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6-Aminocaproic Acid

6-Aminocaproic Acid is a synthetic amino acid that has been used in medical treatments to prevent excessive bleeding and blood loss.
It works by inhibiting the breakdown of fibrin, a key protein involved in blood clotting.
This molecule has been studied for its potential applications in surgery, traumatic injury, and other conditions where controlling hemorrhage is crucial.
Researchers can optimize their studies on 6-Aminocaproic Acid by utilizing PubCompare.ai's AI-driven protocol comparison tool, which helps identify the most effective research strategies from the literature, preprints, and patents.
Thhis cutting-edge technology can take your 6-Aminocaproic Acid research to new heights.

Most cited protocols related to «6-Aminocaproic Acid»

1
Reconstitution of LIL3.2 from Arabidopsis
Reconstitution assays were performed based on protocols as described [4 (link), 5 (link), 9 (link)]. For both LIL3.1 and LIL3.2 isoforms from Arabidopsis thaliana, very similar results were obtained [10 (link)]. Based on the higher purification yield only experimental work with LIL3.2 is shown here. In brief; LIL3 inclusion bodies (30 μM) were solubilized in a reaction buffer containing 100 mM Tris pH 11, 5 mM 6-aminocaproic acid, 1 mM benzamidine and 12.5% sucrose and n-Dodecyl β-d-maltoside (DDM) at a final concentration of 6 mM DDM respectively. 100 mM DTT and 6 μM Chl a (solubilized in diethyl ether/Ethanol 1:1) were added prior to heating samples to 100 °C for 1 min followed by a 2-h incubation at RT in the dark.
Mork-Jansson A.E, & Eichacker L.A. (2019). A strategy to characterize chlorophyll protein interaction in LIL3. Plant Methods, 15, 1.
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Publication 2019
6-Aminocaproic Acid Arabidopsis thalianas benzamidine Biological Assay Buffers Ethanol Ethyl Ether Inclusion Bodies Protein Isoforms Sucrose Tromethamine
2
Engineered Muscle Tissue Myobundles
Myobundles were formed by modifying our previously published methods for engineered rodent muscle tissues (Hinds et al., 2011 (link); Juhas et al., 2014 (link)) (Figure 1—figure supplement 2). Expanded myogenic cells were dissociated in 0.025% trypsin-EDTA to a single cell suspension and encapsulated in a fibrinogen (Akron, Boca Raton, FL) and matrigel solution on laser cut Cerex frames (9.2 × 9.5 mm outer dimensions, 6.8 × 8.3 mm inner dimensions) within PDMS molds (cast from Teflon masters and pretreated with pluronic) at 15 × 106 cells/ml (7.5 × 105 cells per myobundle). Specifically, a cell solution (7.5 × 105 cells in 17.2 µl media per bundle + 2 µl of 50 unit/ml thrombin in 0.1% BSA in PBS [Sigma, St. Louis, MO]) and a gelling solution (11 µl media + 10 µl Matrigel + 10 µl of 20 mg/ml Fibrinogen in DMEM) were prepared in separate vials on ice for up to six myobundles per vial. Gelling solution was added to the cell solution and mixed thoroughly then each bundle was individual pipetted within the PDMS mold and onto the frame. The cell/hydrogel mixture was polymerized for 30 min at 37°C followed by incubation in growth media containing 1.5 mg/ml 6-aminocaproic acid (ACA, Sigma). Myobundles were kept in growth media during gel compaction (3–5 days) and then switched to low glucose DMEM with 2% horse serum (Hyclone, Logan, UT), 2 mg/ml ACA and 10 µg/ml insulin (Sigma). Frames were removed from molds at the time of switch to low serum medium and cultured dynamically in suspension for an additional 1–4 weeks. Starting from a 50 mg donor biopsy, typical cell expansion for 5 passages can allow generation of at least 1000 myobundles with a total mass of >5 g, representing a >100-fold amplification of muscle mass when going from native to engineered tissue system.
All drugs were purchased from Sigma. Clenbuterol hydrochloride, chloroquine phosphate, and cerivastatin sodium salt hydrate were prepared at 1000× stock solutions in PBS (control) and sterile-filtered for use. Lovastatin was prepared as a 10,000× stock solution in DMSO in which case DMSO was used as vehicle control. Drugs studies in myobundles or 2D cultures were initiated after 1 week of differentiation. Myobundles were replenished with fresh media and drug each day to maintain drug concentration.
