| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Fatty acid-binding protein, intestinal|Fatty acid-binding protein 2|Intestinal-type fatty acid-binding protein|I-FABP|FABP2|FABPI |
| 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 | |
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| Target | |
| UniProt # |
Background
rat IFABP/FABP2 (Intestinal Fatty Acid Binding Protein) is a molecular target commonly studied in signal transduction, cardiovascular, and developmental biology 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 IFABP/FABP2 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 IFABP/FABP2 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
IFABP/FABP2 (Intestinal Fatty Acid Binding Protein) may also be referenced as Fatty acid-binding protein, intestinal, Fatty acid-binding protein 2, and Intestinal-type fatty acid-binding protein 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 IFABP/FABP2 relates to vascular biology and endothelial function, cardiac remodeling and injury responses, thrombosis and hemostasis, and blood pressure regulation in signal transduction, cardiovascular, and developmental biology research.
- Interpreting shifts in IFABP/FABP2 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
IFABP/FABP2 has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with signal transduction, cardiovascular, and developmental biology 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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The efficacy and active compounds of Chaihuang Qingyi Huoxue granule to Ameliorate intestinal mucosal barrier injury in rats with severe acute pancreatitis by suppressing the HMGB1/TLR4/NF-κB signaling pathway
IF: 4.8 Journal: International Immunopharmacology Author: Research Center of Integrated Chinese and Western Medicine, The Affiliated Traditional Chinese Medicine Hospital, Southwest Medical University Luzhou, 646000, China. Cited Date: 2024-11-29
Lilrb4 ameliorates ileal injury in rats with hemorrhagic shock and suppresses the activation of NF-κB signaling pathway
IF: 4.2 Journal: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease Author: Department of General Surgery, Wuxi 9th People's Hospital Affiliated to Soochow University, Wuxi, Jiangsu 214000, People's Republic of China. Cited Date: 2024-07-12
Chac1 silencing mitigates hemorrhagic shock-induced intestinal injury by inhibiting oxidative stress and ferroptosis
IF: 1.1 Journal: Signa Vitae Author: Department of Critical Care Medicine, Wuxi 9th People’s Hospital Affiliated to Soochow University, 214000 Wuxi, Jiangsu, China Cited Date: 2023-12-29