10602370001
Roche
Plasmin, bovine
from bovine plasma
Synonyme(s) :
Plasmin
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About This Item
Produits recommandés
Source biologique
bovine plasma
Forme
suspension
Activité spécifique
≥2 units/mg protein (At 25 °C with Chromozym PL as the substrate.)
Poids mol.
Mr ~85 kDa
Conditionnement
pkg of 1 mL (5 U)
Fabricant/nom de marque
Roche
pH optimal
8.9
Conditions d'expédition
wet ice
Température de stockage
2-8°C
Description générale
Plasmin is derived from the proteolytic cleavage of its precursor plasminogen. Human Plasmin is made up of two polypeptide chains. The polypeptide chains are connected via disulfide bridges.
Spécificité
Serine endopeptidase that hydrolyzes peptide and ester bonds at the carboxylic side of Lys or Arg; more selective than trypsin.
Application
Plasmin from bovine has been used as a standard for assessing plasmin biosensors and for proteolytic assays.
Actions biochimiques/physiologiques
Plasmin plays an important role in proteolysis and fibrinolysis. It possesses inflammatory activity. Plasmin is also involved in the hydrolysis of peptide bonds following arginine or lysine. It also cleaves hormones like glucagon, thrombopoietin and growth hormones. Plasmin plays a role in cleavage of complement factors like C3 and C5, coagulation factors V and VIII, matrix proteins, growth factors, E-cadherins and metalloproteinase.
Forme physique
Suspension in 3.2 M ammonium sulfate solution
Autres remarques
For life science research only. Not for use in diagnostic procedures.
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
does not flash
Point d'éclair (°C)
does not flash
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Les clients ont également consulté
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Rath M and Pauling L
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Plasmin as a proinflammatory cell activator
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Journal of Leukocyte Biology, 92(3), 509-519 (2012)
A rapid and sensitive biosensor for measuring plasmin activity in milk
Dacres H, et al.
Sensors and Actuators B, Chemical, 301, 127141-127141 (2019)
Primary structure of the B-chain of human plasmin
WIMAN B.
European Journal of Biochemistry, 76(1), 129-137 (1977)
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