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Thrombin Receptor Activating Peptides

Thrombin Receptor Activating Peptides are a class of synthetic peptides that can activate the proteinase-activated receptor (PAR) family, specifically the thrombin receptor (PAR-1).
These peptides mimic the activating effects of thrombin, a serine protease involved in the blood coagulation cascade, on its cognate receptor.
Thrombin Receptor Activating Peptides have been utilized in research to study the physiological and pathological roles of PAR-1 signaling, which has implications in hemostasis, inflammation, and cell proliferation.
Researchers can explore the power of these peptides using PubCompare.ai's AI-driven platform, which effortlessly locates the best research protocols from literture, preprints, and patents.
The intelligent comparison tools help identify the optimal protocols and products for research needs, driving data-driven experimentation and discovery in this dynamic field.

Most cited protocols related to «Thrombin Receptor Activating Peptides»

1
Rapid Pepsin Digestion and Cooled UPLC-MS
Cited 47 times
Unlabeled proteins, highly deuterated peptides and cytochrome c were analyzed using the UPLC system and conventional HPLC. In both LC-systems, labeled samples (50 µLs) were injected at a flow rate of 100 µL/min into a 2.1 mm × 50 mm stainless steel column that was packed with pepsin immobilized on POROS-20AL beads [prepared as described in8 (link), 9 (link)]. Under these conditions, the digestion time was approximately 30 seconds.
In the HPLC experiments, a Shimadzu HPLC (LC-10ADvp) system was used. Peptic peptides eluting from the online pepsin digestion step were trapped and desalted on a 1 mm × 8 mm C-18 peptide trap (Michrom Biosciences) and desalted for 3 min. The trap was placed inline with the analytical column, a Zorbax C-18, 3.5 µm 300 Å, 1.0 mm × 50 mm column (Agilent Technologies), and eluted into the mass spectrometer with a gradient of 15 to 30% acetonitrile in 6 min at a flow rate of 40 µL/min. HPLC mobile phases contained 0.05 % trifluoroacetic acid. The C-18 peptide trap and analytical column, as well as the injection and switching valves were placed in an ice-bath to maintain the required 0 °C. The mobile phases were kept in a separate ice-bath and then flowed through pre-cooling stainless steel loops (located before the gradient mixing tee) in the main ice-bath to ensure that they were cool prior to meeting deuterated sample. The pepsin column was held above the ice bath at approximately 15 °C9 (link).
In the UPLC experiments, peptic peptides from online pepsin digestion were trapped and desalted on a VanGuard Pre-Column (2.1 mm × 5 mm, ACQUITY UPLC BEH C18, 1.7 µm) for 3 min. The trap was placed in-line with an ACQUITY UPLC BEH C18 1.7 µm 1.0 × 100 mm column (Waters Corp.) and eluted into the mass spectrometer with a 8–40 % gradient of acetonitrile over 6 min at a flow rate of 40 µL/min. The volume of the system from the mixer to the head of the analytical column was ~ 30 µL which includes ~ 8 µL volume of the trap column in line. All mobile phases for the UPLC system contained 0.1 % formic acid.
Mass spectral analyses were carried out on a Waters LCT classic or QToF Premier. The LCT was used for initial validation of the cooled UPLC module chromatography and not for any analyses of deuterium incorporation. LCT classic instrument settings were: 3.2kV cone and 40 V capillary voltages. The LCT source and desolvation temperatures were 150 and 175 °C, respectively with a desolvation gas flow of 1024 L/hour and a cone gas flow of 99 L/hour. LCT mass spectra were acquired using a 0.50 sec scan time and 0.1 sec interscan delay time. QTof instrument settings were: 3.5kV cone and 40 V capillary voltages. The QTof source and desolvation temperatures were 80 and 175 °C, respectively with a desolvation gas flow of 600 L/hour. QTof mass spectra were acquired using a 0.450 sec scan time and 0.050 sec interscan time. All QTof data were collected in ESI (+) and V mode. Deuteration levels were calculated by subtracting the centroid of the isotopic distribution for peptide ions of undeuterated sample from the centroid of the isotopic distribution for peptide ions from the deuterium labeled sample. Deuterium levels were not corrected for back-exchange and are therefore reported as relative 1 (link).
