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Human Plasmin
Native, biologically active whole molecule prepared by activation of purified plasminogen by streptokinase
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Proteins Synonyms: PLM, Fibrinolysin Biological Activity: Min. Activity (pre freeze/lyophilization): 15 units/mg protein Min. Activity (post lyophilization): 10 units/mg protein One unit is defined as the amount of enzyme that hydrolyzes one umole of tosyl-Gly-Pro-Lys-pNA per minute at 25°C, pH 7.8. Note: One unit=1.25 CU. Source: Human Plasma Purity: ≥ 90% by SDS-PAGE. Physical State: Lyophilized from 20 mM NaP04, pH 7.4, with 10 mg/ml D-Mannitol and 10 mg/ml NaCl. Manufacturer: |
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Athens Research & Technology
Produktdetails
Synonyms
PLM, Fibrinolysin
Description of Human Plasmin
Human Plasmin is a 81 kDa protein. Plasmin is a serine protease central to the breakdown of blood clots through fibrinolysis, where it degrades fibrin, the main structural component of clots1. Beyond its primary role in fibrinolysis, plasmin also participates in fibrinogenolysis, complement activation, tissue remodeling, and inflammation. It is synthesized in the liver as the inactive precursor plasminogen, which circulates in the blood and is activated at sites of clot formation by tissue plasminogen activator (tPA), urokinase, or therapeutically by streptokinase. Structurally, plasmin contains multiple domains, including kringle domains that facilitate binding to lysine residues on fibrin and cell surfaces, enhancing its targeting and activity. Functionally, plasmin not only dissolves clots but also activates collagenases, complement components (such as C1 and C5), and cleaves extracellular matrix proteins, contributing to processes like embryonic development, wound healing, and tumor invasion. Deficiencies or dysregulation of plasmin activity can lead to thrombosis or rare disorders such as plasminogen deficiency, which impairs wound healing and tissue repair. Clinically, plasmin and its activators are used as thrombolytic agents to treat conditions like myocardial infarction, stroke, and pulmonary embolism, and ongoing research explores engineered plasmin variants for safer, more targeted therapies.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
Biological Activity
Min. Activity (pre freeze/lyophilization): 15 units/mg protein Min. Activity (post lyophilization): 10 units/mg protein One unit is defined as the amount of enzyme that hydrolyzes one umole of tosyl-Gly-Pro-Lys-pNA per minute at 25°C, pH 7.8. Note: One unit=1.25 CU.
Storage
For long term, store Human Plasmin at ≤ -20°C.
Applications
In Vitro Diagnostics, Coagulation, Fibrinolysis, Complement System, Inflammation, Cancer, Stroke, Biotherapeutics, Cardiovasculsr Disease.
Citations/Publications
Ivanov, I., et al., (2019), 'A mechanism for hereditary angioedema with normal C1 inhibitor: an inhibitory regulatory role for the factor XII heavy chain', Blood. 133(10): pp 1152-1163. Available at: DOI10.1182/blood-2018-06-860270
Nikitin, D., et al., (2022), 'Computer-Aided Engineering of Staphylokinase Toward Enhanced Affinity and Selectivity for Plasmin', Computational and Structural Biotechnology Journal 20: pp 1366–1377. Available at: https://doi.org/10.1016/j.csbj.2022.03.004
Tivawala, R., et al., (2018), 'The Rheumatoid Arthritis-Associated Citrullinome', Cell Chemical Biology 25: pp 691–704. Available at: https://doi.org/10.1016/j.chembiol.2018.03.002
Tivawala, R., et al., (2021), 'The role of SERPIN citrullination in thrombosis', Cell Chemical Biology 28(12): pp 1728-1739.e5. Available at: doi: 10.1016/j.chembiol.2021.07.009.
Frombach, J., et al., (2020), 'Serine Protease-Mediated Cutaneous Inflammation: Characterization of an Ex Vivo Skin Model for the Assessment of Dexamethasone-Loaded Core Multishell-Nanocarriers', Pharmaceutics 12: pp 862. Available at: doi:10.3390/pharmaceutics12090862
Shipped with ice packs
Gel Scan of Human Plasmin
| Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
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