| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Urokinase-type plasminogen activator|U-plasminogen activator|uPA|Urokinase-type plasminogen activator long chain A|Urokinase-type plasminogen activator short chain A|Urokinase-type plasminogen activator chain B|PLAU |
| 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
mouse PLAU/Upa (Urokinase-Type Plasminogen Activator) is a molecular target commonly studied in immunology, cardiovascular, and signal transduction research. Enzymes contribute to cellular physiology through catalytic activity that supports metabolism, nucleic-acid processing, or signaling.
Biological role and mechanism
The biological role of PLAU/Upa 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 PLAU/Upa 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
PLAU/Upa (Urokinase-Type Plasminogen Activator) may also be referenced as Urokinase-type plasminogen activator, U-plasminogen activator, and uPA 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 PLAU/Upa relates to innate and adaptive immune responses, cytokine signaling networks, host–pathogen interactions, and immune cell activation and trafficking in immunology, cardiovascular, and signal transduction research.
- Interpreting shifts in PLAU/Upa 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
PLAU/Upa has been investigated across diverse physiological and disease contexts, and changes in its abundance have been reported in areas aligned with immunology, cardiovascular, 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.
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.
Early host–parasite interaction models reveal a key role for fibrinolysis in intestinal migration
IF: 3.5 Journal: Parasites & Vectors Author: Laboratory of Helminth Parasites of Zoonotic Importance (ATENEA), Institute of Natural Resources and Agrobiology of Salamanca (IRNASA-CSIC), Salamanca, Spain. Cited Date: 2025-10-17
γ-bungarotoxin impairs the vascular endothelial barrier function by inhibiting integrin α5
IF: 3.5 Journal: Toxicology Letters Author: Department of Physiology and Pathophysiology, College of Medicine, Yanbian University, Yanji 133002, Jilin, PR China Cited Date: 2023-07-07