| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | Soluble form of Tumor Necrosis Factor α, Cachectin, TNF-R75 (TNFR2) |
| Cas No. | |
| Concentration | |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Reconstitution | |
| Solubility | Centrifuge the vial before adding solvent (10,000 x g for 5 minutes) to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in sterile water at a concentration of at least 0.1 mg/mL. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. It is recommended to prepare fresh solutions in working buffers just before use. Repeat freeze-thawing may result in loss of activity. |
| Source | Recombinant, E. coli |
| Storage | |
| Target |
Overview
Recombinant human TNF-alpha protein is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to TNF-R55 (TNFR1), TNF-R75 (TNFR2) biology and/or assay development. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows. Researchers commonly pair it with applications such as Cell survival assay.
Key elements and design rationale
- Molecular identity: CAS: 94948-59-1, MW: 17.35 kDa, Formula: C778H1225N215O231S2.
- Source / origin: Recombinant, E. coli.
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: Yes.
Modifications
Disulfide bonds between: Cys145- Cys177
When used as a biochemical or pharmacological tool, results are best interpreted relative to the experimental system (species, expression level, and assay readout) and with appropriate negative and competition-style controls where relevant. This product is intended for research use only.
Biological background
TNF-α is a cytokine that binds to TNFR-55 and TNFR-75 receptors which are expressed on all somatic cells. It is derived from several types of cells but especially by activated monocytes1-2 and can induce cell death of certain tumor cell lines3. It is a 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.The secretion of the acute phase protein TNF-α initiates a cascade of cytokines and increases vascular permeability, thereby recruiting macrophages and neutrophils to a site of bacterial, fungal, viral or parasitic infection. Without TNF-α, mice infected with gram negative bacteria experience septic shock4.The cytokine possesses both growth stimulating properties and growth inhibitory processes, and it appears to have self-regulatory properties as well. For instance, TNF-α induces neutrophil proliferation during inflammation, but it also induces neutrophil apoptosis upon binding to the TNF-R55 receptor5.TNF-α participates in both inflammatory disorders of inflammatory and non-inflammatory origin6. Originally, sepsis was believed to result directly from the invading bacteria itself, but it was later recognized that host system proteins, such as TNF-α induced sepsis in response.TNF-α seems to serve as a mediator in various pathologies. A few such examples include: septic shock, cancer, AIDS, transplantation rejection, multiple sclerosis, diabetes, rheumatoid arthritis, trauma, malaria, meningitis, ischemia-reperfusion injury, adult respiratory distress syndrome, ankylosing spondylitis, inflammatory bowel disease, psoriasis, hidradenitis suppurativa and refractory asthma. Since TNF-α plays a role in several diseases, a substantial amount of research has been conducted concerning TNF-α and anti-TNF-α therapies. TNF-α inhibition can be achieved with a monoclonal antibody or with a circulating receptor fusion protein. Clinical experience so far concludes that it is safe to give TNF antagonists to cancer patients since TNF antagonist treatment results in a period of disease stabilization or better in 20% of patients with advanced cancer7-10.
Research relevance and current trends
- Using high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor/channel subtypes and signaling microdomains.
- Pairing labeled (e.g., fluorescent) proteins/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.
- Increasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.
Common research applications
- Cell survival assay: commonly used to compare signal, binding, or functional readouts across conditions without implying a specific protocol.
Across these use cases, changes in signal or functional readout are generally interpreted as evidence of differences in target abundance, accessibility, or engagement, but alternative explanations (matrix effects, off-target interactions, or assay artifacts) should be considered.
Notes for experimental interpretation
- Assay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.
- Target complexity: closely related family members, splice variants, and post-translational modifications can influence apparent specificity and potency.
- Matrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.
- Control concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
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