Madden L., Juhas M., Kraus W.E., Truskey G.A, & Bursac N. (2015). Bioengineered human myobundles mimic clinical responses of skeletal muscle to drugs. eLife, 4, e04885.
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Publication 2015
(Z)-2-amino-5-chlorobenzophenonamidinohydrazone acetate 6-Aminocaproic Acid Biopsy Brown Oculocutaneous Albinism CD3EAP protein, human Cells cerivastatin chloroquine phosphate Clenbuterol Dietary Supplements Edetic Acid Equus caballus Fibrinogen Fungus, Filamentous Glucose Homo sapiens Hydrogels Insulin Lovastatin matrigel Muscle Tissue Myogenesis Pharmaceutical Preparations Pluronics Reading Frames Rodent Serum Sodium Chloride Sodium Hydroxide Sterility, Reproductive Sulfoxide, Dimethyl Teflon Thrombin Tissue Donors Tissue Engineering Trypsin
3
Comprehensive Genomic Profiling of Esophageal Adenocarcinoma
379 cases (69%) of our EAC cohort were derived from the esophageal adenocarcinoma WGS ICGC study, for which samples are collected through the UK wide OCCAMS (Oesophageal Cancer Classification and Molecular Stratification) consortium. The procedures for obtaining the samples, quality control processes, extractions and whole genome sequencing are as previously described17 (link). Strict pathology consensus review was observed for these samples with a 70% cellularity requirement before inclusion. Comprehensive clinical information was available for the ICGC-OCCAMS cases (Supplementary Table 13). In addition, previously published samples were included in the analysis from Dulak et al.19 (link) (149 WES; 27%) and Nones et al.20 (22 WGS samples; 4%) to total 551 genome characterized EACs. RNA-seq data was available from our ICGC WGS samples (116/379). BAM files for all samples (include those from Dulak et al.19 (link) and Nones et al.20 ) were run through our alignment (BWA-MEM), mutation (Strelka), copy number (ASCAT) and structural variant (Manta) calling pipelines, as previously described17 (link). Our methods were benchmarked against various other available methods and have among the best sensitivity and specificity for variant calling (ICGC benchmarking exercise49 ,50 (link)). Cell lines were whole genome sequenced at 30X coverage with 150bp paired end reads on an Illumina Hiseq4000. Copy number calling was performed by Freec as previously described41 (link). Mutations were called by GATK as previously described41 (link), filtered for germline variants in the 1000 genomes project and any known oncogenic hotspots32 (link) were recovered. Amplifications were defined as genes with 2x the median copy number of the host chromosome or greater.
Total RNA was extracted using All Prep DNA/RNA kit from Qiagen, and the quality was checked on Agilent 2100 Bioanalyzer using RNA 6000 nano kit (Agilent). Qubit High sensitivity RNA assay kit from Thermo Fisher was used for quantification. Libraries were prepared from 250 ng RNA, using TruSeq Stranded Total RNA Library Prep Gold (Ribo-zero) kit, and ribosomal RNA (nuclear, cytoplasmic and mitochondrial rRNA) was depleted, whereby biotinylated probes selectively bind to ribosomal RNA molecules forming probe-rRNA hybrids. These hybrids were pulled down using magnetic beads and rRNA depleted total RNA was reverse transcribed. The libraries were prepared according to Illumina protocol51 (link). Paired end 75-bp sequencing on HiSeq4000 generated the paired end reads. For normal expression controls, we chose gastric cardia tissue, from which some hypothesize Barrett’s esophagus may arise, and duodenum which contains intestinal histology, including goblet cells, which mimics that of Barrett’s esophagus. We did not use Barrett’s esophagus tissue itself as a normal control given the heterogeneous and plentiful phenotypic and genomic changes that it undergoes early in its pathogenesis.
Frankell A.M., Jammula S., Li X., Contino G., Killcoyne S., Abbas S., Perner J., Bower L., Devonshire G., Ococks E., Grehan N., Mok J., O’Donovan M., MacRae S., Eldridge M.D., Tavaré S, & Fitzgerald R.C. (2019). The landscape of selection in 551 esophageal adenocarcinomas defines genomic biomarkers for the clinic. Nature genetics, 51(3), 506-516.
