| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Irisin|Fibronectin type III repeat-containing protein 2|Fibronectin type III domain-containing protein 5|Irisin|FNDC5|FRCP2 |
| 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
rat Irisin (III) is a molecular target commonly studied in metabolism 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 Irisin 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 Irisin 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
Irisin (III) may also be referenced as Irisin, Fibronectin type III repeat-containing protein 2, and Fibronectin type III domain-containing protein 5 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 Irisin relates to energy homeostasis, glucose and lipid metabolism, insulin sensitivity and endocrine regulation, and adipose–liver crosstalk in metabolism research.
- Interpreting shifts in Irisin 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
Irisin has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with metabolism 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.
Effect of Omega-3 or Omega-6 Dietary Supplementation on Testicular Steroidogenesis, Adipokine Network, Cytokines, and Oxidative Stress in Adult Male Rats
IF: 6.543 Journal: Oxidative Medicine and Cellular Longevity Cited Date: 2021-07-08
Inhibitory effects of naringenin on estrogen deficiency-induced obesity via regulation of mitochondrial dynamics and AMPK activation associated with white adipose tissue browning
IF: 6.1 Journal: Life Sciences Author: Graduate Institute and Department of Pharmacology, National Defense Medical Center, Taipei, Taiwan Cited Date: 2024-02-23
Coenzyme Q10 ameliorates obesity by promoting white adipose tissue browning and preserving mitochondrial dynamics in ovariectomized rats fed a high-fat diet
IF: 4.9 Journal: The Journal of Nutritional Biochemistry Author: Department and Graduate Institute of Pharmacology, College of Pharmacy, National Defense Medical University, Taipei. Cited Date: 2025-12-05
Contribution of changes in the orexin system and energy sensors in the brain in depressive disorder-a study in an animal model
IF: 4.4 Journal: Pharmacological Reports Author: Laboratory of Immunoendocrinology, Department of Experimental Neuroendocrinology, Maj Institute of Pharmacology, Polish Academy of Sciences, Sm?tna 12, 31-343, Kraków, Poland Cited Date: 2024-01-26
Effects of Combining Exercise and Dietary Shifts on Motor Coordination and Oxidative Markers in a High‐Fat Diet Model in Rats
IF: 4.2 Journal: Comprehensive Physiology Author: Group of Neurophysiology, Department of Biology, University of the Balearic Islands, Palma de Mallorca, Balearic Islands, Spain. Cited Date: 2025-12-05
Fermented Goat Milk Consumption Enhances Brain Molecular Functions during Iron Deficiency Anemia Recovery
IF: 4.171 Journal: Nutrients Cited Date: 2019-10-07
MATERNAL HIGH-FAT DIET DURING PREGNANCY AND LACTATION PROVOKESDEPRESSIVE-LIKE BEHAVIOR AND INFLUENCES THE IRISIN/BRAIN-DERIVEDNEUROTROPHIC FACTOR AXIS AND INFLAMMATORY FACTORSIN MALE AND FEMALE OFFSPRING IN RATS
IF: 2.544 Journal: Journal of Physiology and Pharmacology Cited Date: 2019-06-30
The effect of electrical stimulation of skeletal muscle on cardioprotection and on muscle-derived myokine levels in rats: A pilot study
IF: Journal: Physiology International Author: Department of Biochemistry, Albert Szent-Gy?rgyi Medical School, University of Szeged, H-6720 Szeged, Hungary Cited Date: 2023-06-09