Wales T.E., Fadgen K.E., Gerhardt G.C, & Engen J.R. (2008). High-speed and high-resolution UPLC separation at zero degrees Celsius. Analytical chemistry, 80(17), 6815-6820.
Publication 2008
acetonitrile ARID1A protein, human Bath C-Peptide Capillaries Chromatography Cytochromes c Deuterium Digestion formic acid Head High-Performance Liquid Chromatographies Ions Isotopes Mass Spectrometry Neoplasm Metastasis Pepsin A Peptides Proteins Radionuclide Imaging Retinal Cone Stainless Steel Steel Thrombin Receptor Activating Peptides Trifluoroacetic Acid
2
Automated Online Proteolysis and Peptide Separation
Cited 18 times
The online flow system used and system details and parameters are illustrated in Figure 1 and described below.
Experimental samples (~50 μL of ~1 μM protein in 0.1% formic acid at pH 2.5) are injected into the on-line flow system diagrammed in Figure 1. The flow system carries the protein solution at 50–120 μL/min through an immobilized acid protease column for proteolysis (15 or 60 μL total volume each). Digested peptides are directed through a second valve to a small C8 or C18 trap column (1×5 mm, 5 μm beads). After sufficient flow (~3 min at 50 μL/min) to transport the peptides into the trap column and wash away buffer salts, the second valve is switched, placing the trap column in the flow of a low volume HPLC pump. A water/acetonitrile gradient (6 μL/min, 10%–50% AcCN over 10–15 min) elutes peptides from the trap column through an analytical C18 column (0.3×50 mm, 3 μm beads) for rough peptide separation, and then to the electrospray needle for further separation of the peptides by mass. Narrow tubing (25 or 65 μm i.d.) is used in the slow flow chromatography stage. To minimize eluant peptide overlap, we use an acetonitrile gradient shaped to elute constant numbers of peptides per unit time. Typical peptide elution peak widths are 20 sec wide at baseline. We have not found peak widths to be limiting in the MS data even for hundreds of peptides, due especially to the ability of the ExMS analysis program [46 (link)] to recognize peptides in MS data even in the presence of significant spectral overlap.
Cleaning steps between serial experiments (several up–down gradients) elute very large peptides not useful for HX-MS experiments, helping to avoid peptide carryover from earlier MS runs and to maintain low column back pressure. If some peptides present a particularly difficult carryover problem [51 (link)], the availability of many other peptides makes it feasible to simply remove them from the experimental list. Overall, each experimental cycle takes 20–25 min followed by a 10–15 min cleaning cycle, resulting in a 40 min total time for each run. This allows for as many as 10 experimental HX runs each day in addition to an all-H run to calibrate chromatographic retention time for each peptide and an all-D run to calibrate their back exchange.
The flow rates and column sizes noted were chosen as a compromise between the competing demands of transit time, resolution, and back pressure. Particular care must be taken with flow system connections to assure against leaks under significant back pressure and to minimize unswept dead volume, which can lead to peak trailing and problems with peptide identification, although the ExMS analysis program operates to minimize this problem. Tubing is carefully cut, inspected, and connected, and ports are sprayed out with clean pressurized air on assembly. Common problems include slippage of connectors due to under-tightening, blockage due to over-tightening, and the trapping of particles at connections.
Mayne L., Kan Z.Y., Chetty P.S., Ricciuti A., Walters B.T, & Englander S.W. (2011). Many Overlapping Peptides for Protein Hydrogen Exchange Experiments by the Fragment Separation-Mass Spectrometry Method. Journal of the American Society for Mass Spectrometry, 22(11), 1898-1905.
