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Heparin Lyase

Heparin Lyase is an enzyme that cleaves heparin, a highly sulfated glycosaminoglycan found in mast cells.
This enzyme is used in research to analyze the structure and function of heparin, a key component of the extracellular matrix.
Heparin Lyase has applications in the development of anticoagulant therapies and the study of heparin-protein interactions.
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Most cited protocols related to «Heparin Lyase»

1
Quantitative Determination of Glycosaminoglycans
Cited 10 times
Urine samples were defrosted at 4 °C and mixed well using a vortex mixer. A 400-μL aliquot of each sample was desalted by passing through a 3 kDa molecule weight cutoff (MWCO) spin column and washed twice with distilled water. A series of urine samples were also prepared for method validation by adding aqueous solutions containing varying amounts of standard CS and HS affording final concentrations of 50–500 ng/mL.
The casing tubes were replaced before 150 μL of digestion buffer (50 mM ammonium acetate containing 2 mM calcium chloride adjusted to pH 7.0) was added to the filter unit. Recombinant heparin lyase I, II, III (pH optima 7.0–7.5) and recombinant chondroitin lyase ABC (10 mU each, pH optimum 7.4) were added to each sample and mixed well. The samples were all placed in a water bath at 37 °C for 2 h, after which enzymatic digestion was terminated by removing the enzymes by centrifugation. Under these reaction conditions, these lyases could completely depolymerize their GAG substrates (in amounts of over 100 μg) into products containing each class of GAG disaccharides. The filter unit was washed twice with 100 μL distilled water and the filtrates, containing the disaccharide products, were dried via vacuum centrifuge and stored at –20 °C.
The dried samples were AMAC-labeled by adding 10 μL of 0.1 M AMAC in DMSO/acetic acid (17/3,V/V) incubating at room temperature for 10 min, followed by adding 10 μL of 1 M aqueous NaBH3CN and incubating for 1 h at 45 °C. A mixture containing all 17-disaccharide standards prepared at 1250 ng/mL was similarly AMAC-labeled and used for each run as an external standard. After the AMAC-labeling reaction, the samples were centrifuged and each supernatant was recovered and an equal volume of DMSO:acetic acid:distilled water (17:3:20) was added to each. Samples were stored in a light-resistant container at room temperature until analyzed via LC-MS/MS.
Sun X., Li L., Overdier K.H., Ammons L.A., Douglas I.S., Burlew C.C., Zhang F., Schmidt E.P., Chi L, & Linhardt R.J. (2015). Analysis of Total Human Urinary Glycosaminoglycan Disaccharides by Liquid Chromatography–Tandem Mass Spectrometry. Analytical chemistry, 87(12), 6220-6227.
Publication 2015
Acetic Acid Adjustment Disorders ammonium acetate Bath Buffers Calcium chloride Centrifugation Chondroitin Digestion Disaccharides Enzymes Heparin Lyase Light Lyase Sulfoxide, Dimethyl Tandem Mass Spectrometry Urine Vacuum
2
Multistep Glycan and Protein Extraction
Cited 9 times
Aligned digestion spots were chosen on six serial sections of both fresh frozen and fixed mouse liver and mouse caudate putamen slides (each 10 μm thick). First, five cycles of hyaluronidase enzyme solution (0.16 TRU/μL hyaluronidase in the presence of 2 M ammonium acetate and 10% glycerol) was applied on the chosen spots. The resulting HA disaccharides were extracted four times by 0.3% ammonium hydroxide solution and the slides were dried at 55 °C for 5 min, which was followed by 20 min incubation at 37 °C with 50 mM ammonium bicarbonate. Next, five cycles of chondroitinase ABC (1 milliunits/μL) enzyme solution was added. To minimize the amount of salt in the enzyme solution, the 5 mM Tris buffer was replaced by 25 mM ammonium bicarbonate buffer and 10% glycerol was also added to minimize diffusion. The resulting CS disaccharides were extracted as the HA disaccharides and the slide was dried at 55 °C for 5 min, which was followed by 20 min incubation with 25 mM ammonium bicarbonate at 37 °C. Next, five cycles of heparin lyase I, II and III mixture was added. The solution contained 1.66 mU/μL of heparin lyase I, 0.33 mU/μL of herparin lyase II and 0.33 mU/μL of heparin lyase III in