Human glu plasminogen

Manufactured by Prolytix

Sourced in United States

Human glu-plasminogen is a laboratory reagent used in the study of the fibrinolytic system. It is a precursor form of the enzyme plasmin, which plays a key role in the breakdown of blood clots. This product is intended for research use only and its function is to provide a source of the glu-plasminogen protein for experimental purposes.

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Lab products found in correlation

Urokinase plasminogen activator, by Merck Group (3 mentions) Horseradish peroxidase hrp conjugated immunoglobulins, by Agilent Technologies (3 mentions) Fibrinogen, by Merck Group (2 mentions) D val leu lys p nitroanilide dihydrochloride, by Merck Group (2 mentions) S 2251, by Merck Group (2 mentions) S2251, by Diapharma (1 mentions) Pro upa, by Abcam (1 mentions) H d val leu lys afc, by AnaSpec (1 mentions) Z gly gly arg amc, by Bachem (1 mentions) Mouse anti his antiserum, by GE Healthcare (1 mentions) Anti c5b 9 antibody, by Quidel (1 mentions) Factor h, by Complement Technology (1 mentions) Factor b, by Complement Technology (1 mentions) Human α thrombin, by Hyphen Biomed (1 mentions) Multiskan go spectrophotometer, by Thermo Fisher Scientific (1 mentions) Alteplase, by Boehringer Ingelheim (1 mentions)

6 protocols using human glu plasminogen

Plasminogen Activation by uPA Kinetics

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The ability of uPA to activate plasminogen was measured at 10 nM of uPA in PBS (pH 7.4) using human Glu-Plasminogen (Haematologic Technologies) and 0.5 mM of the plasmin-specific chromogenic substrate analog H–D–Val–Leu–Lys–pNA or S2251 (DiaPharma). The Glu–plasminogen concentration was varied from 0.5 μM to 10 μM. All the reaction components were preincubated at 37 °C for 10 min prior to mixing. The reaction was started by the addition of uPA, and the absorbance at 405 nm was monitored every 20 s for 10 min at 37 °C. The initial rates were calculated using the approach described (58 (link)) after determining the K_M and k_cat of plasmin for S2251 under our reaction conditions (K_M = 0.2 mM and k_cat = 13.7 s⁻¹):

Absorbance at 405 nm = (2.63 \times 10^{4} \frac{M}{s}) \frac{V_{\max} [Plasminogen]}{K_{M} + [Plasminogen]} t^{2}

The initial rates were obtained by plotting the absorbance at 405 nm divided by the conversion factor in brackets against the time squared. Initial rates were calculated from the first 3 min of the reaction.

Torres-Paris C., Chen Y., Xiao L., Song H.J., Chen P, & Komives E.A. (2023). The autoactivation of human single-chain urokinase-type plasminogen activator (uPA). The Journal of Biological Chemistry, 299(10), 105179.

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Plasmin Activity Quantification in E. faecalis

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Plasmin activity assays were performed as previously described with minor modifications^{18 (link)}. E. faecalis were grown overnight in tryptone yeast media. OD₆₀₀ was normalized by dilution to 0.1, and samples were diluted 10x in the final reaction. Bacteria were incubated with 250nM human glu-plasminogen (Haematologic technologies) with or without 10mM TXA (Fisher) for two hours at 37°C. A final concentration of 4nM uPA or pro-uPA (Biovision) were added and incubation proceeded for 20 minutes. A final concentration of 6μM plasmin-specific fluorogenic substrate (H-D-Val-Leu-Lys-AFC, AnaSpec) was added immediately prior to a 30-minute kinetic fluorescent read at 380/500nm. For assays of uPA activity, PLG was omitted and a substrate specific to uPA (Z-Gly-Gly-Arg-AMC, Bachem) was utilized. When assays were performed in human plasma, fluorescence was read for 120 minutes total. Plasmin or uPA activity is expressed as initial reaction velocity calculated from change in fluorescence over time during the initial phase of the reaction, when pseudo-first order kinetics determine the rate.

Jacobson R.A., Williamson A., Wienholts K., Gaines S., Hyoju S., van Goor H., Zaborin A., Shogan B.D., Zaborina O, & Alverdy J.C. (2021). Prevention of anastomotic leak via local application of tranexamic acid to target bacterial-mediated plasminogen activation: a practical solution to a complex problem.. Annals of surgery, 274(6), e1038-e1046.

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Plasmin Activation Assay Protocol

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Nguyen N.T., Röttgerding F., Devraj G., Lin Y.P., Koenigs A, & Kraiczy P. (2018). The Complement Binding and Inhibitory Protein CbiA of Borrelia miyamotoi Degrades Extracellular Matrix Components by Interacting with Plasmin(ogen). Frontiers in Cellular and Infection Microbiology, 8, 23.

