Human plasmin

Manufactured by Enzyme Research

Sourced in United States

Human plasmin is a proteolytic enzyme that plays a central role in the fibrinolytic system, responsible for the breakdown of blood clots. It is a serine protease derived from the precursor molecule plasminogen.

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5 protocols using human plasmin

Plasminogen and tPA Treatment Effects

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Cells were treated at DIV14 with either 100 nM Human Glu-plasminogen (Enzyme Research Laboratories, HPg 2001), 200 nM Human Plasmin (Enzyme Research Laboratories, HPlasmin), or 10 nM or 200 nM Human tPA (Actilyse®, Boehringer Ingelheim) for 24 h.

Lépine M., Douceau S., Devienne G., Prunotto P., Lenoir S., Regnauld C., Pouettre E., Piquet J., Lebouvier L., Hommet Y., Maubert E., Agin V., Lambolez B., Cauli B., Ali C, & Vivien D. (2022). Parvalbumin interneuron-derived tissue-type plasminogen activator shapes perineuronal net structure. BMC Biology, 20, 218.

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Microfluidic Fibrinolysis Assay

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Fibrinolysis was assessed for neonatal and adult human and porcine samples. A custom microfluidics based assay adapted from Brown et al. was utilized to analyze degradation rates for all sample groups^{17 (link),18 (link)}. A polydimethylsiloxane (Dow Corning, USA) device consisting of a clot reservoir with a perpendicular lying channel was constructed via casting in an acrylic mold. After curing for 24 hours, the device was plasma treated and bonded to a glass slide to create a sealed channel. Clots were formed from plasma and 10% Alexa-Flour 488–labeled adult fibrinogen was added for visualization. Polymerization was initiated with the addition of 0.5 U/ml of thrombin, and 25 μl of the clot solution was immediately injected into the clot reservoir. After polymerizing for two hours, the device was mounted on an EVOS FL Auto microscope (Life Technologies, USA) for imaging. A plasmin solution (0.01 mg/ml plasmin in HEPES buffer) (Human Plasmin, Enzyme Research Laboratories, USA) was injected into a channel inlet, and the clot was imaged every 10 min for 12 hours. ImageJ (National Institutes of Health, USA) was used to determine rate of clot degradation by comparing the first and final images and measuring distance along a perpendicular line to the clot boundary. Clot degradation rates were expressed as the distance the clot boundary traveled divided by 12 hours.

Nellenbach K.A., Nandi S., Kyu A., Sivadanam S., Guzzetta N.A, & Brown A.C. (2020). A Comparison of Neonatal and Adult Fibrin Clot Properties Between Porcine and Human Plasma. Anesthesiology, 132(5), 1091-1101.

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Quantifying Growth Factor Release from Hydrogels

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To assess the ability to release growth factors, 50 uL HS (250 mM NaCl) and PS (145 mM NaCl) gels (10 mg/mL fibrinogen) were fabricated with 100 ng/mL FGF-2 (Peprotech, 100-18b) and 100 ng/mL VEGF-165 (Shenandoah Biotechnology, 100–44) in the bottom of 1.6 mL Eppendorf tubes. To fabricate these gels, a PBS solution of 400 ng/mL FGF-2 and 400 ng/mL VEGF-165 was used instead of the normal 4X cell solution in Step 3 of Section 2.1 above. After gelation, 1 mL of 0.5% protease-free BSA (Sigma, A3059) in PBS was added to each tube and was completely replaced daily. After 0, 1, and 7 days, the supernatant was removed and 50 uL of 0.2 mg/mL human plasmin (Enzyme Research Laboratories) in HEPES buffer (pH 8.5, Boston Bioproducts) was added. Fibrin degradation occurred overnight at 37°C. Growth factor retention was measured using ELISAs (Peprotech, 900-K08 and 900-K10) and a BioTek Synergy 2 luminescent plate reader (Gen5 software).

Jarrell D.K., Vanderslice E.J., Lennon M.L., Lyons A.C., VeDepo M.C, & Jacot J.G. (2021). Increasing salinity of fibrinogen solvent generates stable fibrin hydrogels for cell delivery or tissue engineering. PLoS ONE, 16(5), e0239242.

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Fabricating Dual-Crosslinked Fibrin-Tetronic Hydrogels

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Tetronic® 904 (T904) was generously donated by BASF (Florham Park, NJ). Human fibrinogen (FgN), human alpha thrombin, and human plasmin were purchased from Enzyme Research Laboratories (South Bend, IN). T904 was reacted with acryloyl chloride as previously described (Cho et al., 2012 (link)) and 91% acrylation was determined by ¹H-NMR. Varying compositions of T904/fibrin hybrid hydrogels were prepared by dual enzymatic and Michael-type addition crosslinking (Figure 1). Fibrinogen (FgN) was first reduced by mixing for 1 hour with varying amounts of DTT required to give a final 1:1 acrylate:thiol ratio within the hydrogel. Lyophilized polyplex or pGFP was reconstituted in a solution of T904-acrylate, 2.5 mM CaCl₂, and 0.1U thrombin in 20 mM sodium citrate buffer. The reduced FgN/DTT solution was added to the acrylated T904 solution, mixed by gentle micropipetting, and 25 μL aliquots (2.5 μg DNA/gel) added to decapitated 1 mL syringes or 12 well plates. Samples were incubated at room temperature for 2 hours followed by 37°C for 2 hours for crosslinking.

Zhang J., Sen A., Cho E., Lee J.S, & Webb K. (2014). Poloxamine/fibrin hybrid hydrogels for nonviral gene delivery. Journal of tissue engineering and regenerative medicine, 11(1), 246-255.

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PLGA-based Biomaterial Fabrication

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Poly(lactic-co-glycolic) acid (PLGA; 50:50 ester-terminated; inherent viscosity = 0.55-0.75dL/g) was purchased from Lactel (Birmingham, USA). Recombinant mouse stromal cell-derived factor-1 α (SDF-1α) were acquired from PeproTech (Rocky Hill, USA). B27 growth supplement, DAPI nuclear stain, tetramethylbenzidine (TMB) substrate and Dulbecco's modified eagle medium were acquired from Life Technologies (Carlsbad, USA). Glucose was obtained from Acros Organics (Geel, Belgium). High-binding 96-well enzyme-linked immunosorbent assay (ELISA) plates were acquired from Greiner Bio-One (Frickenhausen, Germany). The organic solvent ethyl acetate was acquired from Alfa Aesar (Ward Hill, USA) and dimethyl sulfoxide (DMSO) from American bioanalytical (Natick, USA). Human fibrinogen (Plasminogen, von Willebrand Factor and Fibronectin Depleted), human α-thrombin, human factor XIIIa (FXIII) and human plasmin were acquired from Enzyme Research Laboratories (South Bend, USA). All other materials and chemicals were purchased from Sigma-Aldrich (St. Louis, USA) and used without further modification or purification.

Dutta D., Fauer C., Mulleneux H.L, & Stabenfeldt S.E. (2015). Tunable Controlled Release of Bioactive SDF-1α via Protein Specific Interactions within Fibrin/Nanoparticle Composites. Journal of materials chemistry. B, Materials for biology and medicine, 3(40), 7963-7973.

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