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Plasminogen / PLG Human Protein

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SKU
BA522
Plasminogen / PLG human protein, 1 mg
Size:
1 mg
  $425.00
2 Weeks*
Bulk/Customize

Other products for "PLG or NM_000301"

Specifications
Specifications
Product Data
Species Human
Protein Source Plasma
Concentration lot specific
Purity >95% pure by SDS-PAGE
Presentation State Purified
Buffer Presentation State: Purified
State: Lyophilized purified fraction
Buffer System: 20 mM Tris, pH 7.5, containing 2 mM EDTA
Preservative: None
Bioactivity Specific: Activity : ≥ 120 units per mg protein.
One unit is defined as the amount of enzyme, which will hydrolyze 1 µmole of N-tosyl-L-arginine ester in 30 minutes at 37°C at pH 8.0.
Reconstitution Method Restore with 255 µl distilled water.
Preparation Lyophilized purified fraction
Protein Description Human Plasminogen.
Note Caution: All human source materials have tested non-reactive for HBsAg, and for anti-HCV, anti HBc and negative for HIV 1, HIV 2 antibodies. No test guarantees a product to be non-infectious. Therefore, all material derived from human fluids or tissues should be considered as potentially infectious.
Storage Upon receipt, store undiluted (in aliquots) at -20°C.
Avoid repeated freezing and thawing.
Stability Shelf life: one year from despatch.
Shipping Ambient
Reference Data
RefSeq NP_000292
Locus ID 5340
Cytogenetics 6q26
Synonyms HAE4
Summary 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. provided by RefSeq, May 2020
Protein Categories Cardiovascular diseases, Enzyme: Peptidases, Intracellular Proteins, Secreated Proteins
Protein Families Druggable Genome, Protease, Secreted Protein
Protein Pathways Complement and coagulation cascades, Neuroactive ligand-receptor interaction
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Documents
Resources

file-alt Citations

Fibrinolysis and proliferative endarteritis: two related processes in chronic infections? The model of the blood-borne pathogen Dirofilaria immitis
González-Miguel, Morchón, Siles-Lucas et al
PLoS One (2015) 10 (4), e0124445 DOI: 10.1371/journal.pone.0124445
Cited by 25
AI Summary: OriGene products, specifically the anti-ACT (TA328183) and anti-FBAL (TA319162) antibodies, were used in this study for ELISA, western blot, and immunofluorescence assays to detect and analyze the expression and localization of Dirofilaria immitis antigens involved in fibrinolysis and proliferative endarteritis.
FigureFigureFigure
Cloning and characterization of a plasminogen-binding enolase from the saliva of the argasid tick Ornithodoros moubata
Díaz-Martín, Manzano-Román, Oleaga et al
Vet Parasitol (2013) 191 (3-4), 301-14 DOI: 10.1016/j.vetpar.2012.09.019
Cited by 49
AI Summary: In this study, OriGene’s pCMV6-Entry vector was used for the cloning and recombinant expression of the O. moubata enolase gene, enabling functional characterization of the protein’s role in tick saliva.
Showing 1-2 of 2 papers.
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