Platelets were imaged in vivo using anti‐CD42 antibodies conjugated with Dylight 488 (Emfret Analytics, Eibelstad, Germany). Fibrin was detected in vivo using a mouse anti‐human fibrin monoclonal antibody (clone 59D8), labelled with Alexa 647, that cross‐reacts with mouse fibrin but not fibrinogen 17 . Full‐length tPA was from Boehringer Ingelheim, Ingelheimam Rhein, Germany. Antithrombin‐III, α‐thrombin, human α2‐antiplasmin and human plasmin were from Haematologic Technologies, Essex Junction, USA. PN‐1 was a gift from Denis Monard, Friedrich Mischer Institute, Basel, Switzerland. Aprotinin was purchased from Fischer Scientific, Pittsburgh, USA. The chromogenic substrate H‐d‐pyroglutamyl‐Gly‐l‐Arg‐p‐nitroanilide (S‐2444) and Gly‐Arg‐p‐nitroanilide were from Chromogenix Instrumentation Laboratories, Milan, Italy and Sigma‐Aldrich, St. Louis, USA respectively. Human blood was collected in citrated tubes from healthy donors who were informed about the objectives of the study. Platelet‐rich plasma was prepared by centrifugation at 100 × g for 10 min at room temperature. Aliquots of platelet‐rich plasma were centrifuged at 1500 × g for 10 min to obtain platelet‐poor plasma and the supernatant plasma was centrifuged at 11,000 × g for 5 min to obtain platelet‐free plasma.
Human plasmin
Manufactured by Prolytix
Sourced in United States
Human plasmin is a serine protease enzyme that plays a key role in the breakdown of blood clots. It is a core component of the fibrinolytic system, responsible for the dissolution of fibrin, the main structural protein in blood clots.
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3 protocols using human plasmin
1
In vivo Imaging of Platelets and Fibrin
2
Plasmin-Mediated Clot Degradation
3
Synthesis and Functionalization of CdSe/CdS/ZnS Quantum Dots
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CdSe/CdS/ZnS QDs with peak photoluminescence (PL) at ∼630 nm were synthesized using standard hot-solvent methods. (30, 31) The as-synthesized hydrophobic QDs were transferred to aqueous solution through ligand exchange with DHLA, (32, 33) GSH, (34) PEG-appended DHLA (DHLAâ€"PEG), (35, 36) or SB-appended DHLA (DHLAâ€"SB), (37-40) as described in the Supporting Information. Peptides were from Bio-Synthesis Inc. (Lewisville, TX, USA), and their sequences are listed in the Supporting Information. Alexa Fluor 647 (A647) C2 maleimide dye was from Life Technologies (Carlsbad, CA, USA). Buffers were prepared with water purified by a Barnstead Nanopure water purification system (Thermo Scientific, Ottawa, ON, Canada) and sterilized by autoclaving prior to use. Buffers included borate buffer (50 mM and pH 8.5), phosphate-buffered saline (12 mM phosphate, 137 mM NaCl, 2.7 mM KCl, and pH 7.4) and standard Trisâ€"borateâ€"ethylenediaminetetraacetic acid (EDTA) (TBE; 89 mM Tris, 89 mM boric acid, and 2 mM EDTA) buffer or Trisâ€"borate (TB) buffer (no EDTA) for gel electrophoresis. Bovine trypsin was from Sigma-Aldrich (Oakville, ON, Canada). Human α-thrombin and human plasmin were from Haematologic Technologies (Essex Junction, VT, USA). Additional materials are listed in the Supporting Information.
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