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10874477001

Roche

Plasminogen

from human serum

Synonym(s):

plasminogen

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About This Item

UNSPSC Code:
12352204

biological source

human serum

Quality Level

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

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).

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.

Quality

Contaminants: <0.05% plasmin; the preparation does not contain 6-aminohexanoic acid

Sequence

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.

Storage and Stability

Store at 2 to 8 °C. (Store dry!)

Other Notes

For life science research only. Not for use in diagnostic procedures.

Pictograms

Health hazard

Signal Word

Warning

Hazard Statements

Precautionary Statements

Hazard Classifications

STOT RE 2

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

does not flash

Flash Point(C)

does not flash


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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
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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