory cell responses.
• In NF-κB luciferase reporter assay.

Packaging

10 μg in poly bottle

Biochem/physiol Actions

Tumore necrosis factor-α (TNF-α), also known as cachectin, is expressed as a 26 kDa membrane bound protein and is then cleaved by TNF-α converting enzyme (TACE) to release the soluble 17 kDa monomer, which forms homotrimers in circulation. TNF-α plays roles in antitumor activity, immune modulation, inflammation, anorexia, cachexia, septic shock, viral replication and hematopoiesis. TNF-α is expressed by a great variety of cells, with numerous inductive and suppressive agents. Primarily, TNF-α is produced by macrophages in response to immunological challenges such as bacteria (lipopolysaccharides), viruses, parasites, mitogens and other cytokines. TNF-α is cytotoxic for many transformed cells (its namesake activity) but in normal diploid cells, it can stimulate proliferation (fibroblasts), differentiation (myeloid cells) or activation (neutrophils). TNF-α also shows antiviral effects against both DNA and RNA viruses and it induces production of several other cytokines. Although TNF-α is used in clinical trials as an antitumor agent, Sigma′s cytokine, growth factor and hormone products are for research only. TNF-α and the related molecule TNF-β (LT-α) share close structural homology with 28% amino acid sequence identity and both activate the same TNF receptors, TNFR1 and TNFR2. Mouse and human TNF-α share 79% amino acid sequence identity. Unlike human TNF-α, the mouse form is N-glycosylated.

Preparation Note

Tumor Necrosis Factor-α (TNF-α) is expressed in human HEK 293 cells and has been shown to be predominantly a glycosylated, non-covalently linked homotrimer with a molecular mass of 51 kDa (gel filtration). Production in human 293 cells offers authentic glycosylation. Glycosylation contributes to stability in cell growth media and other applications.

Analysis Note

The specific activity was determined by the dose-dependent cytotoxity of the TNF alpha sensitive cell line L-929 in the presence of actinomycin D.

Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Frequently Asked Questions

Which document(s) contains shelf-life or expiration date information for a given product?
If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.
How do I get lot-specific information or a Certificate of Analysis?
The lot specific COA document can be found by entering the lot number above under the "Documents" section.
How do I find price and availability?
There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote. USA customers: 1-800-325-3010 or view local office numbers.
What is the Department of Transportation shipping information for this product?
Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
How should product H8916, Tumor Necrosis Factor-alpha human be dissolved?
Product H8916 is soluble in sterile PBS or sterile water with 0.1 % endotoxin free human serum albumin. H8916 can be made without addition of albumin providing the protein concentration is high, 200-500 μg/ml. Since the vial contains 10 μg, then a volume of either sterile PBS or sterile water in the range of 20 -50 μl will be added to give the 200 -500 μg/ml protein concentration.
What is the solution stablity of H8916, Tumor Necrosis Factor-alpha human?
A stock solution of H8916 can be kept at a concentration of200-500 ug/ml (micrograms/ml) for up to 1 week at 4 °C.For long term storage, aliquot into single use size and store at -80 °C. Please avoid freeze thaw cycles as this can effect the activity.
How should product H8916, Tumor Necrosis Factor-alpha human be dissolved?
Product H8916 is soluble in sterile PBS or sterile water with 0.1 % endotoxin free human serum albumin. H8916 can be made without addition of albumin providing the protein concentration is high, 200-500 μg/ml. Since the vial contains 10 μg, then a volume of either sterile PBS or sterile water in the range of 20 -50 μl will be added to give the 200 -500 μg/ml protein concentration.
What is the difference between H8916 and T6674, Tumor Necrosis Factor-α human?
Both products are recombinant Tumor Necrosis Factor-α human, however, they are expressed in different cell types.T6674 is expressed in Escherichia coli and H8916 is expressed in human HEK 293 cells. When recombinant human proteins are produced in human cells they are more authentic in terms of proper folding, phosphorylation, and glycosylation of the protein.Human proteins expressed inEscherichia coli do not undergo these proper post-translational modifications.
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References

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