the presence of 2.5 mM calcium hydroxide, 12.5 mM ammonium bicarbonate and 10% glycerol. The resulting HS disaccharides were extracted as the HA and CS disaccharides and the slide was dried at 55 °C for 5 min, which was followed by 20 min incubation with 50 mM ammonium bicarbonate at 37 °C. Next, a solution containing 10 mM DTT, 0.1% RapiGest and 10% glycerol was applied on the chosen spots and the tissue slide was incubated at 55 °C for 20 min. This was followed by addition of a solution containing 20 mM iodoacetamide, 25 mM ammonium bicarbonate and 10% glycerol and the tissue slide was placed in a darkbox for 20 min at room temperature. Next, five cycles of trypsin enzyme solution (100 ng/μL) in the presence of 10% glycerol were added to achieve digestion of proteins. Samples were then incubated with aprotinin (2 μg/μL) at 37 °C for 45 min to stop trypsin activity. Finally, five cycles of PNGase F (500,000 units/mL) were added. The peptides and glycans were extracted by 10% acetic acid and separated by C18 spin column. Samples were loaded in 5% ACN/0.1%FA, the flow-through and wash fraction contained the N-glycans, while peptides were released first by 40% ACN 0.1% FA then by 60% ACN 0.1% FA, combined and dried under vacuum. Individual cycles consisted of microwave irradiation for 10 min (for CS, HS and proteins, 270 W; for HA, 540 W) except for N-glycans where incubation took place in an incubator (37 °C, 40 min/cycle). Subsequent LC-MS methods and data interpretation can be found in the Supporting Information along with a table summarizing the experiments performed (Table S-1, Supporting Information).
Turiák L., Shao C., Meng L., Khatri K., Leymarie N., Wang Q., Pantazopoulos H., Leon D.R, & Zaia J. (2014). Workflow for Combined Proteomics and Glycomics Profiling from Histological Tissues. Analytical chemistry, 86(19), 9670-9678.
Publication 2014
Acetic Acid ammonium acetate ammonium bicarbonate Ammonium Hydroxide Aprotinin Buffers Chondroitin ABC Lyase Diffusion Digestion Disaccharides Enzymes Exanthema F 500 Frozen Sections Glycerin Glycopeptidase F heparinase III Heparin Lyase Hyaluronidase Hydroxide, Calcium Iodoacetamide Liver Lyase Mice, House Microwaves Neostriatum Peptides Polysaccharides Protein Digestion Proteins Sodium Chloride Tissues Tromethamine Trypsin Vacuum
3
Efficient Cardiac Differentiation of hPSCs
Cited 8 times
When hPSCs had grown to 80%–90% confluence 2–3 days after plating, the medium was changed from E8 to differentiation basal medium, which contains E8 basal medium (DMEM/F‐12, l‐ascorbic acid, selenium, transferrin, and NaHCO3) 14, 1× Chemically Defined Lipid Concentrate (100×, catalog no. 11905‐031; Thermo Fisher Scientific Life Sciences) and 1× penicillin‐streptomycin (catalog no. 15140‐122; Thermo Fisher Scientific Life Sciences). The day was defined as day 0. CHIR99021 (5 μM, catalog no. 4423; Tocris Bioscience, Avonmouth, Bristol, UK, https://www.tocris.com) was added to the differentiation basal medium at day 0 for 24 hours. IWP2 (3 μM, catalog no. 3533; Tocris Bioscience) was added from day 2 to day 5. Heparin was added to the medium at the indicated dosages and times. Insulin (20 μg/ml, catalog no. I9278; Sigma‐Aldrich, St. Louis, MO, http://www.sigmaaldrich.com) was added to differentiation basal medium to maintain cardiomyocytes from day 7 onward. The medium was changed daily until day 7, but changed every 2–3 days from day 7 onward. The growth factors, inhibitors, and enzymes used in culture were as follows: activin A (10 ng/ml, catalog no. 338‐AC/CF; R&D Systems, Minneapolis, MN, https://www.rndsystems.com), BMP4 (10 ng/ml, catalog no. 314‐BP/CF; R&D Systems), fibroblast growth factor 2 (FGF2; 100 ng/ml, catalog no. 100‐18B; Peprotech, Rocky Hill, NJ, https://www.peprotech.com), transforming growth factor β (TGFβ) 1 (1.74 ng/ml, catalog no. 240‐B/CF; R&D), dorsomorphin (3 μM, catalog no. 04‐0024; Stemgent, Lexington, MA, https://www.stemgent.com), LDN‐193189 (0.1 μM, catalog no. 04‐0074; Stemgent), PD0325901 (1 μM, catalog no. 04‐0008; Stemgent), SB431542 (3 μM, catalog no. s1067; Selleckchem, Houston, TX, http://www.selleckchem.com), heparin (catalog no. H3149; Sigma‐Aldrich), heparinase I (catalog no. P0735S; New England Biolabs, Ipswich, MA, https://www.neb.com).