Publication 2011
acetonitrile Acids Buffers Chromatography formic acid High-Performance Liquid Chromatographies Needles Peptide Hydrolases Peptides Pressure Proteins Proteolysis Retention (Psychology) Salts Thrombin Receptor Activating Peptides
3
Evaluating QuaMeter on Mass Spectrometry Data
Cited 6 times
We tested QuaMeter on several data sets spanning six different mass spectrometers. Table 1 summarizes all the data sets used in this study. In brief, we analyzed three different samples (bovine serum albumin, β-galactosidase, and yeast) on six different platforms. Each sample was analyzed in replicates spread over time to perform instrument quality control and maintenance. Full experimental details of these data sets are available in the Supporting Information.
The MS/MS scans present in all data sets were identified using MyriMatch or Pepitome. MyriMatch is a database search engine, whereas Pepitome is a spectral library search engine. Table 1 summarizes the sequence databases and mass tolerances used in all searches. Detailed configuration parameters for all searches are listed in the Supporting Information. MyriMatch was configured to derive semitryptic peptides from the protein database while using carbamidomethylation of cysteine (+57.0125 Da), oxidation of methionine (+15.996 Da), and formation of N-terminal pyroglutamine (−17.0265 Da) as variable modifications. Pepitome was configured to consider only fully tryptic and semitryptic peptides from the NIST ion trap spectral library (http://peptide.nist.gov). All search engines produced identifications in pepXML format.
IDPicker software filtered the peptide identifications from all search engines at a false discovery rate (FDR) of 5% unless otherwise stated. For MyriMatch, the software automatically combined the MVH and XCorr scores for FDR filtering. IDPicker was configured to use HGT, Kendall-Tau, and mzFidelity scores for filtering Pepitome results. Peptides passing the FDR thresholds were assembled into protein identifications following parsimony rules, and proteins with at least two distinct peptide identifications were considered for further analysis. QuaMeter software processed the raw files and corresponding IDPicker identifications to produce QC metrics for each data file. Since we wanted to compare the QC metrics generated from QuaMeter to that of MSQC software, we made the IDPicker identifications accessible to the MSQC software via an AWK script. We also created scripts in the R statistical programming language for combining multiple metric files to perform variability analysis. Detailed software configurations, scripts, and data processing methods are presented in the Supporting Information.
Ma Z.Q., Polzin K.O., Dasari S., Chambers M.C., Schilling B., Gibson B.W., Tran B.Q., Vega-Montoto L., Liebler D.C, & Tabb D.L. (2012). QuaMeter: Multivendor Performance Metrics for LC–MS/MS Proteomics Instrumentation. Analytical chemistry, 84(14), 5845-5850.
Publication 2012
cDNA Library Cysteine GLB1 protein, human Immune Tolerance Methionine Peptides Proteins Radionuclide Imaging Saccharomyces cerevisiae Serum Albumin, Bovine Strains Tandem Mass Spectrometry Thrombin Receptor Activating Peptides Trypsin
4
Peptide Response Curve in Plasma Mass Spec
Cited 6 times
A response curve consisting of peptides spiked into plasma was prepared as described previously (34 (link)). In brief, for the 3-MRM data set, a 9-point response curve was generated by spiking 11 synthetic peptides (representing prostate-specific antigen, horseradish peroxidase, leptin, myelin basic protein, myoglobin, aprotinin, and C-reactive protein) into digested plasma (1 μg/μL) so as to span a concentration range of 1–500 fmol/μL, with corresponding isotopically labeled (13C/15N) peptide standards added at a fixed concentration of 50 fmol/μL to all samples [referred to as study I in (34 (link))]. A 1-μL volume of each sample was analyzed in quadruplicate by LC-MRM-MS. Three data sets were acquired with a 4000 Q TRAP mass spectrometer (Applied Biosystems) at unit/unit resolution with a dwell time of 10 ms and an interscan delay time of 5 ms for each transition. One data set was acquired on a TSQ Quantum Ultra (Thermo Fisher Scientific) triple-quadrupole mass spectrometer with a 10-ms dwell time for each transition at unit/unit resolution. In all cases, only data from 10 peptides were analyzed, owing to insufficient detection of the 11th peptide.
