TNF-alpha/TNFSF2 Protein, Guinea (N-His)

Customer Review

Based on 1 Customer Validation

TNF-alpha/TNFSF2 protein binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR, inducing cell death in specific tumors and causing fever. It can also stimulate cell proliferation, induce insulin resistance, promote angiogenesis, and mediate bone resorption. TNF-alpha's intracellular domain induces IL12 production, highlighting its diverse physiological impact. TNF-alpha/TNFSF2 Protein, Guinea (N-His) is the recombinant TNF-alpha/TNFSF2 protein, expressed by E. coli , with N-6*His labeled tag.

For research use only. We do not sell to patients.
  • Species: Others
  • 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
  • Help & FAQs

Biological Activity

Description

TNF-alpha/TNFSF2 protein binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR, inducing cell death in specific tumors and causing fever. It can also stimulate cell proliferation, induce insulin resistance, promote angiogenesis, and mediate bone resorption. TNF-alpha's intracellular domain induces IL12 production, highlighting its diverse physiological impact. TNF-alpha/TNFSF2 Protein, Guinea (N-His) is the recombinant TNF-alpha/TNFSF2 protein, expressed by E. coli , with N-6*His labeled tag.

Background

TNF-alpha/TNFSF2 protein, a cytokine, binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. Predominantly secreted by macrophages, it possesses the ability to induce cell death in specific tumor cell lines and serves as a potent pyrogen, causing fever through direct action or by stimulating interleukin-1 secretion. TNF-alpha is implicated in the induction of cachexia, and under certain conditions, it can stimulate cell proliferation and induce cell differentiation. Moreover, it induces insulin resistance in adipocytes by inhibiting insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake, contributing to GKAP42 protein degradation in adipocytes and, consequently, TNF-induced insulin resistance. Beyond its metabolic effects, TNF-alpha plays a role in angiogenesis by synergistically inducing VEGF production with IL1B and IL6. Additionally, it promotes osteoclastogenesis, mediating bone resorption, and its intracellular domain (ICD) form induces IL12 production in dendritic cells, underscoring its multifaceted impact on diverse physiological processes.

Verified Bioactivity

Measured in a cytotoxicity assay using L-929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED50 this effect is 0.04334 ng/mL, corresponding to a specific activity is 2.307×107units/mg.

MCE Validation Data

  • Purity - SDS-PAGE

    Purity - SDS-PAGE

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

  • Bioactivity - Cell-Based Assay

    Bioactivity - Cell-Based Assay

    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 0.04334 ng/mL, corresponding to a specific activity is 2.307×107 units/mg.

Technical Parameters

  • Species Others
  • Source E. coli
  • Tag N-6*His
  • Accession
  • Gene ID
  • Molecular Construction
    • N-term
    • 6*His
    • TGF-α (L79-L234)
      Accession # P51435
    • C-term
  • Protein Length

    Full Length of Tumor necrosis factor, soluble form Chain

  • Synonyms

    TNF; Tumor Necrosis Factor (TNF Superfamily, Member 2); Prev. TNFA; Tumor Necrosis Factor-Alpha; TNF-Alpha; Tumor Necrotic Factor Alpha; TNFSF2; TNF Superfamily, Member 2; Tumor Necrosis Factor Ligand Superfamily Member 2; TNF, Macrophage-Derived; TNF-A;

  • AA Sequence

    LRSASQNDNDKPVAHVVANQQAEEELQWLSKRANALLANGMGLSDNQLVVPSDGLYLIYSQVLFKGQGCPSYLLLTHTVSRLAVSYPEKVNLLSAIKSPCQKETPEGAERKPWYEPIYLGGVFQLQKGDRLSAEVNLPQYLDFADSGQIYFGVIAL

  • Predicted Molecular Mass

    17.2 kDa

  • Molecular Weight

    Approximately 19 kDa, based on SDS-PAGE under reducing conditions.

  • Purity

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

Product Properties

Appearance

Lyophilized powder.

Formulation

Lyophilized from a 0.22 μm filtered solution of 50 mM Tris-HCl, 300 mM NaCl, pH 7.4.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

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.

Calculators

Reconstitution Calculator

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

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

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

Concentration (start) Concentration (start)
×
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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