| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Galectin-1|Gal-1|14 kDa laminin-binding protein|HLBP14|14 kDa lectin|Beta-galactoside-binding lectin L-14-I|Galaptin|HBL|HPL|Lactose-binding lectin 1|Lectin galactoside-binding soluble 1|Putative MAPK-activating protein PM12|S-Lac lectin 1|LGALS1 |
| 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 LGALS1 (Galectin-1) is a molecular target commonly studied in signal transduction, cardiovascular, and cell division and proliferation 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 LGALS1 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 LGALS1 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
LGALS1 (Galectin-1) may also be referenced as Galectin-1, Gal-1, and 14 kDa laminin-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 LGALS1 relates to vascular biology and endothelial function, cardiac remodeling and injury responses, thrombosis and hemostasis, and blood pressure regulation in signal transduction, cardiovascular, and cell division and proliferation research.
- Interpreting shifts in LGALS1 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
LGALS1 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 cell division and proliferation 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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