Western blot analysis of extracts from human liver and pancreas tissues using Plasminogen Antibody #12657 (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower).
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
For western blots, incubate membrane with diluted primary antibody in 5% w/v BSA, 1X TBS, 0.1% Tween® 20 at 4°C with gentle shaking, overnight.
NOTE: Please refer to primary antibody product webpage for recommended antibody dilution.
From sample preparation to detection, the reagents you need for your Western Blot are now in one convenient kit: #12957 Western Blotting Application Solutions Kit
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
Load 20 µl onto SDS-PAGE gel (10 cm x 10 cm).
NOTE: Volumes are for 10 cm x 10 cm (100 cm2) of membrane; for different sized membranes, adjust volumes accordingly.
* Avoid repeated exposure to skin.
posted June 2005
revised June 2020
Protocol Id: 10
Plasminogen Antibody recognizes endogenous levels of total plasminogen protein.
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).
Explore pathways + proteins related to this product.