TNF-beta/TNFSF1 Protein, Human

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TNF-β (tumor necrosis factor β) also called lymphotoxin-α (LT-α), a member of the tumor necrosis factor superfamily, is a cytokine produced by lymphocytes. TNF-β activates the NF-κB signaling pathway, inducing cancer cell proliferation, invasion. TNF-β up-regulates genes connected with metastasis, promotes epithelial-to-mesenchymal-transition, stimulates its own expression. TNF-β mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. TNF-beta/TNFSF1 Protein, Human is a recombinant protein consisting of 158 amino acids (L35-L205) and is produced in E. coli.

For research use only. We do not sell to patients.
  • Species: Human
  • Source: E. coli
  • Storage:
    Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
  • Biological Activity
  • Technical Parameters
  • Product Properties
  • Documentation
  • References
  • Help & FAQs

Biological Activity

Description

TNF-β (tumor necrosis factor β) also called lymphotoxin-α (LT-α), a member of the tumor necrosis factor superfamily, is a cytokine produced by lymphocytes. TNF-β activates the NF-κB signaling pathway, inducing cancer cell proliferation, invasion[1][2]. TNF-β up-regulates genes connected with metastasis, promotes epithelial-to-mesenchymal-transition, stimulates its own expression[3]. TNF-β mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. TNF-beta/TNFSF1 Protein, Human is a recombinant protein consisting of 158 amino acids (L35-L205) and is produced in E. coli.

Background

TNF-β is expressed by a variety of cells, including T cells, B cells and natural killer (NK) cells[1].
The amino acid sequence of human TNF beta protein has low homology between mouse and rat TNF alpha protein. While, rat TNF alpha shares 95.54% aa sequence identity with mouse TNF alpha protein.
TNF-β can be secreted and binds with high affinity to TNF receptors 1 and 2 (TNFR-1 and TNFR-2), and it is transiently expressed on the cell surfaces of activated B and T cells, where it forms a complex with LT-β as an LTα1β2 heterotrimer, activates NF-kB, MAPK, and PI3K/AKT pathways and induces cancer cells proliferation, invasion[1].
TNF-β is translated as a 25 kDa glycosylated polypeptide with 171 amino acid residues. TNF-β up-regulates of NF-κB signaling and activates of pro-inflammatory activity[1].TNF-β induces tumor cells proliferation, migration and increases the expression of p-p65, p-IkBα in a dose dependent manner[2].

In Vitro

TNF-β (human) (1, 10 ng/mL; 12 h; primary human chondrocytes) induces TNF-β and TNF-β-R expression on surface of chondrocytes and enhances adhesiveness to T lymphocytes when cocultured with T lymphocytes (Jurkat cells) for 4 h[1].
TNF-β (human) (1, 5, 10 ng/mL; 24 h) markedly stimulates HCT116 proliferation and migration in a dose dependent manner, and increases the expression of p-p65, p-IkBα in HCT116 cells in a dose dependent manner[2].

Verified Bioactivity

The ED50 is <80 pg/mL as measured by L-929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D, corresponding to a specific activity of >1.25 × 107 units/mg.

Technical Parameters

  • Species Human
  • Source E. coli
  • Tag Tag Free
  • Accession
  • Gene ID
  • Molecular Construction
    • N-term
    • TNF-β (L35-L205)
      Accession # P01374
    • C-term
  • Protein Length

    Full Length of Mature Protein

  • Synonyms

    LTA; Lymphotoxin Alpha (TNF Superfamily, Member 1); Prev. TNFB; Lymphotoxin Alpha Transcript Variant 4; TNFSF1; Lymphotoxin Alpha Transcript Variant 3; Tumor Necrosis Factor Ligand Superfamily Member 1; Tumor Necrosis Factor Ligand 1E; Lymphotoxin-Alpha;

  • AA Sequence

    LPGVGLTPSAAQTARQHPKMHLAHSTLKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAYSPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQLSTHTDGIPHLVLSPSTVFFGAFAL

  • Predicted Molecular Mass

    18.8 kDa

  • Molecular Weight

    Approximately 15-19 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

  • Purity

    ≥ 95%, as determined by reducing SDS-PAGE.

Product Properties

Appearance

Lyophilized powder

Formulation

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Storage & Stability

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Shipping

Room temperature in continental US; may vary elsewhere.

References

Calculators

Reconstitution Calculator

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

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=
Mass (in vial) Mass (in vial)
÷
Desired Reconstitution Concentration Desired Reconstitution Concentration
Dilution Calculator

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

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Volume (start) Volume (start)
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The Specific Activity Calculator Equation
  • Specific Activity (Unit/mg)
  • Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) Specific Activity (Unit/mg)
Unit/mg
= 106 ÷
Biological Activity (ED50) Biological Activity (ED50)
106 ÷
ng/mL
MOQ
Minimum order quantity
100 mg

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