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Fluorogenic Substrate

Fluorogenic Substrate: A chemical compound that undergoes a fluorescent change upon interaction with a specific enzyme or target, enabling sensitive detection and quantification of biological processes.
These substrates are widely used in research for monitoring enzyme activity, cell signaling, and other dynamic cellular events.
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Most cited protocols related to «Fluorogenic Substrate»

1
Kinetic Analysis of SARS-CoV M^pro Enzyme Activity

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Publication 2006
Biological Assay Buffers Edetic Acid enzyme activity Enzyme Assays Fluorogenic Substrate Kinetics Peptide Hydrolases Psychological Inhibition Severe acute respiratory syndrome-related coronavirus Tromethamine
2
Monitoring Plasmodium PEXEL Trafficking Pathways
Transgenic parasites expressed PfEMP3-GFP or PfEMP3R>A-GFP chimeras from plasmids pPfEMP3WTGlux.1 or PfEMP3R>AGlux.1, respectively. Transgenic parasites expressing KAHRP-GFP contained the plasmid pKAHRPGlux.1, comprising DNA encoding residues 1-96 of KAHRP (PFB0100c). Parasites expressing ACPs-GFP are previously described 21 (link). Parasites expressing PfEMP3xQ-GFP contained the plasmid pPfEMP3xQGlux.1, encoding residues 1-36 of PfEMP3, followed by an alanine (to allow for signal peptidase cleavage at IYSEA-) and residues 63-82 of PfEMP3 (which include residues 63aQ64 of the PEXEL) cloned into pGlux.1. The plasmids pPMVHA1.5 pPMIXHA1.5 were integrated into either the Plasmepsin V locus (PF13_0133) or Plasmepsin IX locus (PF14_0281), respectively to append HA tags. The transgenic parasites 3D7-PMVmutHA episomally expressed plasmid pTETPMVmutHA, which contains DNA encoding Plasmepsin V with D118A, D365A and F370A substitutions fused to the same tags as in 3D7-PMVHA, cloned into the anhydrotetracycline (ATc) regulatable plasmid pTGFP 29 (link). The same DNA encoding Plasmepsin V with D118A, D365A and F370A substitutions fused to HA, but with alternate cloning sites, was cloned into pGlux.1, removing GFP, to create pPMVmutHA2. This plasmid contains the constitutively expressed crt promoter and is non-inducible. Recombinant GBP130 or GBP130 RLE>A was expressed in E. coli harbouring plasmids pGBP130-3Cmyc18His or pGBP130-3A-3Cmyc18His, respectively, which encodes residues 66 to 196 of GBP130 (containing the wild-type or mutant PEXEL). Recombinant Plasmepsin V was expressed in E. coli harbouring plasmid pHisPMVtrunc, which contains DNA encoding residues 37-521 of Plasmepsin V cloned into pProExHTb.
Plasmepsin V activity was assayed either with anti-HA beads containing ipPMVHA or ipPMVmutHA or 3–5 μg of HPLC-eluted protein added to the reaction that contained either PEXEL peptide substrate, recombinant PEXEL substrate or fluorogenic PEXEL peptide substrate. Digest reactions were analysed by HPLC and LC-MS/MS, immunoblot and fluorescence intensity, respectively.
Boddey J.A., Hodder A.N., Günther S., Gilson P.R., Patsiouras H., Kapp E.A., Pearce J.A., de Koning-Ward T.F., Simpson R.J., Crabb B.S, & Cowman A.F. (2010). An aspartyl protease directs malaria effector proteins to the host cell. Nature, 463(7281), 627-631.
Publication 2009
Alanine anhydrotetracycline Animals, Transgenic Chimera Cytokinesis Escherichia coli Fluorescence Fluorogenic Substrate High-Performance Liquid Chromatographies Immunoblotting Parasites Peptides plasmepsin Plasmids Proteins signal peptidase Tandem Mass Spectrometry
3
Monitoring Plasmodium PEXEL Trafficking Pathways
