| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | FN|Fibronectin|FN1|CIG|ED-B|FINC|FNZ|GFND|GFND2|LETS|MSF|Cold-insoluble globulin|CIG) |
| 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
human FN1 (Fibronectin) is a molecular target commonly studied in stem cells, cancer, and signal transduction 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 FN1 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 FN1 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
FN1 (Fibronectin) may also be referenced as FN, Fibronectin, and FN1 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 FN1 relates to tumor microenvironment biology, cell proliferation and apoptosis, metastasis and invasion pathways, and angiogenesis and immune-oncology mechanisms in stem cells, cancer, and signal transduction research.
- Interpreting shifts in FN1 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
FN1 has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with stem cells, cancer, and signal transduction 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.
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Enhancing Vasculogenesis in Dental Pulp Development: DPSCs-ECs Communication via FN1-ITGA5 Signaling
IF: 4.8 Journal: Stem Cell Reviews and Reports Author: State Key Laboratory of Oral & Maxillofacial Reconstruction and Regeneration, National Clinical Research Center for Oral Diseases, Shaanxi Clinical Research Center for Oral Diseases, Department of Pediatric Dentistry, School of Stomatology, The Fourth Mil Cited Date: 2024-03-08
Analysis of alterations of serum inflammatory cytokines and fibrosis makers in patients with essential hypertension and left ventricular hypertrophy and the risk factors
IF: 4.06 Journal: American Journal of Translational Research Cited Date: 2022-07-07
A novel serum protein biomarker for the late-stage diagnosis of nasopharyngeal carcinoma
IF: 3.4 Journal: BMC Cancer Author: Department of Laboratory Medicine, The Eighth Affiliated Hospital, Sun Yat-Sen University, Shenzhen, 518033, China. Cited Date: 2025-04-11
A comparative proteomic analysis for non-invasive early prediction of hypoxic-ischemic injury in asphyxiated neonates
IF: Journal: Research Square Cited Date: 2023-03-24