Product Pathways - Adhesion
Plasminogen Antibody #12657
|12657S||100 µl (10 western blots)||---||In Stock||---|
|12657||carrier free and custom formulation / quantity||email request|
Already purchased this product? Write a Review.
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
Plasminogen Antibody recognizes endogenous levels of total plasminogen protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro132 of human plasminogen protein. Antibodies are purified by protein A and peptide affinity chromatography.
Plasminogen is the inactive, proenzyme precursor to the serine protease plasmin that degrades fibrin within blood clots, promotes cell migration through proteolytic degradation of extracellular matrix proteins, and regulates angiogenesis and wound healing through activation of matrix metalloproteases (1-4). Inactive plasminogen is produced and secreted by liver cells and is found in the circulatory system and extracellular fluids (1). The plasminogen protein is composed of an amino terminal preactivation peptide followed by five kringle domains and a serine proteinase domain (5). The plasminogen zymogen binds to sites on the cell surface and is subsequently cleaved to release the active serine proteinase plasmin. Identified plasminogen cell surface receptors (including S100A10, enolase and PLGRKT) share carboxy-terminal lysine residues that interact with plasminogen kringle domains, resulting in cell surface localization of plasminogen (6-8). Cleavage of plasminogen can be catalyzed by a number of distinct enzymes, including tissue specific plasminogen activator (tPA), urokinase plasminogen activator (uPA), and kallikrein (1). An additional plasminogen cleavage product is the angiogenesis inhibitor angiostatin, which is derived from the first four kringle domains (9). A number of related angiogenesis inhibitors, derived from various parts of the plasminogen kringle region, have been shown to inhibit endothelial cell growth and proliferation (10). Mutations in the corresponding PLG gene have been linked to plasminogen deficiencies, characterized by decreased plasmin expression and ligneous conjunctivitis in some individuals (11).
- Plow, E.F. et al. (1995) FASEB J 9, 939-45.
- Creemers, E. et al. (2000) Am J Pathol 156, 1865-73.
- Gong, Y. et al. (2008) J Clin Invest 118, 3012-24.
- Gong, Y. and Hoover-Plow, J. (2012) J Biomed Biotechnol 2012, 437920.
- Petersen, T.E. et al. (1990) J Biol Chem 265, 6104-11.
- Miles, L.A. et al. (2005) Front Biosci 10, 1754-62.
- Lighvani, S. et al. (2011) Blood 118, 5622-30.
- Ceruti, P. et al. (2013) Exp Hematol Oncol 2, 12.
- O'Reilly, M.S. et al. (1994) Cell 79, 315-28.
- Nguyen, T.M. et al. (2007) Blood 109, 4793-802.
- Mehta, R. and Shapiro, A.D. (2008) Haemophilia 14, 1261-8.
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.