Publication 2018
6-Aminocaproic Acid Adenocarcinoma Of Esophagus Barrett Esophagus Biological Assay Cardia Cell Lines Chromosomes Cytoplasm DNA Library Duodenum Esophageal Cancer Genes Genetic Heterogeneity Genome Germ-Line Mutation Goblet Cells Gold Hybrids Hypersensitivity Inclusion Bodies Intestines Mitochondria Mutation Oncogenes pathogenesis Phenotype Ribosomal RNA RNA-Seq Strains Tissues
4
Ischemia Reperfusion Injury Treatment in Swine

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Publication 2014
6-Aminocaproic Acid Animals Animals, Laboratory Cardiac Conduction System Disease Cells Dental Occlusion Epicardium Fibrin Fibrinogen Fungus, Filamentous Heart Human Induced Pluripotent Stem Cells IGF1 protein, human Injuries Institutional Animal Care and Use Committees Ischemia Ligation Magnetic Resonance Spectroscopy Microspheres Myocardium Needles Neoplasm Metastasis Obstetric Delivery Operative Surgical Procedures Pigs Reperfusion Reperfusion Injury Rivers Therapies, Investigational Thrombin Ventricular Fibrillation Woman
5
Mitochondrial Isolation and Blue Native Electrophoresis
Mitochondria were isolated from mouse tissue using differential centrifugation as previously described (31 (link)). For blue native electrophoresis, 100 µg mitochondria were solubilized in solubilization buffer: 1% (w/v) digitonin (Calbiochem), 20 mM Tris, pH 7.4, 0.1 mM EDTA, 50 mM NaCl, 10% (v/v) glycerol. Following 15 min of incubation on ice, non-solubilized material was removed by centrifugation and the supernatant was mixed with loading dye (5% (w/v) Coomassie Brilliant Blue G-250 (Serva), 100 mM Tris pH 7, 500 mM 6-aminocaproic acid). Samples were resolved on 4–10% (w/v) acrylamide gradient BN-PAGE gels (50 (link)). BN gels were further subjected to western blot analysis or Coomassie Brilliant Blue R staining as indicated.
Milenkovic D., Matic S., Kühl I., Ruzzenente B., Freyer C., Jemt E., Park C.B., Falkenberg M, & Larsson N.G. (2013). TWINKLE is an essential mitochondrial helicase required for synthesis of nascent D-loop strands and complete mtDNA replication. Human Molecular Genetics, 22(10), 1983-1993.
Publication 2013
6-Aminocaproic Acid Acrylamide brilliant blue G Buffers Centrifugation Coomassie brilliant blue R Digitonin Edetic Acid Electrophoresis Gels Glycerin Mice, House Mitochondria Sodium Chloride Tissues Tromethamine Western Blot

Most recents protocols related to «6-Aminocaproic Acid»

1
Purification of ATP Synthase Complex
The strain expressing Atp6 subunit C-terminally tagged by HA-6xHis in the mitochondrial genome was characterized previously to cause no damage to the ATP synthase structure41 (link). This strain was used to pull down the whole ATP synthase complex by Ni-NTA agarose beads. Briefly, 5 mg of mitochondria were centrifuged and suspended in 1 mL of sonication buffer (250 mM sucrose, 50 mM NaH2PO4, 5 mM 6-aminocaproic acid, 1 mM EDTA, pH 7.5, protease inhibitors cocktail tablet (Roche), 1 µM PMSF) and sonicated 6 times 10 s, with 10 s intervals on ice. After centrifugation at 6000 × g 10 min at 4 °C, supernatant was ultracentrifuged at 268,526 × g for 1 h (Thermo Scientific™ Sorvall™ WX ultracentrifuge, TFT80.2 rotor). The pellet was washed twice with the sonication buffer without EDTA (without suspending it) and then suspended with the use of the potter in 500 µl MP extraction buffer (150 mM potassium acetate, 10% glycerol, 2 mM 6-aminocaproic acid, 30 mM HEPES, pH 7.4, 1% N-dodecyl-β-maltoside, 2 mM PMSF and protease inhibitors cocktail tablet, EDTA-free, Roche). After 20 min incubation on ice, the membranes were centrifuged for 30 min at 21,950 × g, 4 °C and the extract was incubated with 200 µL of the Ni–NTA agarose washed previously by Binding buffer (50 mM NaCl, 10% glycerol, 10 mM imidazole, 20 mM NaH2PO4, pH = 7.9, 0,1% n-dodecyl-β-maltoside, 2 mM PMSF, protease inhibitors cocktail tablet) for overnight. Next day the beads were washed twice with the Binding buffer, then suspended in 400 µL of Binding buffer, dosed and after addition of 100 µL of 5 × Laemmli sample buffer, boiled during 5 min. The 50 µg of the extract and 2 µg of bead eluate were loaded on the 15% SDS-PAGE gel. Then the gel was stained with Coomassie blue or silver staining according to manufacturer’s protocol (Pierce sliver stain kit, Thermo Fisher Scientific) to visualize the proteins.
