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The formation of the recombinant plasmid by incorporating the gene encoding the Human PLG protein (274-560aa) into a plasmid vector initiates the generation of the recombinant Human PLG protein. Transforming the recombinant plasmid into e.coli cells and then selecting the positive e.coli cells based on their ability to survive in the presence of a specific antibiotic. The positive e.coli cells are cultured under conditions that stimulate the expression of the gene of interest. The protein is equipped with a N-terminal 6xHis tag. After expression, affinity purification is employed to isolate and purify the recombinant Human PLG protein from the cell lysate. Denaturing SDS-PAGE is utilized to resolve the resulting recombinant Human PLG protein, revealing a purity level exceeding 85%.
The formation of the recombinant plasmid by incorporating the gene encoding the Human PLG protein (274-560aa) into a plasmid vector initiates the generation of the recombinant Human PLG protein. Transforming the recombinant plasmid into e.coli cells and then selecting the positive e.coli cells based on their ability to survive in the presence of a specific antibiotic. The positive e.coli cells are cultured under conditions that stimulate the expression of the gene of interest. The protein is equipped with a N-terminal 6xHis tag. After expression, affinity purification is employed to isolate and purify the recombinant Human PLG protein from the cell lysate. Denaturing SDS-PAGE is utilized to resolve the resulting recombinant Human PLG protein, revealing a purity level exceeding 85%.
| Cat.No | ACP02628 | Target Name | PLG |
|---|---|---|---|
| Target Synonyms | Plasmin; Plasmin heavy chain A; Plasmin light chain B; Plasminogen; PLG; PLMN_HUMAN | Form | Liquid or Lyophilized powder |
| Expression System | E.coli | Expression Range | 274-560aa |
| Mol Weight | 36.0 kDa | Protein Length | Partial |
| Purity | Greater than 85% as determined by SDS-PAGE. | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P00747 |
|---|
Uniprot Id
P00747
Target Species
Human
Target Name
PLG
Target Full Name
Plasminogen
Target Function
Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.; Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo.
Target Involvement
Plasminogen deficiency (PLGD)
Target Subcellular Location
Secreted. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface.
Target Protein Families
Peptidase S1 family, Plasminogen subfamily
Target Tissue Specificity
Present in plasma and many other extracellular fluids. It is synthesized in the liver.
Target Research Area
Others
Target Synonyms
Plasmin; Plasmin heavy chain A; Plasmin light chain B; Plasminogen; PLG; PLMN_HUMAN
Target Background
The plasminogen protein encoded by this gene is a serine protease that circulates in blood plasma as an inactive zymogen and is converted to the active protease, plasmin, by several plasminogen activators such as tissue plasminogen activator (tPA), urokinase plasminogen activator (uPA), kallikrein, and factor XII (Hageman factor). The conversion of plasminogen to plasmin involves the cleavage of the peptide bond between Arg-561 and Val-562. Plasmin cleavage also releases the angiostatin protein which inhibits angiogenesis. Plasmin degrades many blood plasma proteins, including fibrin-containing blood clots. As a serine protease, plasmin cleaves many products in addition to fibrin such as fibronectin, thrombospondin, laminin, and von Willebrand factor. Plasmin is inactivated by proteins such as alpha-2-macroglobulin and alpha-2-antiplasmin in addition to inhibitors of the various plasminogen activators. Plasminogen also interacts with plasminogen receptors which results in the retention of plasmin on cell surfaces and in plasmin-induced cell signaling. The localization of plasminogen on cell surfaces plays a role in the degradation of extracellular matrices, cell migration, inflamation, wound healing, oncogenesis, metastasis, myogenesis, muscle regeneration, neurite outgrowth, and fibrinolysis. This protein may also play a role in acute respiratory distress syndrome (ARDS) which, in part, is caused by enhanced clot formation and the suppression of fibrinolysis. Compared to other mammals, the cluster of plasminogen-like genes to which this gene belongs has been rearranged in catarrhine primates.
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