| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Tumor necrosis factor|Cachectin|TNF-alpha|Tumor necrosis factor ligand superfamily member 2|TNF-a|Tumor necrosis factor, membrane form|N-terminal fragment|NTF|Intracellular domain 1|ICD1|Intracellular domain 2|ICD2|C-domain 1|C-domain 2|Tumor necrosis factor, soluble form|TNF|TNFA| TNFSF2 |
| Assay Time | |
| Detection Method | |
| Detection Range | |
| Product Type | |
| Reactivity | |
| Sample Type(s) | Serum, Plasma, Cell Culture Supernatant, cell or tissue lysate, Other liquid samples |
| Sensitivity | |
| Species | |
| Storage | |
| Target | |
| UniProt # |
Background
canine TNF-α (Tumor Necrosis Factor Alpha) is a molecular target commonly studied in immunology, cardiovascular, and cancer research. Many proteins are studied as molecular readouts that can change with cellular state, tissue remodeling, or stress responses.
Biological role and mechanism
The biological role of TNF-α is typically understood in terms of its molecular category and interaction network. Depending on the model system, it may participate in cell–cell communication, intracellular signaling, enzymatic processing, or regulation of gene expression programs. Mechanistic interpretation is often strengthened by considering upstream regulators and downstream readouts rather than relying on a single marker.
Expression and abundance of TNF-α can vary by tissue, cell type, and physiological state. In many systems, levels are influenced by factors such as developmental stage, immune activation, metabolic status, and cellular stress. Because sample matrix and pre-analytical handling can affect measured concentrations, interpretation is typically strongest when experiments keep collection and processing consistent across groups.
Nomenclature and related terms
TNF-α (Tumor Necrosis Factor Alpha) may also be referenced as Tumor necrosis factor, Cachectin, and TNF-alpha in the literature or in databases. When comparing results across studies, confirm that the reported analyte refers to the same molecule, species context, and molecular form (e.g., precursor vs mature protein, or soluble vs membrane-associated forms).
Why it matters in research
- Understanding how TNF-α relates to innate and adaptive immune responses, cytokine signaling networks, host–pathogen interactions, and immune cell activation and trafficking in immunology, cardiovascular, and cancer research.
- Interpreting shifts in TNF-α levels alongside other pathway components or complementary markers.
- Connecting molecular changes to phenotypes such as inflammation, remodeling, metabolism shifts, or cell-state transitions (context-dependent).
Molecular forms and interpretation
For some targets, isoforms, proteolytic processing, or post-translational modifications (such as phosphorylation or glycosylation) can influence function and apparent abundance. If multiple molecular forms are expected in your model, align interpretation with the form most relevant to the biological question.
Disease and translational relevance
TNF-α has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with immunology, cardiovascular, and cancer studies. These associations are interpreted as research findings rather than diagnostic or therapeutic claims, and they should be evaluated alongside model-specific covariates and study design.
Can’t Find What You’re Looking For? We can help you source the best match or customize an ELISA solution for your study. Options may include alternative target synonyms, different species reactivity, sample type/matrix compatibility (serum/plasma/lysate/supernatant), assay format (sandwich/competitive), sensitivity/range, detection chemistry (colorimetric/fluorescent/chemiluminescent), plate format (pre-coated/uncoated, strips vs full plate), 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.
In Vitro Antiviral and Anti-Inflammatory Activities of N-Acetylglucosamine: Development of an Alternative and Safe Approach to Fight Viral Respiratory Infections
IF: 6.208 Journal: International Journal of Molecular Sciences Cited Date: 2023-03-17
Newcastle disease virus LaSota strain induces apoptosis and activates the TNFα/NF‐κB pathway in canine mammary carcinoma cells
IF: 2.385 Journal: Veterinary and Comparative Oncology Author: Department of Veterinary Clinical Sciences, College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China Cited Date: 2023-06-16
Alterations of Pro-Inflammatory Cytokines and Tissue Protein Expressions in Cats with Interstitial Cystitis
IF: 1.217 Journal: Pakistan Veterinary Journal Cited Date: 2019-03-07
Effect of intra-articular administration of autologous PRP and activated PRP on inflammatory mediators in dogs with osteoarthritis
IF: 0.877 Journal: veterinary medicine Cited Date: 2020-02-01
Can procalcitonin be used as a clinical biomarker during bacterial, viral and parasitic infections in dogs?
IF: 0.323 Journal: Japanese Journal of Veterinary Research Cited Date: 2021-03-26
Evaluation of serum levels of CRP and TNF-α in dogs infected with Ehrlichia canis and Anaplasma phagocytophilum
IF: Journal: Open Veterinary Journal Author: Department of General and Clinical Pathology, Faculty of Veterinary Medicine, Trakia University, Stara Zagora, Bulgaria Cited Date: 2025-10-11
Investigation of Inflammatory Mediators and Metalloproteinase (MMP-2 and MMP-9) Enzymes Effects on Application of Intra-articular Autologous Platelet Rich Plasma (PRP) or Bio-Physical Activator of Autologous Platelet Rich Plasma in Dogs with Osteoarthritis
IF: Journal: Kurtulus PARLAKDEPARTMENT OF SURGERY PHD THESIS / Cited Date: 2018-12-16