Panja C., Wiesyk A., Niedźwiecka K., Baranowska E, & Kucharczyk R. (2023). ATP synthase interactome analysis identifies a new subunit l as a modulator of permeability transition pore in yeast. Scientific Reports, 13, 3839.
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Publication 2023
6-Aminocaproic Acid ATP-sepharose Buffers Centrifugation Coomassie blue dodecyl maltoside Edetic Acid G 526 Genome, Mitochondrial Glycerin HEPES imidazole Laemmli buffer Mitochondria Nitric Oxide Synthase Potassium Acetate Protease Inhibitors Proteins Protein Subunits SDS-PAGE Sepharose Sodium Chloride Stains Strains Sucrose Tablet Tissue, Membrane
2
Mitochondrial ATP Synthase Complex Analysis
Two-dimensional gel electrophoresis was based on the protocol of Schamel43 (link) with slight modifications. Briefly, the ATP synthase complexes were liberated from inner mitochondrial membrane of isolated mitochondria by incubation with 1–2% digitonin in extraction buffer (30 mM HEPES, 150 mM potassium acetate, 12% glycerol, 2 mM 6-aminocaproic acid, 1 mM EGTA, protease inhibitor cocktail tablets EDTA-free (Roche), pH 7.4) for different time intervals up to 60 min and separated using NativePAGE™ 3–12% Bis–Tris Gels (Thermo Fisher Scientific) to separate monomeric and dimeric ATP synthase complexes44 (link). For second dimensional analysis the lanes were cut from the gel and placed in SDS-PAGE running buffer (25 mM Tris, 192 mM Glycine, 0.1% SDS, pH 8.3 with 1% β-mercaptoethanol), heated in a microwave for 10 secs and incubated for another 10 min in a shaker. The gel strips were then loaded on the top of a 16% SDS-PAGE gel, and electrophoresis was conducted under denaturing conditions. Then the gel was stained with Coomassie blue or silver staining and bands cut-off were analyzed by mass spectrometry. For Western blotting proteins from the gel were transferred into PVDF or nitrocellulose membranes using iBlot system (Thermo Fisher Scientific). For SDS-PAGE analysis of steady state level of proteins, yeast cells were disrupted by alkaline lysis with NaOH/TCA45 (link). Western blot analysis was performed using the polyclonal rabbit anti-Mco10 antibody, anti-ATP synthase subunits antibodies (gifts from Marie-France Giraud, Bordeaux, France and Martin van der Laan, Germany), anti-Rip1 and Cob1 antibodies (provided by dr hab. Ulrike Topf, IBB PAS) or anti-Cox2 (Thermo Fisher Scientific).
Panja C., Wiesyk A., Niedźwiecka K., Baranowska E, & Kucharczyk R. (2023). ATP synthase interactome analysis identifies a new subunit l as a modulator of permeability transition pore in yeast. Scientific Reports, 13, 3839.