Lin Y., Linask K.L., Mallon B., Johnson K., Klein M., Beers J., Xie W., Du Y., Liu C., Lai Y., Zou J., Haigney M., Yang H., Rao M, & Chen G. (2016). Heparin Promotes Cardiac Differentiation of Human Pluripotent Stem Cells in Chemically Defined Albumin‐Free Medium, Enabling Consistent Manufacture of Cardiomyocytes. Stem Cells Translational Medicine, 6(2), 527-538.
Publication 2016
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide activin A Ascorbic Acid Bicarbonate, Sodium Bone Morphogenetic Protein 4 Chir 99021 dorsomorphin Enzymes Fibroblast Growth Factor 2 Growth Factor Heparin Heparin Lyase inhibitors Insulin LDN 193189 Lipids Myocytes, Cardiac PD-0325901 Penicillins Selenium Streptomycin TGF-beta1 Transferrin
4
Plasma miRNA Expression Profiling
Cited 8 times
Taqman MicroRNA Assays were used to do expression profiling of the plasma miRNAs of interest. All reagents, primers and probes were obtained from Applied Biosystems (Applied Biosystems, Foster City, CA). 10 ng of DNAse and Heparinase treated plasma RNA for each sample was used for the individual assays in 15 μl reactions containing RT mixture and Taqman primer mix. The mix was incubated at 16°C for 30 min, 42°C for 60 min, and 85°C for 5 min. miRNA expression levels were quantified using the ABI prim 7900 HT Sequence detection system (Applied Biosystems). For the purpose, 15 μl reverse transcription (RT) reaction was diluted with 30μl of water and 11.25 μl of the diluted RT product was mixed with 12.5 μl of 2 x Taqman PCR mixture, 1.25 μl Taqman primer and probe mixture in a final volume of 25ul. Real time PCR was performed in triplicate, including no-template controls. Relative expression of the mature miRNAs was calculated utilizing the comparative CT (2−ΔΔCT) method (26 (link)) with miRNA-16 as the endogenous control to normalize the data (27 (link)). The cycle threshold (CT) is defined as the number of cycles required for the FAM signal to cross the threshold in real time PCR. ΔCT was calculated by subtracting the CT values of miR-16 from the CT values of the miRNA of interest. ΔΔCT was then calculated by subtracting mean ΔCT of the control samples from ΔCT of tested samples. Fold change of miRNA was calculated by the equation 2−ΔΔCT.
Wang J., Chen J., Chang P., LeBlanc A., Li D., Abbruzzesse J.L., Frazier M.L., Killary A.M, & Sen S. (2009). MicroRNAs in Plasma of Pancreatic Ductal Adenocarcinoma Patients as Novel Blood Based Biomarkers of Disease. Cancer prevention research (Philadelphia, Pa.), 2(9), 807-813.
Publication 2009
Biological Assay Deoxyribonuclease I Heparin Lyase MicroRNAs Oligonucleotide Primers Plasma Real-Time Polymerase Chain Reaction Reverse Transcription
5
Nanomechanical Characterization of Endothelial Glycocalyx
Cited 7 times
Thickness and stiffness of the eGC were determined using the Atomic Force Microscope (AFM) nanoindentation technique. Preservation of the endothelial cell layer on aorta preparations was approved by immunostaining of PECAM-1/CD31 (Figure 1). Figure 2 A, B illustrates the basic principles of this method. By using a Multimode AFM (Veeco, Mannheim, Germany) with a feedback-controlled heating device (Veeco) measurements were performed at 37°C as described previously [29 (link)].