For the 5-MRM data set, an equimolar mixture of the 7 proteins was digested, added to digested plasma, and then diluted with digested plasma to generate a 9-point response curve spanning the same concentration range (1–500 fmol/μL) in a digested-plasma background (1 μg/μL). Corresponding stable isotope–labeled internal standard (SIS) peptides were added to each sample at 50 fmol/μL [referred to as study II in (34 (link))]. We monitored 5 MRM transitions for each analyte and SIS peptide on a 5500 Q TRAP mass spectrometer (Applied Biosystems) by scheduled MRM with a target cycle time of 0.5 s, a retention-time window of 90 s, and an interscan delay of 3 ms. The 2 additional transitions were selected from previous optimization experiments conducted with the synthetic peptides. The pooled and filtered human plasma used for all experiments was from Bioreclamation.
Abbatiello S.E., Mani D.R., Keshishian H, & Carr S.A. (2009). Automated Detection of Inaccurate and Imprecise Transitions in Peptide Quantification by Multiple Reaction Monitoring Mass Spectrometry. Clinical chemistry, 56(2), 291-305.
Publication 2009
Aprotinin C Reactive Protein Homo sapiens Horseradish Peroxidase Isotopes Leptin Myelin Basic Protein Myoglobin Peptides Plasma Prostate-Specific Antigen Proteins Retention (Psychology) sodium-influx-stimulating peptide Thrombin Receptor Activating Peptides
5
Tryptic Peptide Analysis by LC-MS/MS
Cited 6 times
Tryptic peptides were subject to LC-MS/MS analysis using an Agilent 1100 LC system (Santa Clara, CA) connected to a Finnigan LTQ ion trap mass spectrometer (Thermo Fisher Scientific, Inc., San Jose, CA), as described previously 20 (link). Briefly, the peptide mixture was injected, using an autosampler (Agilent), and loaded onto a C18 peptide trap (Agilent). After washing, peptides were eluted from the trap with a gradient of acetonitrile (0 – 60% in 35 min) at a flow rate of 250 nL/min. The eluted peptides were then separated in a C18 PicoFrit column (New Objectives, Boston, MA) positioned directly in front of the orifice of an ion transfer tube of the LTQ mass spectrometer. Spectra were acquired in a data-dependent manner with dynamic exclusion option enabled. Each survey MS scan was followed by five MS/MS scans.
Wang G., Wu W.W., Zhang Z., Masilamani S, & Shen R.F. (2009). Decoy Methods for Assessing False Positives and False Discovery Rates in Shotgun Proteomics. Analytical chemistry, 81(1), 146-159.
Publication 2008
acetonitrile Forehead Peptides Radionuclide Imaging Tandem Mass Spectrometry Thrombin Receptor Activating Peptides Trypsin

Most recents protocols related to «Thrombin Receptor Activating Peptides»

1
Platelet Aggregation by Agonists
Human platelets purified from citrated blood were mixed with increasing doses of GH-ALG or rabbit ATG and aggregation was monitored for 60 minutes on a TA-8V STAGO aggregometer. To induce platelet aggregation, ristocetin (1.5 mg/ml), Thrombin Receptor Activator Peptide (TRAP,1.5 µM), arachidonic acid (0.3 mg/ml), ADP (adenosine diphosphate, 5 µM), epinephrine (5 µM) and collagen (1.25 µg/ml) were evaluated.
Rousse J., Royer P.J., Evanno G., Lheriteau E., Ciron C., Salama A., Shneiker F., Duchi R., Perota A., Galli C., Cozzi E., Blancho G., Duvaux O., Brouard S., Soulillou J.P., Bach J.M, & Vanhove B. (2023). LIS1, a glyco-humanized swine polyclonal anti-lymphocyte globulin, as a novel induction treatment in solid organ transplantation. Frontiers in Immunology, 14, 1137629.