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Publication 2023
2-Mercaptoethanol 6-Aminocaproic Acid Anti-Antibodies Antibodies Antibodies, Anti-Idiotypic Bistris Buffers Cells Coomassie blue Digitonin Edetic Acid Egtazic Acid Electrophoresis Electrophoresis, Gel, Two-Dimensional Gifts Glycerin Glycine HEPES Mass Spectrometry Microwaves Mitochondria Mitochondrial Membrane, Inner Nitric Oxide Synthase Nitrocellulose polyvinylidene fluoride Potassium Acetate Protease Inhibitors Proteins Protein Subunits PTGS2 protein, human Rabbits Saccharomyces cerevisiae SDS-PAGE Tissue, Membrane Tromethamine Western Blot
3
Thylakoid Membrane Protein Analysis
SDS-PAGE and immunoblot analysis of proteins were performed as previously described (6 (link)) with each lane containing protein corresponding to 8 μg total chlorophyll. Thylakoid membranes were isolated as described (58 (link)). Briefly, cells were harvested at logarithmic growth phase (2 × 106 cells mL−1) and washed in MKT buffer (10 mM Tricine–KOH, pH 7.5, 20 mM KCl, 25 mM MgCl2, 5 mM aminocaproic acid, 1 mM benzamidine, and 0.2 mM PMSF) once before breaking by passage through a French pressure cell. Membranes were collected by centrifugation at 31,000g for 30 min, then resuspended in ACA 750 (750 mM aminocaproic acid, 50 mM Bis–Tris, pH 7.0, 0.5 mM EDTA) to a concentration of 1 mg mL−1 chlorophyll. Membranes were solubilized by addition of an equal volume of aminocaproic acid 750 containing 2% n-dodecyl β-D-maltoside (β-DM, Anatrace) for a final concentration of 0.5 mg ml-1 chlorophyll and 1% β-DM. Membranes were solubilized for 10 min on ice in the dark before centrifugation to pellet unsolubilized material. Solubilized membranes were then mixed 60:1 with loading buffer (100 mM BisTris–HCl, pH 7.0, 5% Coomassie G-250, 0.5 mM aminocaproic acid, and 30% sucrose) and 15 μl (corresponding to 7.5 μg chlorophyll) were loaded onto a 4 to 16% precast BN-PAGE gel (Life Technologies). Second dimension analysis was performed by solubilizing BN-PAGE gel slices in 2× Laemmli buffer (59 (link)) and loading into precast 2D gels (Life Technologies). All 2D images were taken on an AlphaInnotech Alphaimager using identical exposure times of 30 s.
Mass spectrometry experiments were performed at the Vincent J. Coates Protein Mass Spectrometry Facility. Bands were excised from BN-PAGE gels, digested with trypsin, and subjected to analysis by reverse phase LC-MS/MS on a Thermo Scientific LTQ XL ion trap mass spectrometer.
Calderon R.H., de Vitry C., Wollman F.A, & Niyogi K.K. (2023). Rubredoxin 1 promotes the proper folding of D1 and is not required for heme b559 assembly in Chlamydomonas photosystem II. The Journal of Biological Chemistry, 299(3), 102968.
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Publication 2023
6-Aminocaproic Acid benzamidine Bistris Buffers Cells Centrifugation Chlorophyll Chlorophyll A Edetic Acid Gels Immunoblotting Laemmli buffer Magnesium Chloride Mass Spectrometry Pressure Proteins SDS-PAGE Sucrose Tandem Mass Spectrometry Thylakoid Membrane Tissue, Membrane tricine Trypsin
4
Antifibrinolytics in Spinal Surgery
Studies were included in this review if they met all the following Population/Intervention/Comparison/Outcome(s) (PICOS) criteria: (P) The study included spinal surgeries of all types (lumbar, thoracic, thoracolumbar, and cervical) used either anteriorly or posteriorly. (I) antifibrinolytics (AP, TXA, or EACA); (C) Placebo; (O) Total blood loss, transfusion rate and the occurrence of deep venous thrombosis (DVT) and pulmonary embolism (PE); (S) randomized controlled trials (RCTs). Exclusion criteria were as follows: case control study, cohort study and retrospective study; duplicate publications; relevant specific data cannot be obtained; comments, letters, and guidelines; study did not report outcomes of interest.
Tan H., Pan S., Wei C., Chen Z, & Chen T. (2023). Comparative efficacy and safety of different hemostatic medications during spinal surgery: A network meta-analysis. Medicine, 102(9), e32923.
