TNF alpha Protein (AA 77-233) (His tag)
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- Target See all TNF alpha Proteins
- TNF alpha (Tumor Necrosis Factor alpha (TNF alpha))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 77-233
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This TNF alpha protein is labelled with His tag.
- Purpose
- Recombinant Human Tumor Necrosis Factor α/TNFα (C-6His)
- Sequence
- MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA EAKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIALLE HHHHHH
- Characteristics
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Recombinant Human Tumor Necrosis Factor α/TNFα (C-6His)
- Purity
- > 95 % as determined by reducing SDS-PAGE.
- Sterility
- 0.2 μm filtered
- Endotoxin Level
- Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test
- Top Product
- Discover our top product TNF alpha Protein
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
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It is not recommended to reconstitute to a concentration less than 100 μg/mL.
Dissolve the lyophilized protein in ddH2O.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles. - Buffer
- Lyophilized from a 0.2 μm filtered solution of 20 mM PB,150 mM NaCl, pH 7.4.
- Handling Advice
- Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
- Storage
- 4 °C/-20 °C/-80 °C
- Storage Comment
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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.
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- Target
- TNF alpha (Tumor Necrosis Factor alpha (TNF alpha))
- Alternative Name
- Tumor Necrosis Factor/TNF (TNF alpha Products)
- Background
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Recombinant Human Tumor necrosis factor/TNF is produced with our E. coli expression system. The target protein is expressed with sequence (Val77-Leu233) of Human TNF fused with a 6His tag at the C-terminus.
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 AA subsitution of AAs 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. - Molecular Weight
- 18.5 kDa
- UniProt
- P01375
- Pathways
- NF-kappaB Signaling, Apoptosis, Caspase Cascade in Apoptosis, TLR Signaling, Cellular Response to Molecule of Bacterial Origin, Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process, Production of Molecular Mediator of Immune Response, Positive Regulation of Endopeptidase Activity, Hepatitis C, Protein targeting to Nucleus, Inflammasome
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