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Recombinant Human Tumor necrosis factor (TNF), partial (Active) | CSB-AP004881HU

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CSB-AP004881HU
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  • Recombinant Human Tumor necrosis factor (TNF) ,partial (Active)
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
€288.00 - €652.00
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Description

Recombinant Human Tumor necrosis factor (TNF) ,partial (Active) | CSB-AP004881HU | Cusabio

Protein Description: Extracellular Domain

Alternative Name (s) : Tumor Necrosis Factor; Cachectin; TNF-Alpha; Tumor Necrosis Factor Ligand Superfamily Member 2; TNF-a; TNF; TNFA; TNFSF2

Gene Names: TNF

Research Areas: Cancer

Species: Homo sapiens (Human)

Source: E.coli

Tag Info: N-terminal 6xHis-tagged

Expression Region: 57-233aa

Sequence Info: GPQREEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL

Biological Activity: The ED50 as determined in a cytotoxicity assay using L‑929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D is less than 1 ng/ml.

MW: 21.8 kDa

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

Endotoxin: Less than 1.0 EU/µg as determined by LAL method.

Relevance: 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.

PubMed ID:

Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.

Function: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Upregulates the expression of protein phosphatase 1 (PP1) , which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective

Involvement in disease: Psoriatic arthritis (PSORAS)

Subcellular Location: Cell membrane, Single-pass type II membrane protein, SUBCELLULAR LOCATION: Tumor necrosis factor, membrane form: Membrane, Single-pass type II membrane protein, SUBCELLULAR LOCATION: Tumor necrosis factor, soluble form: Secreted, SUBCELLULAR LOCATION: C-domain 1: Secreted, SUBCELLULAR LOCATION: C-domain 2: Secreted

Protein Families: Tumor necrosis factor family

Tissue Specificity:

Paythway: MAPKsignalingpathway

Form: Lyophilized powder

Buffer: Lyophilized from a 0.2 μm filtered 20 mM PB, 100 mM NaCl, pH 7.2

Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Uniprot ID: P01375

Uniprot Entry Name:

HGNC Database Link: HGNC

UniGene Database Link: UniGene

KEGG Database Link: KEGG

STRING Database Link: STRING

OMIM Database Link: OMIM

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