Transgenic parasites expressed PfEMP3-GFP or PfEMP3R>A-GFP chimeras from plasmids pPfEMP3WTGlux.1 or PfEMP3R>AGlux.1, respectively. Transgenic parasites expressing KAHRP-GFP contained the plasmid pKAHRPGlux.1, comprising DNA encoding residues 1-96 of KAHRP (PFB0100c). Parasites expressing ACPs-GFP are previously described 21 (link). Parasites expressing PfEMP3xQ-GFP contained the plasmid pPfEMP3xQGlux.1, encoding residues 1-36 of PfEMP3, followed by an alanine (to allow for signal peptidase cleavage at IYSEA-) and residues 63-82 of PfEMP3 (which include residues 63aQ64 of the PEXEL) cloned into pGlux.1. The plasmids pPMVHA1.5 pPMIXHA1.5 were integrated into either the Plasmepsin V locus (PF13_0133) or Plasmepsin IX locus (PF14_0281), respectively to append HA tags. The transgenic parasites 3D7-PMVmutHA episomally expressed plasmid pTETPMVmutHA, which contains DNA encoding Plasmepsin V with D118A, D365A and F370A substitutions fused to the same tags as in 3D7-PMVHA, cloned into the anhydrotetracycline (ATc) regulatable plasmid pTGFP 29 (link). The same DNA encoding Plasmepsin V with D118A, D365A and F370A substitutions fused to HA, but with alternate cloning sites, was cloned into pGlux.1, removing GFP, to create pPMVmutHA2. This plasmid contains the constitutively expressed crt promoter and is non-inducible. Recombinant GBP130 or GBP130 RLE>A was expressed in E. coli harbouring plasmids pGBP130-3Cmyc18His or pGBP130-3A-3Cmyc18His, respectively, which encodes residues 66 to 196 of GBP130 (containing the wild-type or mutant PEXEL). Recombinant Plasmepsin V was expressed in E. coli harbouring plasmid pHisPMVtrunc, which contains DNA encoding residues 37-521 of Plasmepsin V cloned into pProExHTb.
Plasmepsin V activity was assayed either with anti-HA beads containing ipPMVHA or ipPMVmutHA or 3–5 μg of HPLC-eluted protein added to the reaction that contained either PEXEL peptide substrate, recombinant PEXEL substrate or fluorogenic PEXEL peptide substrate. Digest reactions were analysed by HPLC and LC-MS/MS, immunoblot and fluorescence intensity, respectively.
Boddey J.A., Hodder A.N., Günther S., Gilson P.R., Patsiouras H., Kapp E.A., Pearce J.A., de Koning-Ward T.F., Simpson R.J., Crabb B.S, & Cowman A.F. (2010). An aspartyl protease directs malaria effector proteins to the host cell. Nature, 463(7281), 627-631.
Publication 2009
Alanine anhydrotetracycline Animals, Transgenic Chimera Cytokinesis Escherichia coli Fluorescence Fluorogenic Substrate High-Performance Liquid Chromatographies Immunoblotting Parasites Peptides plasmepsin Plasmids Proteins signal peptidase Tandem Mass Spectrometry
4
FRET Assay for SARS-CoV-2 and SARS-CoV 3CLpro Inhibition
A fluorescence resonance energy transfer (FRET) protease assay was applied to measure the inhibitory activity of compounds against SARS-CoV-2 3CLpro and SARS-CoV 3CLpro. The fluorogenic substrate MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2 was synthesized by GenScript (Nanjing, China). The FRET-based protease assay was performed as follows. The recombinant SARS-CoV-2 3CLpro (30 nM final concentration) or SARS-CoV 3CLpro (100 nM final concentration) was mixed with serial dilutions of each compound, oral liquid or the dissolved lyophilized powder in 80 µL assay buffer (50 mM Tris–HCl, pH 7.3, 1 mM EDTA) and incubated for 10 min. The reaction was initiated by adding 40 µL fluorogenic substrate at a final concentration of 20 µM. After that, the fluorescence signal at 320 nm (excitation)/405 nm (emission) measured immediately every 35 s for 3.5 min with a Bio-Tek Synergy4 plate reader. The initial velocities of reactions with compounds added at various concentrations compared to the reaction added with DMSO were calculated and used to generate inhibition profiles.