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Publication 2023
Adenosine Diphosphate antithymocyte immunoglobulin Arachidonic Acid BLOOD Blood Platelets Collagen Epinephrine Homo sapiens Platelet Aggregation Ristocetin Thrombin Receptor Activating Peptides TRAP1 protein, human
2
Peptide Separation and Quantification
Tryptic peptides (~ 500 ng for sequential window acquisition of all theoretical fragment ion spectra (SWATH) analysis of each sample were analysed using a Evosep One LC system (using Evotip C18 trap column loading system) coupled to an AB Sciex 6600 TripleTOF mass spectrometer (AB Sciex, Massachusetts, USA). Peptide samples were separated on an Evosep performance column (8 cm × 150 µm) packed with 1.5 µm Dr Maisch C18 beads. The column was maintained at 35 °C using the 60SPD method. The peptides were then eluted over 21 min with a gradient of 0–35% Solvent B (Solvent A: 0.1% Formic Acid; Solvent B: 100% ACN/0.1% Formic Acid).
For data-dependent (concatenated fractions) acquisition (DDA), ~ 500 ng of tryptic peptides of each sample were analysed using a Dionex Ultimate 3000 RSLC system coupled to an AB Sciex 6600 Triple TOF mass spectrometer. Peptide samples were inline desalted using an Acclaim PepMap C18 trap column (75 μm × 2 cm; 2 min at 5 μl min−1 using 2% ACN/0.2% FA). Trapped peptides were gradient eluted and separated on a Waters Acquity CSH C18 NanoEase column (75 μm × 25 cm, 1.7 μm particle size) maintained at 45 °C at a flow-rate of 0.3 μl min−1 with a linear gradient of 4 – 40% Solvent B over 45 min (Solution A: 0.1% Formic Acid; Solvent B: 80% ACN/0.1% Formic Acid). Precursor (MS) scans were acquired from m/z 400–1500 (2+–5+ charge states) using an accumulation time of 200 ms followed by 40 fragment ion (MS/MS) scans, acquired from m/z 100–1800 with 20 ms accumulation time each. For SWATH, precursor scans ranged from m/z 400–900 using an accumulation time of 100 ms, and fragment ions were acquired from m/z 100–1800 with 15 ms accumulation time per window across 60 variable-width windows that overlapped by 0.5 Da.
Baichan P., Naicker P., Augustine T.N., Smith M., Candy G., Devar J, & Nweke E.E. (2023). Proteomic analysis identifies dysregulated proteins and associated molecular pathways in a cohort of gallbladder cancer patients of African ancestry. Clinical Proteomics, 20, 8.
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Publication 2023
formic acid Ions Peptides Radionuclide Imaging Solvents Tandem Mass Spectrometry Thrombin Receptor Activating Peptides Trypsin Z-100
3
Tandem Mass Spectrometry for Peptide Sequencing
Tryptic peptides were analyzed using a nanoflow ultra-high-performance liquid chromatograph and an electrospray Orbitrap mass spectrometer (RSLCnano and Q Exactive Plus, Thermo) for tandem MS peptide sequencing. Peptide mixtures were loaded onto a pre-column (100-µm ID × 2-cm column packed with C18 reversed-phase resin; particle size, 5 µm; pore size, 100 Å) and washed for 5 min with aqueous 2% acetonitrile and 0.1% FA. Solvent A comprised 98% ddH2O, 2% acetonitrile and 0.1% FA, and solvent B comprised 90% acetonitrile, 10% ddH2O and 0.1% FA. Trapped peptides were eluted or separated on a C18 analytical column (75-µm ID × 50 cm; particle size, 2 µm; pore size, 100 Å; Thermo Fisher Scientific) using a 90-min gradient at a flow rate of 300 nl min−1 of 2% to 3% solvent B over 5 min, 3% to 30% solvent B over 27 min, 30% to 38.5% solvent B over 5 min, 38.5% to 90% solvent B over 3 min and then held at 90% for 3 min, followed by 90% to 2% solvent B in 1 min and re-equilibrated for 18 min. MS resolution was set at 70,000, and MS/MS resolution was set at 17,500 with a maximum IT of 50 ms. The top 16 tandem mass spectra were collected using data-dependent acquisition following each survey scan and 60-s exclusion for previously sampled peptide peaks. For phosphoproteomic, fucoproteomic and HLA-DRB1 WT and glycofucomutant interactor profiling, MaxQuant62 (link) software (version 1.6.2.10) was used to identify and/or quantify phosphopeptides and proteins for the data-dependent acquisition runs. The false discovery rate was set to 1%.