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Plasmin Activation and Measurement

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Human glu-plasminogen was obtained from Haematologic Technologies (Essex Junction, VT, USA). Plasminogen was activated to plasmin using urokinase plasminogen activator (uPA) from Merck Millipore, Darmstadt, Germany. Both the chromogenic substrate S-2251 (D-Val-Leu-Lys p-nitroanilide dihydrochloride) and fibrinogen were purchased from Sigma-Aldrich (Steinheim, Germany). Purified C3b was obtained from Complement Technology, Tyler, TX, USA. A. baumannii Tuf was detected using a polyclonal rabbit antiserum raised against Streptococcus pneumoniae Tuf [29 (link)]. C3 and fibrinogen polyclonal antisera were purchased from Acris Antibodies (Herford, Germany). The monoclonal hexahistidine antibody was obtained from GE Healthcare (Munich, Germany). Horseradish peroxidase (HRP)-conjugated immunoglobulins were purchased from Dako (Hamburg, Germany) and Alexa Fluor 488-conjugated anti-rabbit immunoglobulins from Life Technologies (Darmstadt, Germany).

Koenigs A., Zipfel P.F, & Kraiczy P. (2015). Translation Elongation Factor Tuf of Acinetobacter baumannii Is a Plasminogen-Binding Protein. PLoS ONE, 10(7), e0134418.

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Plasminogen Activation and Complement Regulation

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Human serum (NHS) was collected from healthy blood donors as described previously^{50 (link)}. Human glu-plasminogen was purchased from Haematologic Technologies (Essex Junction, VT, USA) and urokinase plasminogen activator (uPA) (Merck, Darmstadt, Germany) were used for the activation of plasminogen to plasmin. The chromogenic substrate S-2251 (D-Val-Leu-Lys p-nitroanilide dihydrochloride) were from Sigma-Aldrich (Steinheim, Germany). Factor H, Factor B, C3b, and C5 were purchased from Complement Technology (Tyler, TX, USA). Polyclonal anti-plasminogen antibody was purchased from Acris Antibodies (Herford, Germany), and the monoclonal anti-plasminogen antibody (clone 10-V-1) was from Calbiochem, Merck, Darmstadt, Germany). The polyclonal anti-FH and anti-C3 antibody were obtained from Merck Biosciences (Bad Soden, Germany) and the polyclonal anti-C5, anti-Factor B antibody as well as the neoepitope-specific monoclonal anti-C5b-9 antibody was from Quidel (San Diego, CA, USA). The mouse anti-His antiserum was obtained from Novagen (Merck Darmstadt, Germany) and Qiagen (Hilden, Germany) and the horseradish peroxidase (HRP)-conjugated immunoglobulins were purchased from Dako (Hamburg, Germany).

Schmidt F.L., Sürth V., Berg T.K., Lin Y.P., Hovius J.W, & Kraiczy P. (2021). Interaction between Borrelia miyamotoi variable major proteins Vlp15/16 and Vlp18 with plasminogen and complement. Scientific Reports, 11, 4964.

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Fibrinogen Polymerization and Fibrinolysis Assay

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Fibrinogen polymerization was measured based on turbidity changes at 340 nm using a Thermo Scientific Multiskan GO spectrophotometer. The final concentrations of the sample and reagents in 100 μL of HBS buffer were as follows: 0.1-NIH U/mL human α-thrombin (Hyphen BioMed) or 0.1-U/mL batroxobin (Nuokang Bio-pharmaceutical), 1mM calcium chloride (CaCl₂) and 0.5-mg/mL fibrinogen purified from the proband and normal control. This mixture was incubated at 37 °C for 110 minutes. Three important parameters were calculated based on the change in turbidity with time: lag time, maximum slope (V_max), and final turbidity.
Fibrinolysis was examined by adding 80-μg/mL human Glu-plasminogen (Haematologic Technologies), 1mM CaCl₂, and 1.2nM recombinant human tissue plasminogen activator (Alteplase; Boehringer Ingelheim) to the fibrin clots formed in the polymerization experiment mentioned above. In particular, according to the results of clottability and polymerization, the fibrinogen concentration of the proband in the thrombin group was moderately increased (∼1.1 times, Supplementary Figure S1A) to ensure the same amount of fibrin clots involved in fibrinolysis progress. The change in optical density was monitored at 340 nm for 145 minutes, and the total lysis times were measured based on the curves. All experiments were performed in triplicates.

Li Y., Liang Q., Wu W., Hu X., Wang H., Wang X, & Ding Q. (2023). Fibrinogen BOE II: dysfibrinogenemia with bleeding and defective thrombin binding. Research and Practice in Thrombosis and Haemostasis, 7(5), 102145.

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