The inhibition of SARS-CoV-2 PLpro by compounds as well as Shuanghuanglian preparations was measured similar to that described previously [23 (link)] with a fluorogenic peptide (RLRGG-AMC) synthesized by GenScript (Nanjing, China). The reactions were performed in a total volume of 120 μL. First, 50 nM PLpro was incubated with the indicated concentrations of tested compounds or Shuanghuanglian preparations in the condition of 50 mM HEPES, pH 7.5, 0.1 mg/mL BSA, 5 mM DTT for 10 min. The reactions were initiated by the addition of 10 µM fluorogenic peptide. After that, the fluorescence signal at 360 nm (excitation)/460 nm (emission) was measured immediately every 1 min for 5 min with a Bio-Tek Synergy4 plate reader. The initial velocities of reactions with compounds or Shuanghuanglian added at various concentrations compared to the reaction added with DMSO were calculated and used to generate inhibition profiles.
For each compound or Shuanghuanglian preparation, at least three independent experiments were performed for the determination of IC50 values. The IC50 values were expressed as the mean ± SD and determined via nonlinear regression analysis using GraphPad Prism software 8.0 (GraphPad Software, Inc., San Diego, CA, USA).
Su H.X., Yao S., Zhao W.F., Li M.J., Liu J., Shang W.J., Xie H., Ke C.Q., Hu H.C., Gao M.N., Yu K.Q., Liu H., Shen J.S., Tang W., Zhang L.K., Xiao G.F., Ni L., Wang D.W., Zuo J.P., Jiang H.L., Bai F., Wu Y., Ye Y, & Xu Y.C. (2020). Anti-SARS-CoV-2 activities in vitro of Shuanghuanglian preparations and bioactive ingredients. Acta Pharmacologica Sinica, 41(9), 1167-1177.
Publication 2020
Biological Assay Buffers Edetic Acid Fluorescence Fluorescence Resonance Energy Transfer Fluorogenic Substrate HEPES Peptide Hydrolases Peptides Powder prisma Psychological Inhibition SARS-CoV-2 Severe acute respiratory syndrome-related coronavirus shuang-huang-lian Sulfoxide, Dimethyl Technique, Dilution Tromethamine
5
Proteasome Activity Assay Protocol
In vitro assay of 26S proteasome activities was performed as previously described10 (link). Cells were collected in proteasome activity assay buffer (50 mM Tris-HCl (pH 7.5), 250 mM sucrose, 5 mM MgCl2, 0.5 mM EDTA, 2 mM ATP and 1 mM dithiothreitol) and lysed by passing 10 times through a 27 gauge needle attached to a 1 ml syringe. Lysate was centrifuged at 10,000g for 10 min at 4°C. 15–25 μg of total protein of cell lysates were transferred to a 96-well microtiter plate (BD Falcon) and then the fluorogenic substrate was added to lysates. For measuring the chymotrypsin-like activity of the proteasome we used either Z-Gly-Gly-Leu-AMC (Enzo) or Suc-Leu-Leu-Val-Tyr-AMC (Enzo). We used Z-Leu-Leu-Glu-AMC (Enzo) to measure the caspase-like activity of the proteasome and Ac-Arg-Leu-Arg-AMC for the proteasome trypsin-like activity. Fluorescence (380-nm excitation, 460-nm emission) was monitored on a microplate fluorometer (Infinite M1000, Tecan) every 5 min for 1 h at 37°C. Protein concentration of the cell homogenates was determined using the BCA protein assay (Pierce).
Vilchez D., Boyer L., Morantte I., Lutz M., Merkwirth C., Joyce D., Spencer B., Page L., Masliah E., Berggren W.T., Gage F.H, & Dillin A. (2012). Increased proteasome activity determines human embryonic stem cell identity. Nature, 489(7415), 304-308.
Publication 2012
26S proteasome arginine 4-methyl-7-coumarylamide Biological Assay Buffers Caspase Cells Chymotrypsin Dithiothreitol Edetic Acid Fluorescence Fluorogenic Substrate GLU-AMC glycyl-glycyl-leucine leucylleucine Magnesium Chloride Multicatalytic Endopeptidase Complex Needles Proteins Sucrose Syringes Tromethamine Trypsin valyltyrosine

