R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
uPA (E2M6I) Rabbit mAb #15800
Filter:
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 32, 50 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
uPA (E2M6I) Rabbit mAb recognizes endogenous levels of total uPA protein. The antibody detects the 50 kDa zymogen and the 32 kDa chain B, and does not detect chain A.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser266 of human uPA protein.
Background
uPA (PLAU, urokinase-type plasminogen activator) is a secreted serine protease that plays an important role in plasminogen activation (1). uPA exists as a secreted 50 kDa inactive zymogen. Upon binding to its high affinity serine protease urokinase-type plasminogen activator receptor (uPAR), it is processed to two interlinked chains, 18 kDa chain A and 32 kDa chain B, and becomes activated to convert plasminogen to its active form, plasmin, in a spatially restricted manner on the cell surface (2). Plasmin then carries out its protease activity toward a wide range of substrates. uPA activity is inhibited by serpins (serine protease inhibitors), such as plasminogen activator inhibitor (PAI) (3). uPA, uPAR, and PAI form a Urokinase Plasminogen Activation System (uPAS) (4). This system plays a key role in regulating a broad range of biological processes under normal physiological conditions, such as tissue wound healing (5), cell migration (6), fibrinolysis (7), and angiogenesis (8). The system also contributes to disease progression, such as cancer development (9), neurodegeneration disorders (10), inflammatory lung disease, and rheumatoid arthritis (11,12).
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- Mahmood, N. et al. (2018) Front Oncol 8, 24.
- Fay, W.P. et al. (1997) Blood 90, 204-8.
- Ismail, A.A. et al. (2021) Int J Mol Sci 23, 337. doi: 10.3390/ijms23010337.
- Yepes, M. (2022) Neural Regen Res 17, 2404-2406.
- Reichel, C.A. et al. (2012) Trends Cardiovasc Med 22, 192-6.
- Medcalf, R.L. (2017) J Thromb Haemost 15, 2089-2098.
- Montuori, N. and Ragno, P. (2014) Chem Immunol Allergy 99, 105-22.
- Madunić, J. (2018) Thromb Haemost 118, 2020-2036.
- Yepes, M. et al. (2021) Int J Mol Sci 22, 4380. doi: 10.3390/ijms22094380.
- Schuliga, M. et al. (2013) Curr Opin Pharmacol 13, 386-93.
- Buckley, B.J. et al. (2019) Curr Drug Targets 20, 970-981.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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