In brief, the central component of the AFM is a very sensitive mechanical nanosensor – a triangular cantilever with a mounted spherical tip (here: electrically uncharged polystyrene, diameter = 10 µm, Novascan, Ames, IA, USA) that is utilized to periodically indent the cells. A spherical tip was used for this AFM approach instead of a sharp tip because of a larger interaction area between tip and sample that decreases the effective pressure and results in less mechanical noise [30 (link)]. The cantilever functions as a soft spring (spring constant = 11 pN/nm). The xyz-position of the tip is precisely controlled by a piezo-element (Figure 2 A). A laser beam is reflected by the gold-coated backside of the cantilever to a position-sensitive quadrupled photodiode allowing measurements of the cantilever deflection (V). Determination of the spring constant (Kcant) by the thermal tuning method and measurement of the deflection sensitivity (α) of the cantilever on bare glass coverslips facilitate the calculation of the force (F) acting on the cantilever and, in turn, the force exerted by the cantilever to the sample.
Since the piezo displacement (xpiezo) and the deflection sensitivity (α) are known, the indentation depth (deformation) of the sample (xsample) can be calculated.
For reasons of readability the indentation depth is hereafter called “thickness”. It should be noted that the indentation depth rather represents an apparent thickness, rather than the exact anatomical thickness.
Force indentation curves of a single cell were obtained by plotting the force (F) necessary to indent the cell (indentation depth, xsample). The sample stiffness can be derived from Hook´s law.
The stiffness (K) is the mechanical resistance of a sample against a defined deformation (e.g. indentation). K depends strongly on the indentation depth and the location, because cells contain a variety of substructures and organelles. The experimental parameters including an indentation velocity of 1 µm/s, a loading force of approximately 400 pN, an indentation frequency in the range of 0.25 - 0.5 Hz, a ramp size of 2 µm, a trig threshold of 35 nm and a tip velocity of 0.5 - 1 µm/s.
Previous experiments, using 1 µm AFM-tips, showed that the glycocalyx thickness is somewhat variable [29 (link),31 (link)]. Since we were interested in the overall condition of the glycocalyx and especially in its changes induced by different stimuli, we here chose larger tips (10 µm), as they indent a larger area. Thus they provided “more averaged” results and enabled us to avoid the data being influenced by the spatial distribution of the eGC thickness. All measurements were performed in HEPES-buffered solution [standard composition in millimolars: 140 NaCl, 5 KCl, 1 MgCl2, 1 CaCl2, 5 Glucose, 10 HEPES (N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid), pH 7.4] supplemented with 1% FCS in order to prevent eGC collapse [32 (link)].
Light microscopy was used to ensure that the tip position of the mechanical nanosensor was located neither at the nuclear, nor at the junctional region of cultured endothelial cells. However, this approach was not feasible in (thick) explanted aortas due to the lack of transparency of sub-endothelial layers such as the Tunica media and T. externa.
Figure 3 A, B show typical force indentation curves of an untreated as well as heparinase-treated aortic endothelial cell (“overview mode”). Each force indentation curve was then analyzed separately with a higher magnification (“working mode”) by using a linear approximation for determination of the eGC nanomechanics (Figure 3 C).
Wiesinger A., Peters W., Chappell D., Kentrup D., Reuter S., Pavenstädt H., Oberleithner H, & Kümpers P. (2013). Nanomechanics of the Endothelial Glycocalyx in Experimental Sepsis. PLoS ONE, 8(11), e80905.