Publication 2023
6-Aminocaproic Acid Antifibrinolytic Agents Blood Transfusion Deep Vein Thrombosis Hemorrhage Lumbar Region Neck Operative Surgical Procedures Placebos Pulmonary Embolism
5
Purification of Yeast Membrane Protein Complexes
Yeast strains were grown in 11 L yeast extract peptone dextrose media (20 g/L peptone, 20 g/L glucose, 10 g/L yeast extract) supplemented with 100 μg/mL ampicillin and 0.02% antifoam in a Microferm fermenter (New Brunswick Scientific) at 30 °C for 1 d (>22 h), with aeration of 34 cubic feet per hour and stirring at 300 rpm. All subsequent steps were performed at 4 °C. Cells were harvested by centrifugation at 4,000 × g for 15 min and resuspended in 1 mL/g lysis buffer (8 g/L NaCl, 0.2 g/L KCl, 1.44 g/L Na2HPO4, 0.24 g/L KH2PO4, 80 g/L sucrose, 20 g/L sorbitol, 20 g/L glucose, 5 mM 6-aminocaproic acid, 5 mM benzamidine hydrochloride, 5 mM ethylenediaminetetraacetic acid, 10 mg/L phenylmethylsulfonyl fluoride, pH 7.4). Cells were lysed with 0.5 mm glass beads in a bead beater (BioSpec), with six cycles of 1 min of bead beating and 1 min of cooling. Cell debris was removed by centrifugation at 4,000 × g for 15 min. Membranes were then collected by ultracentrifugation (Beckman L-90K, Ti70 rotor) at 145,000 × g for 40 min, resuspended in 0.5 mL/g lysis buffer using a Dounce homogenizer, and stored at −80 °C prior to protein purification.
Frozen membranes were thawed at room temperature, and all the purification steps were performed at 4 °C. Membranes were solubilized with 1% (w/v) n-dodecyl β-D-maltoside (DDM; Anatrace) and mixed for 30 min. Insoluble material was removed by ultracentrifugation at 158,000 × g for 1h (Beckman L-90K, Ti70 rotor), and membranes were filtered with a 0.45 μm syringe filter and applied to a 0.5 mL anti-FLAG M2 affinity gel in a column (Millipore Sigma) pre-equilibrated in DDM Tris-buffered saline (DTBS; 50 mM Tris-HCl, 150 mM NaCl, 0.02% [w/v] DDM, pH 7.4). The column was washed with 10 column volumes of DTBS, and protein was eluted with three column volumes of DTBS containing 150 μg/mL of 3×FLAG peptide and one column volume of DTBS without peptide. Protein was then concentrated to ~200 μL with a 100 kDa molecular weight cutoff (MWCO) Amicon Ultracentrifugal filter (Millipore Sigma) at 1,000 × g, diluted with 4 mL glyco-diosgenin Tris-buffered saline (50 mM Tris-HCl, 150 mM NaCl, 0.004% [w/v] glyco-diosgenin [Anatrace], pH 7.4) and concentrated to ~200 μL in the same concentrator. For Vma12p-3×FLAG and Vma22p-3×FLAG, samples were further concentrated to ~1 to 2 mg/mL with a 100 kDa MWCO Vivaspin 500 centrifugal concentrator (Sartorius) at 12,000 × g. For Vma21p-3×FLAG, the sample was concentrated at 1,000 × g. Protein concentration was determined by bicinchoninic acid assay (Pierce).
Wang H., Bueler S.A, & Rubinstein J.L. (2023). Structural basis of V-ATPase VO region assembly by Vma12p, 21p, and 22p. Proceedings of the National Academy of Sciences of the United States of America, 120(6), e2217181120.
Publication 2023
6-Aminocaproic Acid Ampicillin benzamidine hydrochloride bicinchoninic acid Biological Assay Buffers Cells Centrifugation COOL-1 protein, human Cuboid Bone Diosgenin Edetic Acid Fermentors FLAG peptide Foot Freezing Glucose Peptides Peptones Phenylmethylsulfonyl Fluoride Proteins Saline Solution Sodium Chloride Sorbitol Sucrose Syringes Tissue, Membrane Tromethamine Ultracentrifugation Yeast, Dried

Top products related to «6-Aminocaproic Acid»

1
6 aminocaproic acid by Merck Group
Sourced in United States, Sao Tome and Principe
6-aminocaproic acid is a chemical compound used as a laboratory reagent. It is a colorless, crystalline solid with the molecular formula C6H13NO2. The primary function of 6-aminocaproic acid is to act as a chemical intermediate in various organic synthesis reactions.