Lester D.K., Burton C., Gardner A., Innamarato P., Kodumudi K., Liu Q., Adhikari E., Ming Q., Williamson D.B., Frederick D.T., Sharova T., White M.G., Markowitz J., Cao B., Nguyen J., Johnson J., Beatty M., Mockabee-Macias A., Mercurio M., Watson G., Chen P.L., McCarthy S., MoranSegura C., Messina J., Thomas K.L., Darville L., Izumi V., Koomen J.M., Pilon-Thomas S.A., Ruffell B., Luca V.C., Haltiwanger R.S., Wang X., Wargo J.A., Boland G.M, & Lau E.K. (2023). Fucosylation of HLA-DRB1 regulates CD4+ T cell-mediated anti-melanoma immunity and enhances immunotherapy efficacy. Nature Cancer, 4(2), 222-239.
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Publication 2023
A-A-1 antibiotic acetonitrile ARID1A protein, human High-Performance Liquid Chromatographies HLA-DRB1 Antigen Peptides Phosphopeptides Proteins Radionuclide Imaging Resins, Plant Solvents Tandem Mass Spectrometry Thrombin Receptor Activating Peptides Trypsin
4
Platelet Aggregation Assay
Light transmission of 40 µL platelet suspension, supplemented with 160 µL Tyrode’s buffer (final concentration: 200 × 103 platelets/μL) containing 100 μg/mL fibrinogen and 2 mM Ca2+, and platelet aggregation was monitored over 10 min using a four-channel APACT4004 aggregometer (Labitec, Ahrensburg, Germany). Aggregation studies with ADP were performed in platelet-rich plasma (PRP). Washed platelets and PRP were incubated with 20 µg/mL EA-20, control IgG antibody and/or seroblock (Bio-Rad, Feldkirchen, Germany) and/or Losartan (50 µM, Sigma, Taufkirchen, Germany) for 5 min. Platelet aggregation was induced by the addition of type I collagen (Col-I, Haemochrom Diagnostica GmbH, Essen, Germany), collagen-related peptide (CRP, Cambcol, Cambridgeshire, UK), thrombin (Roche, Grenzach-Wyhlen, Germany) and thrombin receptor activator for peptide 6 (TRAP-6, Haemochrom Diagnostica GmbH, Essen, Germany), and adenosine diphosphate (ADP, Sigma, Taufkirchen, Germany).
Han C., Ren P., Mamtimin M., Kruk L., Sarukhanyan E., Li C., Anders H.J., Dandekar T., Krueger I., Elvers M., Goebel S., Adler K., Münch G., Gudermann T., Braun A, & Mammadova-Bach E. (2023). Minimal Collagen-Binding Epitope of Glycoprotein VI in Human and Mouse Platelets. Biomedicines, 11(2), 423.