Publication 2013
Aorta Biologic Preservation CD31 Antigens Cells Cultured Cells Electricity Endothelial Cells Endothelium Glucose Glycocalyx Gold Heparin Lyase HEPES Hypersensitivity Light Microscopy Magnesium Chloride Medical Devices Microscopy, Atomic Force Mineralocorticoid Excess Syndrome, Apparent Organelles Polystyrenes Pressure Shock Sodium Chloride Tunica Media Van der Woude syndrome

Most recents protocols related to «Heparin Lyase»

1
Pulmonary Endarterectomy Under Deep Hypothermia
PEA was performed from median sternotomy, the patient was cooled to 18°C to 20°C using cardiopulmonary bypass (CBP), and bilateral PEA was performed under deep hypothermic circulatory arrest. Unfractionated heparin (Leo Pharmaceutical Products, Denmark) was used for intraoperative anticoagulation monitored by activated clotting time (ACT) (target > 480 s Kaolin-ACT, Medtronic.Inc. ACTII, Minneapolis, MN, USA). Before the initiation of CBP, 500 to 1000 ml of blood was harvested, and returned to the patient after weaning off CPB, heparin reversal by protamine sulfate, and decannulation. During CPB to maintain patients’ volume status and to minimize the use of crystalloids (plasmalyte 50 mg/ml, Baxter) and possible volume overload autologous blood transfusion (cell saver), allogenic red blood cell (RBC) transfusions (Hb < 60 g/l), 2 to 6 units of solvent-detergent treated standardized plasma (Octaplas®, Octapharma AG, Lachen, Switzerland) or albumin 20% were used. Tranexamic acid was used 30 mg/kg intravenously before the surgical incision and again 15 mg/kg every 2 h for the duration of CPB. ACT was controlled every 20 min on CPB and 3 min after each heparin bolus. After CPB, administration of protamine and harvested blood infusion, coagulation status was controlled (heparinase-ACT, complete blood count, APTT, PT, fibrinogen, AT and D-dimer). Postoperatively in the operation room allogenic RBC were transfused if Hb < 90 g/l or Hct < 30%. The threshold for platelet transfusion was the platelet count <100 ×109/l and for standardized plasma, Octaplas®, PT < 30%.
Myllylahti L., Ropponen J., Lax M., Lassila R, & Nykänen A.I. (2023). Upregulation of Coagulation Factor VIII and Fibrinogen After Pulmonary Endarterectomy in Patients with Chronic Thromboembolic Pulmonary Hypertension. Clinical and Applied Thrombosis/Hemostasis, 29, 10760296231158369.
Publication 2023
Activated Partial Thromboplastin Time Albumins BLOOD Blood Transfusion, Autologous Cardiopulmonary Bypass Cells Circulatory Arrest, Deep Hypothermia Induced Complete Blood Count Detergents Erythrocytes fibrin fragment D Fibrinogen Heparin Heparin Lyase Kaolin Median Sternotomy Patients Pharmaceutical Preparations Plasma Plasmalyte A Platelet Counts, Blood Platelet Transfusion Protamines Red Blood Cell Transfusion Solutions, Crystalloid Solvents Sulfate, Protamine Surgical Wound Tranexamic Acid
2
Quantification of Cardiac Tissue GAGs
At the time of tissue harvesting around 200 mg of left ventricular tissue from healthy and peri-infarct areas on d7 and d28 post-NSTEMI were snap-frozen to be processed to extract total sulfated GAGs. First, dried-powdered samples were weighed and suspended in a buffer to a final concentration of 25 mg of tissue/ml. Tissue digestion was performed by incubating the tissue suspension with proteinase K (PK, 50 μg/ml, Sigma-Aldrich, USA) at 56 °C O/N. After enzymatic inactivation at 90 °C for 30 min, Dnase (7.5 U/ml, Qiagen, Germany) was added and samples were incubated O/N. Lipid elimination was performed by chloroform extraction45 (link). After GAGs dialysis, 1,9-dimethylmethylene blue (DMMB) assay was used to quantify GAGs. HS and CS quantities were determined by incubating digested samples with a cocktail of heparinases78 (link) (Iduron, UK). Specifically, chondroitinase ABC (25 mU/sample, 2 h at 37 °C) was used for specific CS elimination. The absence of a significant abundance of other GAGs in tissue samples was checked by combining both heparinases and chondroitinases.
