P1867
Plasmin from human plasma
lyophilized powder, ≥2.0 units/mg protein
Synonym(s):
Fibrinolysin
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About This Item
Recommended Products
form
lyophilized powder
Quality Level
specific activity
≥2.0 units/mg protein
impurities
HIV, Hepatitis B and Hepatitis C, tested negative
UniProt accession no.
application(s)
diagnostic assay manufacturing
storage temp.
−20°C
Gene Information
human ... PLG(5340)
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General description
Plasmin functions as a key enzyme of the fibrinolytic cascade, and is also important in inflammation processes.
Application
A complex between plasmin and an inhibitor has been isolated in a study via affinity chromatography from urokinase-activated human plasma. It has also been used in a study to investigate activation of human epithelial sodium channel (ENaC) by plasmin and chymotrypsin.
Biochem/physiol Actions
It is inhibited by α 2-antiplasmin and its interaction with fibrin is blocked. It digests the N-terminal region of the cytoplasmic protein αsynuclein preventing its uptake by surrounding cells.
Plasmin exhibits preferential cleavage at the carboxyl side of lysine and arginine residues with higher selectivity than trypsin. Converts polymerized fibrin into soluble products.
pH Optimum: 8.5
pH 7.5: ~40% of maximal activity, pH 9.5: ~50% of maximal activity
Temperature Optimum: 37 °C with rapid inactivation at 56 °C
pH Optimum: 8.5
pH 7.5: ~40% of maximal activity, pH 9.5: ~50% of maximal activity
Temperature Optimum: 37 °C with rapid inactivation at 56 °C
Packaging
Package size based on protein content
Unit Definition
One unit will produce one μmole of p-Nitroanilide from D-Val-Leu-Lys-p-Nitroanilide per minute at pH 7.5 at 37 °C.
Physical form
Lyophilized powder containing sodium phosphate, mannitol, and NaCl.
Disclaimer
RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Silke Haerteis et al.
The Journal of general physiology, 140(4), 375-389 (2012-09-12)
Proteolytic activation of the epithelial sodium channel (ENaC) involves cleavage of its γ subunit in a critical region targeted by several proteases. Our aim was to identify cleavage sites in this region that are functionally important for activation of human
Tatiana Syrovets et al.
Journal of leukocyte biology, 92(3), 509-519 (2012-05-09)
The serine protease plasmin generated from its zymogen plasminogen is best known for its function as a key enzyme of the fibrinolytic cascade. However, beyond fibrinolysis, plasmin has a number of crucial functions in a variety of processes, including inflammation.
S Müllertz et al.
The Biochemical journal, 159(3), 545-553 (1976-12-01)
A complex between plasmin and an inhibitor was isolated by affinity chromatography from urokinase-activated human plasma. The complex did not react with antibodies against any of the known proteinase inhibitors in plasma. A rabbit antiserum against the complex was produced.
On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin.
B Wiman et al.
The Journal of biological chemistry, 254(18), 9291-9297 (1979-09-25)
Shu He et al.
British journal of haematology, 160(6), 806-816 (2013-01-31)
To assess whether Haemocomplettan(®) (fibrinogen concentrate) or Fibrogammin(®) (Factor XIII concentrate) can be used to manage bleeding complications of antithrombotic treatment, we examined a normal plasma pool spiked with AR-H067637 (thrombin inhibitor) or rivaroxaban (activated factor X-inhibitor), to which one
Protocols
Protocol for Enzymatic Assay of Plasmin with D-Val-Leu-Lys-p-Nitroanilide Dihydrochloride
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