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Publication 2023
Adenosine Diphosphate Blood Platelets Buffers collagen-related peptide Collagen Type I Fibrinogen Immunoglobulin G Light Losartan Platelet-Rich Plasma Platelet Aggregation Thrombin Thrombin Receptor Activating Peptides thrombin receptor peptide (42-47) Transmission, Communicable Disease
5
Orbitrap-based Shotgun Proteomics Protocol
One out of eight sets of experiments were analyzed on an Orbitrap Fusion Lumos Tribrid mass spectrometer coupled with the nanoAcquity LC system. Approximately, 1 μg of peptides were loaded onto a nanoAcquity UPLC Symmetry C18 trap column (Waters) with 95% solvent A (0.1% FA in water (LCMS grade)) and 5% solvent B (0.1% FA in acetonitrile (LCMS grade)) using the nanoAcquity LC system at a flow rate of 300 nL/min. Peptides were separated on a C18 ACQUITY UPLC HSS T3 column (Waters) and eluted using a 60 min gradient from 3 to 48% of solvent B at a flow rate of 300 nL/min. The eluent from the C18 column was electrosprayed into the Orbitrap Lumos using a 1.8 kV spray voltage and a 260 °C ion transfer tube in positive mode. Peptides with the precursor mass range within m/z of 300 to 2000, with +2 to +7 charges, were selected for further fragmentation in MS2. The resolution for MS1 was set to 60,000 FWHM. The cycle time for MS1 scans was set to 3s. The automatic gain control (AGC) and the maximum injection time were set at 4e5 and 50 ms, respectively. The most intense precursor ions were selected and isolated using an ion trap with a peptide-like monoisotopic profile (MIPS) and an intensity threshold of 5e4, and fragmented with higher-energy collisional dissociation (HCD) (40% collision energy). The fragment ions (MS2) were analyzed in the orbitrap with a resolution of 30,000 FWHM at the auto-normal scan rate. The AGC target and the maximum injection time were set at 1e5 and 54 ms, respectively. The first mass of the MS2 scan was set to 90 m/z to detect b1 ions. Dynamic exclusion was enabled, and the precursor ion was fragmented twice and excluded for 30 s to avoid the repetitive acquisition of the same precursor ion having a similar m/z within ±10 ppm.
The mass spectrometry raw data were converted into .mgf format using the MSConvert tool, and the centroid peaks were created using the peak picking option. The resulting .mgf files were submitted to the Mascot/MSGF+ database search programs. The data were searched the same way as described in the previous section with semi-tryptic enzymatic cleavage. Mass tolerance for precursor and fragment ions was set to 5 ppm and 0.02 Da, respectively. Variable modifications were set as Oxidation (M) and Amidination (K and N-term of peptide/protein). The detected peptides on a Mascot within 1% FDR were considered as confident identifications. N-terminal amidinated peptides were manually checked for the presence of b1 ions.
Misal S.A., Ovhal S.D., Li S., Karty J.A., Tang H., Radivojac P, & Reilly J.P. (2023). Non-Specific Signal Peptidase Processing of Extracellular Proteins in Staphylococcus aureus N315. Proteomes, 11(1), 8.
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Publication 2023
acetonitrile Cytokinesis Enzymes Immune Tolerance Ions Laser Capture Microdissection Mass Spectrometry nucleoprotein, Measles virus Peptides Radionuclide Imaging Self Confidence Solvents Thrombin Receptor Activating Peptides Trypsin Z 300

Top products related to «Thrombin Receptor Activating Peptides»

1
Zorbax 300sb c18 peptide trap by Agilent Technologies
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The Zorbax 300SB-C18 peptide traps are analytical HPLC columns designed for the separation and purification of peptides. They feature a silica-based stationary phase with a C18 alkyl chain modification, providing a reversed-phase separation mechanism suitable for peptide analysis and sample preparation.
2
Adenosine diphosphate (adp) by Merck Group
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ADP is a high-performance liquid chromatography (HPLC) system designed for analytical and preparative separations. It features advanced technology to deliver precise and reproducible results. The core function of ADP is to facilitate the separation, identification, and purification of complex mixtures of chemical compounds.
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Q exactive by Thermo Fisher Scientific
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The Q Exactive is a high-resolution mass spectrometer designed for accurate and sensitive analysis of a wide range of samples. It features a quadrupole mass filter and an Orbitrap mass analyzer, providing high-resolution, accurate mass measurements for qualitative and quantitative applications.
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Q exactive mass spectrometer by Thermo Fisher Scientific
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The Q Exactive mass spectrometer is a high-resolution, accurate-mass (HRAM) instrument designed for advanced proteomics, metabolomics, and small molecule applications. It combines a quadrupole mass filter with a high-field Orbitrap mass analyzer to provide precise mass measurements and high-quality data.