Contessotto P., Spelat R., Ferro F., Vysockas V., Krivickienė A., Jin C., Chantepie S., Chinello C., Pauza A.G., Valente C., Rackauskas M., Casara A., Zigmantaitė V., Magni F., Papy-Garcia D., Karlsson N.G., Ereminienė E., Pandit A, & Da Costa M. (2023). Reproducing extracellular matrix adverse remodelling of non-ST myocardial infarction in a large animal model. Nature Communications, 14, 995.
Publication 2023
Biological Assay Buffers Chloroform Chondroitin ABC Lyase Chondroitinases Deoxyribonucleases Dialysis Digestion dimethylmethylene blue Endopeptidase K Enzymes Freezing Heparin Lyase Infarction Left Ventricles Lipids Non-ST Elevated Myocardial Infarction Tissues
3
Glycosylation Profiling and SARS-CoV-2 Spike Protein Binding
Cells treated with compounds or DMSO control were stained with biotinylated lectins (Vector Laboratories) (VVA, PNA 0.2 μg/mL; Pan-Lectenz, 2,3-Lectenz, GSL II, PHA-L, GNL, DSL, RCAI, ECL, LCA, PHA-E, WGA 1 μg/mL) or mouse mAbs to Tn (1E3)44 (link),99 (link), Tn-MUC1 (5E5)65 (link), FXYD5 (6C5 and NCC-MC53)64 (link) diluted 1:5000 in PBA (PBS with 1% (w/v) BSA) for 1 h at 4 °C. For SARS-CoV-2 spike protein binding, NSC80997, DMSO control or Heparinase mix (2.5 mU/mL HSase II, and 5 mU/mL HSase III; IBEX) treated cells were incubated with recombinant SARS-CoV-2 biotinylated spike protein S1/S2 (20 µg/mL) for 30 min at 4 °C. Spike protein was produced and biotinylated as previously described71 (link). Cells were washed with PBA and incubated with streptavidin conjugated to Alexa Fluor 488 or 647 (Invitrogen), FITC-conjugated rabbit anti-mouse immunoglobulins (Dako), or Goat anti-mouse IgG, Alexa Flour 488 (Invitrogen) diluted 1:2000 in PBA, respectively. Cells were washed twice and resuspended in PBA and analyzed using a SA3800 spectral analyzer running the SA3800 software (SONY) or a FACSCalibur instrument running BDFACStation software (BD Bioscience). Cells were gated to exclude dead cells and doublets (Supplementary Fig. 4B) and data was analyzed using FlowJo software (FlowJo, LCC).
Sørensen D.M., Büll C., Madsen T.D., Lira-Navarrete E., Clausen T.M., Clark A.E., Garretson A.F., Karlsson R., Pijnenborg J.F., Yin X., Miller R.L., Chanda S.K., Boltje T.J., Schjoldager K.T., Vakhrushev S.Y., Halim A., Esko J.D., Carlin A.F., Hurtado-Guerrero R., Weigert R., Clausen H, & Narimatsu Y. (2023). Identification of global inhibitors of cellular glycosylation. Nature Communications, 14, 948.
Publication 2023
alexa fluor 488 anti-IgG Antibodies, Anti-Idiotypic Cells Cloning Vectors erythroagglutinating phytohemagglutinin Flour Fluorescein-5-isothiocyanate Goat Heparin Lyase Lectin Monoclonal Antibodies M protein, multiple myeloma MUC1 protein, human Mus PHA-L Pseudo-Hurler Polydystrophy Rabbits SARS-CoV-2 spike protein, SARS-CoV-2 Streptavidin Sulfoxide, Dimethyl Type II Mucolipidosis
4
Automated Thrombin Generation Assay
TG was measured using a commercially available fluorogenic assay kit (Technothrombin®, Vienna, Austria) on a fully automated coagulation analyser (Ceveron®, Alpha, Technoclone, Vienna, Austria). Blood was drawn in citrated tubes, centrifuged in 3000 rpm for 10 min to obtain platelet poor plasma and kept at -70 degrees Celsius until analysis. Samples were thawed and hepzyme (Dade® Hepzyme® freeze-dried preparation of purified bacterial heparinase I > 125 IU/ml with added stabilizers) was added to T0 samples in order to remove heparin. TG was then initiated through the addition of tissue factor 0.3 pmol/L and phospholipids 3 pmol/L. The concentration of thrombin was measured with a fluorescent peptide substrate, which is cleaved by thrombin to release a fluorophore. The rate of thrombin generation is measured over time resulting in a thrombin formation curve. The following parameters of thrombin activity were recorded: (a) lag time until thrombin generation initiation (minutes); (b) peak thrombin generation – the maximal concentration of thrombin formed (nM); (c) time to peak thrombin generated (minutes); (d) endogenous thrombin potential (ETP) which equals the area under the curve (AUC) and represents the total amount of thrombin generated (nM) [21 ].
