TNF b Human, His
Description
Production and Purification
TNF-β Human, His is synthesized via bacterial expression systems and purified using affinity chromatography:
Biological Activity and Functional Mechanisms
TNF-β Human, His exhibits cytotoxic and pro-inflammatory effects through receptor binding and signaling pathways:
Key Activities
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Cytotoxicity: Induces apoptosis in tumor cells (e.g., L929 fibrosarcoma) in the presence of actinomycin D (ED₅₀ < 0.3 ng/mL).
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Inflammatory Signaling: Activates nuclear factor-κB (NF-κB) in chondrocytes, promoting matrix metalloproteinase (MMP) and cyclooxygenase-2 (COX-2) expression, contributing to rheumatoid arthritis (RA) pathology.
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Immune Regulation: Binds TNFR1 and TNFR2, modulating lymphoid organ development and immune cell adhesion.
Comparison with TNF-α
| Feature | TNF-β | TNF-α |
|---|---|---|
| Primary Source | Activated T/B lymphocytes | Macrophages, monocytes |
| Receptor Binding | TNFR1, TNFR2 (via soluble or membrane-bound forms) | TNFR1 (soluble), TNFR2 (membrane-bound) |
| Cytotoxicity | Direct tumor cell lysis | Tissue necrosis, systemic inflammation |
| Sequence Homology | 35% with TNF-α | — |
Research Applications and Clinical Relevance
TNF-β Human, His is utilized in:
Experimental Models
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In Vitro Assays:
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In Vivo Studies:
Therapeutic Potential
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Targeted Cancer Therapy: Exploiting TNF-β’s cytotoxicity against tumor cells.
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Anti-Inflammatory Strategies: Neutralizing TNF-β in autoimmune diseases refractory to TNF-α inhibitors.
Standard Curve for TNF-β Assay
| TNF-β Concentration (pg/mL) | Signal (EU) | %CV |
|---|---|---|
| 0.23 | 121 | 6.7 |
| 1.2 | 339 | 6.0 |
| 4.9 | 1021 | 4.7 |
| 20 | 3642 | 6.6 |
SEC-MALS Analysis
Product Specs
Product Science Overview
Tumor Necrosis Factor-Beta (TNF-β), also known as Lymphotoxin-alpha (LT-α), is a cytokine that plays a crucial role in the regulation of immune responses and inflammation. It is a member of the tumor necrosis factor superfamily, which includes other well-known cytokines such as Tumor Necrosis Factor-Alpha (TNF-α). TNF-β is produced by lymphocytes and exhibits cytotoxic activity against tumor cells, making it a significant molecule in cancer research and immunotherapy .
The human recombinant form of TNF-β, tagged with a His-tag, is a single, non-glycosylated polypeptide chain consisting of 192 amino acids. The His-tag, a sequence of histidine residues, is added to the N-terminus of the protein to facilitate purification through affinity chromatography. This recombinant protein is typically expressed in Escherichia coli (E. coli) and purified using proprietary chromatographic techniques .
TNF-β functions as a soluble homotrimer and can also form heterotrimers with Lymphotoxin-beta (LT-β) when anchored to the cell surface. It exhibits a variety of biological activities, including the induction of cell death in certain tumor cell lines, regulation of immune responses, and involvement in the development of secondary lymphoid organs. TNF-β’s cytotoxic activity is measured using assays such as the cytotoxicity assay with L929 mouse fibrosarcoma cells in the presence of actinomycin D .
The recombinant form of TNF-β is widely used in research to study its role in immune regulation, inflammation, and cancer. It is utilized in various assays to investigate its cytotoxic effects, signaling pathways, and interactions with other cytokines. The His-tagged version allows for easy purification and detection, making it a valuable tool in biochemical and cellular studies .
The recombinant TNF-β protein is typically stored at -20°C for long-term storage, with the addition of carrier proteins such as human serum albumin (HSA) or bovine serum albumin (BSA) to enhance stability. It is recommended to avoid multiple freeze-thaw cycles to maintain the protein’s integrity. For short-term use, the protein can be stored at 4°C .