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Nanospray flex ion source es071 by Thermo Fisher Scientific
The Nanospray Flex Ion Source ES071 is a compact, high-performance ion source designed for liquid chromatography-mass spectrometry (LC-MS) applications. It utilizes a nanospray technique to generate a fine spray of sample ions, enabling efficient ionization and high sensitivity for analyte detection.
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Picofrit column by New Objective
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The PicoFrit column is a laboratory equipment used for chromatographic separations. It is designed for high-performance liquid chromatography (HPLC) applications. The PicoFrit column features a fused silica capillary with an integrated spray tip for direct electrospray ionization (ESI) mass spectrometry (MS) detection.
7
Maxiscript t7 kit by Thermo Fisher Scientific
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The MAXIscript T7 kit is a laboratory equipment product that allows for the in vitro transcription of RNA from DNA templates. The kit includes the necessary reagents and enzymes to synthesize capped or uncapped RNA transcripts.
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Pac 1 fitc by BD
Sourced in United States, Germany, United Kingdom
PAC-1-FITC is a fluorescent-labeled antibody used for detecting and quantifying apoptosis in flow cytometry applications. It binds to the cleaved form of caspase-3, a key executioner caspase involved in the apoptotic pathway. The FITC (Fluorescein Isothiocyanate) label allows for the visualization and detection of apoptotic cells.
9
Streptavidin coupled dynabeads by Thermo Fisher Scientific
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Streptavidin-coupled Dynabeads are magnetic beads coated with the streptavidin protein. Streptavidin has a high affinity for biotin, enabling the beads to be used for the capture and separation of biotinylated molecules.
10
Thrombin receptor activator peptide 6 trap 6 by Merck Group
Sourced in United Kingdom
Thrombin Receptor Activator Peptide 6 (TRAP-6) is a synthetic peptide that directly activates the thrombin receptor, also known as the protease-activated receptor-1 (PAR-1). This peptide is commonly used in research applications to study platelet activation and thrombin signaling pathways.

More about "Thrombin Receptor Activating Peptides"

Thrombin Receptor Activating Peptides (TRAPs) are a class of synthetic peptides that can activate the proteinase-activated receptor (PAR) family, specifically the thrombin receptor (PAR-1).
These peptides mimic the activating effects of thrombin, a serine protease involved in the blood coagulation cascade, on its cognate receptor.
TRAPs have been widely utilized in research to study the physiological and pathological roles of PAR-1 signaling, which has implications in hemostasis, inflammation, and cell proliferation.
Researchers can explore the power of these peptides using PubCompare.ai's AI-driven platform, which effortlessly locates the best research protocols from literature, preprints, and patents.
The intelligent comparison tools help identify the optimal protocols and products for research needs, driving data-driven experimentation and discovery in this dynamic field.
In addition to TRAPs, researchers may also employ other tools and techniques to study PAR-1 signaling and related processes.
For example, Zorbax 300SB-C18 peptide traps can be used for the purification and enrichment of peptides, while ADP (adenosine diphosphate) can be used to study platelet activation and aggregation.
The Q Exactive mass spectrometer and Nanospray Flex Ion Source ES071 can be utilized for the high-resolution analysis of peptides and proteins, and the PicoFrit column can be used for liquid chromatography-mass spectrometry (LC-MS) applications.
Furthermore, the MAXIscript T7 kit can be employed for the in vitro transcription of RNA, and PAC-1-FITC (a fluorescently labeled PAR-1 agonist) and Streptavidin-coupled Dynabeads can be used for the detection and isolation of PAR-1-expressing cells.
Researchers may also utilize Thrombin Receptor Activator Peptide 6 (TRAP-6) as a tool to study PAR-1 activation and its downstream effects.
By leveraging these tools and techniques, along with the power of TRAPs and the AI-driven insights provided by PubCompare.ai, researchers can drive data-driven experimentation and make groundbreaking discoveries in the field of PAR-1 signaling and its implications for hemostasis, inflammation, and cell proliferation.