Wiessman M., Kheifets M., Schamroth Pravda N., Leshem Lev D., Ziv E., Kornowski R., Spectre G, & Perl L. (2023). Thrombogenicity and endothelial progenitor cells function during Acute myocardial infarction - comparison of Prasugrel versus Ticagrelor. Journal of Thrombosis and Thrombolysis, 55(3), 407-414.
Publication 2023
3,3'-diallyldiethylstilbestrol Bacteria Biological Assay BLOOD Blood Platelets Coagulation, Blood Freezing Heparin Heparin Lyase Peptides Phospholipids Plasma Thrombin Thromboplastin Times, Reptilase
5
Plasma cDNA Extraction and Quantification
Blood samples were collected in heparinized tubes before 2017 or EDTA tubes after 2017, and processed within two hours after collection with one centrifugation at 2000 g (10 min) at 4 °C before storage at -20 °C. cDNA was retrospectively extracted from 200 to 1700 μL of plasma using a QIAamp® Circulating Nucleic Acid Kit (Qiagen, Hilden, Germany). Double-stranded DNA quantification was performed by a fluorimetric method using a Quant-iT™ ds DNA HS Kit (ThermoFisher Scientific, Waltham, MA, USA).
4 ng of cDNA was preamplified with 12 cycles for heparin plasma and 9 cycles for EDTA plasma using 12.5 μL TaqMan Universal PCR Master Mix (Applied Biosystems) for heparin and 12.5 μL Q5 Hot Start High Fidelity Master Mix (New England Biolabs) for EDTA, respectively. Heparin plasma cDNA was treated with 2 μL of heparinase I bactericide beforehand to improve mutational detection by ddPCR.
Drouyer A., Beaussire L., Jorda P., Leheurteur M., Guillemet C., Berghian A., Georgescu D., Di Fiore F., Perdrix A, & Clatot F. (2023). Clinical relevance of circulating ESR1 mutations during endocrine therapy for advanced hormone-dependent endometrial carcinoma. BMC Cancer, 23, 1061.
Publication 2023
BLOOD Cell-Free Nucleic Acids Centrifugation DNA, Complementary DNA, Double-Stranded Edetic Acid Fluorometry Heparin Heparin Lyase Mutation Plasma

Top products related to «Heparin Lyase»

1
Heparinase 1 by Merck Group
Sourced in United States, United Kingdom
Heparinase I is a laboratory enzyme used for the degradation of heparin. It functions by cleaving specific glycosidic bonds within the heparin molecule.
2
Chondroitinase abc by Merck Group
Sourced in United States, Germany, Canada, Hungary, United Kingdom, Sweden
Chondroitinase ABC is a bacterial enzyme that catalyzes the breakdown of chondroitin sulfate, a type of glycosaminoglycan found in the extracellular matrix of many tissues. It is commonly used in research applications to study the role of chondroitin sulfate in various biological processes.
3
Heparin by Merck Group
Sourced in United States, Germany, United Kingdom, Italy, France, Canada, China, Japan, Israel, Switzerland, Australia, Macao, Sweden, Sao Tome and Principe, Spain, Netherlands, Brazil, Austria, Poland
Heparin is a pharmaceutical product manufactured by Merck Group. It is a naturally occurring anticoagulant, primarily used as a laboratory reagent to prevent the clotting of blood samples.
4
Heparinase by Merck Group
Sourced in United States
Heparinase is a laboratory reagent used to break down heparin, a naturally occurring anticoagulant. It is commonly used in clinical and research settings to facilitate various analytical procedures involving heparin-containing samples.
