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About This Item
UNSPSC Code:
12352204
NACRES:
NA.54
Product Name
Plasminogen, from human serum
biological source
human serum
form
lyophilized
specific activity
~11 units/mg protein (activated with streptokinase at 37 °C and pH 7.4 with Chromozym PL as the substrate.)
mol wt
90-94 kDa
packaging
pkg of 20 U
manufacturer/tradename
Roche
technique(s)
activity assay: suitable
application(s)
life science and biopharma
shipped in
wet ice
Quality Level
Analysis Note
Contaminants: <0.05% plasmin; the preparation does not contain 6-aminohexanoic acid
Application
Plasminogen is used for the determination of the activity of plasminogen activators. The enzyme is a substrate for tissue plasminogen activator (t-PA) in the t-PA test and a reference substance for t-PA therapy. It is used as the in-process control in the production of t-PA.
Features and Benefits
Contents
Lyophilizate, stabilized with bovine serum albumin.
Lyophilizate, stabilized with bovine serum albumin.
General description
Plasminogen is a profibrinolysin from human serum. Plasminogen, the proenzyme of the fibrinolytically active enzyme plasmin, is a single chain glycoprotein. Various isoelectric forms exist and can be separated by means of isoelectric focusing (IEF). The lyophilizate is stabilized with bovine serum albumin (BSA).
Other Notes
For life science research only. Not for use in diagnostic procedures.
Native plasminogen (glu-plasminogen) has a N-terminal glutamic acid group. Partial plasma proteolysis gives rise to a molecule with N-terminal lysine (lys-plasminogen). Cleavage with elastase results in val-plasminogen. The complete amino acid sequence contains 790 amino acids. Roche Applied Science supplies glu-plasminogen.
Preparation Note
Stabilizers: stabilized with BSA
Working solution: Solvent is recommended in 20 mM sodium phosphate buffer, pH 7.5, 100 mM NaCl.
Storage conditions (working solution): -15 to -25 °C
A solution in 20 mM sodium phosphate buffer, pH ca. 7.5, 100 mM NaCl is stable for several months without loss of activity when stored at -15 to -25 °C.
Note:
Plasminogen is susceptible to autolysis, which may result in activation. Contact with the skin or other contamination (e.g., by microorganisms), is therefore to be avoided.
Working solution: Solvent is recommended in 20 mM sodium phosphate buffer, pH 7.5, 100 mM NaCl.
Storage conditions (working solution): -15 to -25 °C
A solution in 20 mM sodium phosphate buffer, pH ca. 7.5, 100 mM NaCl is stable for several months without loss of activity when stored at -15 to -25 °C.
Note:
Plasminogen is susceptible to autolysis, which may result in activation. Contact with the skin or other contamination (e.g., by microorganisms), is therefore to be avoided.
Store at 2 to 8 °C. (Store dry!)
signalword
Warning
hcodes
pcodes
Hazard Classifications
STOT RE 2
Storage Class
11 - Combustible Solids
wgk
WGK 2
flash_point_f
does not flash
flash_point_c
does not flash
Regulatory Information
高风险级别生物产品--人源产品
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A Krüger et al.
Cancer gene therapy, 7(2), 292-299 (2000-04-19)
The serine protease urokinase-type plasminogen activator, uPA, when bound to its specific receptor, uPAR (CD87), plays a significant role in tumor cell invasion and metastasis. In breast cancer, enhanced uPA antigen in the primary tumor is correlated with poor prognosis
Andrea Schweinitz et al.
The Journal of biological chemistry, 279(32), 33613-33622 (2004-05-20)
The serine protease urokinase-type plasminogen activator (uPA) interacts with a specific receptor (uPAR) on the surface of various cell types, including tumor cells, and plays a crucial role in pericellular proteolysis. High levels of uPA and uPAR often correlate with
Claudine Ferland et al.
Journal of immunology (Baltimore, Md. : 1950), 173(7), 4417-4424 (2004-09-24)
Increased eosinophil counts are a major feature of asthmatic airways. Eosinophil recruitment requires migration through epithelium and tissue extracellular matrix by activation of proteases. We assessed the capacity of IL-16, a CD4(+) cell chemotactic factor, to induce migration of eosinophils
H Roger Lijnen
Biochemistry. Biokhimiia, 67(1), 92-98 (2002-02-14)
Several molecular interactions between the matrix metalloproteinase (MMP) and the plasminogen/plasmin (fibrinolytic) system may affect cellular fibrinolysis. MMP-3 (stromelysin-1) specifically hydrolyzes urokinase (u-PA), yielding a 17 kD NH2-terminal fragment containing the functionally intact receptor (u-PAR)-binding sequence and a 32 kD
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