2
N dodecyl β d maltoside by Merck Group
Sourced in United States
N-Dodecyl β-D-maltoside is a non-ionic detergent used in biochemical research and applications. It is a sugar-based surfactant that can be used to solubilize and stabilize membrane proteins. N-Dodecyl β-D-maltoside has a critical micelle concentration of approximately 0.17 mM in water at 25°C.
3
Aminocaproic acid by Merck Group
Sourced in United States
Aminocaproic acid is a synthetic amino acid used as a laboratory reagent. It functions as an antifibrinolytic agent, inhibiting the breakdown of fibrin clots.
4
Thrombin by Merck Group
Sourced in United States, Germany, United Kingdom, China, Sao Tome and Principe, Switzerland, Sweden, Ireland, Macao, India, Australia, France, Spain
Thrombin is a serine protease enzyme that plays a crucial role in the blood coagulation process. It is responsible for the conversion of fibrinogen to fibrin, which is the main structural component of blood clots. Thrombin also activates other factors involved in the clotting cascade, promoting the formation and stabilization of blood clots.
5
Aprotinin by Merck Group
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Aprotinin is a protease inhibitor derived from bovine lung tissue. It is used as a laboratory reagent to inhibit protease activity in various experimental procedures.
6
Fibrinogen by Merck Group
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Fibrinogen is a plasma protein that plays a crucial role in the blood clotting process. It is a component of the coagulation cascade and is essential for the formation of fibrin clots.
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6 aminohexanoic acid by Merck Group
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6-aminohexanoic acid is a chemical compound used in various laboratory applications. It is a straight-chain, aliphatic amino acid with a carboxyl group at one end and an amino group at the other. The compound can be utilized as a building block in the synthesis of polymers and other organic compounds. Its core function is to serve as a versatile chemical intermediate in research and development settings.
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Dimethyl sulfoxide (dmso) by Merck Group
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
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ε aminocaproic acid by Merck Group
Sourced in United States
ε-aminocaproic acid is a chemical compound used as a laboratory reagent. It functions as an inhibitor of the enzyme plasmin, which is involved in the breakdown of blood clots. The compound is commonly used in research and analytical applications where the control of plasmin activity is required.
10
ε aminocaproic acid εaca by Merck Group
Sourced in Germany
ε-aminocaproic acid (εACA) is a chemical compound with the formula (CH2)5CHNH2COOH. It is a naturally occurring amino acid that can be used in various laboratory applications.

More about "6-Aminocaproic Acid"

6-Aminocaproic Acid, also known as Aminocaproic Acid or ε-Aminocaproic Acid (εACA), is a synthetic amino acid that has been widely studied and utilized in medical treatments.
This molecule is known for its ability to inhibit the breakdown of fibrin, a crucial protein involved in blood clotting, making it an important tool in controlling excessive bleeding and hemorrhage.
The applications of 6-Aminocaproic Acid span various medical fields, including surgery, traumatic injury, and other conditions where managing blood loss is crucial.
Researchers have explored its potential in enhancing post-operative recovery, mitigating blood loss during cardiac procedures, and treating conditions like menorrhagia and hemophilia.
To optimize their studies on 6-Aminocaproic Acid, researchers can leverage the power of PubCompare.ai's AI-driven protocol comparison tool.
This cutting-edge technology helps identify the most effective research strategies by analyzing the literature, preprints, and patents.
By utilizing PubCompare.ai, researchers can stay ahead of the curve and take their 6-Aminocaproic Acid studies to new heights.
In addition to 6-Aminocaproic Acid, related compounds like N-Dodecyl β-D-maltoside, DMSO, and Aprotinin have also been studied for their potential in medical applications.
These molecules, along with Thrombin and Fibrinogen, play crucial roles in the coagulation cascade and can provide valuable insights for researchers exploring new avenues in hemostasis and thrombosis management.
By incorporating these insights and leveraging the advanced tools offered by PubCompare.ai, researchers can uncover new frontiers in the field of 6-Aminocaproic Acid and related compounds, ultimately benefiting patient care and advancing medical science.