5
Heparinase 3 by Merck Group
Sourced in United States
Heparinase III is a laboratory reagent that is used for the enzymatic degradation of heparin. It is a protein-based enzyme that specifically cleaves heparin, a common anticoagulant, into smaller fragments. The primary function of Heparinase III is to facilitate the analysis and characterization of heparin and heparin-related molecules in various research and diagnostic applications.
6
Hyaluronidase by Merck Group
Sourced in United States, Germany, Switzerland, United Kingdom, Japan, China, Italy, France, Macao, Israel, Australia, Sao Tome and Principe, Canada, Spain, Netherlands, Czechia
Hyaluronidase is an enzyme used in laboratory settings. It functions by breaking down hyaluronic acid, a component of the extracellular matrix.
7
Heparinase 2 by Merck Group
Sourced in United States
Heparinase II is a laboratory enzyme used for the cleavage of heparin and heparan sulfate. It is a useful tool for the characterization and analysis of these glycosaminoglycans.
8
Teg 5000 thrombelastograph hemostasis analyzer system by Haemonetics
Sourced in United States
The TEG® 5000 Thrombelastograph® Hemostasis Analyzer System is a laboratory instrument used to assess a patient's hemostatic (blood clotting) function. It measures the viscoelastic properties of blood and provides information about the dynamics of clot formation and dissolution.
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Heparinase 1 3 by Merck Group
Sourced in United States
Heparinase I/III is a laboratory enzyme used to degrade heparin, a naturally occurring anticoagulant. It is commonly used in research and analytical settings to facilitate the measurement of heparin and related compounds.
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Acetic acid by Merck Group
Sourced in United States, Germany, United Kingdom, Italy, India, China, France, Spain, Switzerland, Poland, Sao Tome and Principe, Australia, Canada, Ireland, Czechia, Brazil, Sweden, Belgium, Japan, Hungary, Mexico, Malaysia, Macao, Portugal, Netherlands, Finland, Romania, Thailand, Argentina, Singapore, Egypt, Austria, New Zealand, Bangladesh
Acetic acid is a colorless, vinegar-like liquid chemical compound. It is a commonly used laboratory reagent with the molecular formula CH3COOH. Acetic acid serves as a solvent, a pH adjuster, and a reactant in various chemical processes.

More about "Heparin Lyase"

Heparin Lyase, also known as Heparinase or Heparinase I, is a versatile enzyme that plays a crucial role in the analysis and research of heparin, a highly sulfated glycosaminoglycan found in mast cells.
This enzyme is widely used in various applications, from the development of anticoagulant therapies to the study of heparin-protein interactions.
Heparin Lyase is capable of cleaving heparin, a key component of the extracellular matrix, allowing researchers to investigate its structure and function.
This enzyme is particularly valuable in the field of heparin research, as it provides a powerful tool for analyzing the complex molecular composition and properties of this crucial biomolecule.
Chondroitinase ABC, another related enzyme, can also be employed in conjunction with Heparin Lyase to further expand the scope of glycosaminoglycan research.
The combination of these enzymes enables a more comprehensive understanding of the intricate interactions between different types of glycosaminoglycans and their roles in various biological processes.
Heparinase, Heparinase II, and Heparinase III are additional variants of the Heparin Lyase enzyme, each with its own unique characteristics and applications.
These enzymes can be utilized to study the diverse aspects of heparin-related phenomena, such as its involvement in anticoagulation, inflammation, and cell signaling.
Hyaluronidase, an enzyme that degrades hyaluronic acid, another important glycosaminoglycan, can also be employed in conjunction with Heparin Lyase to explore the interplay between different extracellular matrix components.
The TEG® 5000 Thrombelastograph® Hemostasis Analyzer System is a specialized instrument that can be used in conjunction with Heparin Lyase to assess the effects of heparin on blood coagulation, ultimately contributing to the development of more effective anticoagulant therapies.
PubCompare.ai's AI-driven platform offers seamless access to the most reliable Heparin Lyase protocols, empowering researchers to locate the best methods from literature, preprints, and patents.
This innovative solution enhances reproducibility and optimizes the research process, providing researchers with the tools they need to unlock the full potential of Heparin Lyase and related enzymes.