Most recents protocols related to «Fluorogenic Substrate»

1
Matrix Metalloproteinase Inhibition Assay
Not available on PMC !

Example 6

Individual inhibitors were dissolved in TCN buffer (50 mM Tris-HCl, 10 mM CaCl2, 150 mM NaCl2, 0.05% Brij 35 at pH 7.5) at appropriate dilutions then added to the wells of a microtiter plate (10 μL/well) in triplicate. Each well of test agent (and appropriate control wells) was then treated with activated MMP-2 or 9 (10 μL of a 40 nM solution in 50 mM Hepes, 10 mM CaCl2), 1% Brij 35 at pH 7.5; R&D Systems) followed by 30 μL TCN buffer and 150 μL the fluorogenic peptide substrate (Mca-PLGL-Dpa-AR-NH2; R&D Systems). The resulting mixtures were incubated 1 h at 27° C. then analyzed using a FL600 fluorescent plate reader (excitation=310/20; emission=420/50; optics=bottom; sensitivity=225) and KC4 Software.

TABLE 2
MMP inhibition data
Imaging
AgentMMP-2MMP-9
15.193.54
231.620.2
34.612.59
415.415.3
50.580.74
62.742.98
RP8056.507.40

US11865195B2. Evaluation of presence of and vulnerability to atrial fibrillation and other indications using matrix metalloproteinase-based imaging (2024-01-09). Lantheus Medical Imaging, Inc. [US], Yale University [US]. Inventors: Albert J. Sinusas [US], Joseph G. Akar [US], Richard R. Cesati [US], Heike S. Radeke [US], Stephen B. Haber [US].
Full text: Click here
Patent 2024
Biological Assay Brij 35 Buffers Eye Fluorogenic Substrate HEPES Hypersensitivity Matrix Metalloproteinase 9 Matrix Metalloproteinase Inhibitors MMP2 protein, human Peptides Psychological Inhibition Technique, Dilution Tromethamine
2
Comparison of Coagulation Factors and Thrombin Generation
INR levels in the fingertip capillary blood from the patients were measured using CoaguChek XS Plus. Simultaneously, venous blood samples were collected into a tube containing 3.2% buffered sodium citrate. The tubes were transferred to a conventional laboratory and centrifuged at 1,550×g for 15 minutes. The plasma obtained after centrifugation was used to measure the INR by a conventional laboratory test using a standard coagulation analyzer ACL TOP 750.
All coagulation factor tests were performed using the ACL TOP 750 analyzer. The coagulation factors were measured by a PT-based clotting test using HemosIL RecombiPlasTin reagent (ISI 1.0) for factors II, V, VII, and X (Instrumentation Laboratory, Lexington, MA, USA) and by an activated partial thromboplastin-based clotting test using SynthASil reagent for factors VIII, XI, XI, and XII (Instrumentation Laboratory SpA). Fibrinogen was measured using the Fibrinogen-C XL kit (Instrumentation Laboratory SpA). Proteins C and S were also tested using the ACL TOP 750 analyzer.
Thrombin generation was measured as previously described [8 (link)]. Briefly, 20 μL of reagent containing tissue factor at a final concentration of 1 or 5 pmol/L, as well as phospholipids or thrombin calibrators, was distributed in each well of 96-well plates, and 80 μL of test plasma was added. After the addition of 20 μL of fluorogenic substrate in HEPES buffer containing CaCl2, fluorescence was measured using a Fluoroskan Ascent fluorometer (Thermo Labsystems, Helsinki, Finland), and thrombin generation curves were calculated using the Thrombinoscope software (Thrombinoscope, Maastricht, the Netherlands). The curves were analyzed using parameters that describe the initiation, propagation, and termination phases of thrombin generation, including lag time, peak thrombin, time to peak, and ETP.
Kim Y.S., Choi J.W., Song S.H., Hwang H.Y., Sohn S.H., Kim J.S., Kang Y., Gu J.Y., Kim K.H, & Kim H.K. (2023). Comparison of the International Normalized Ratio Between a Point-of-Care Test and a Conventional Laboratory Test: the Latter Performs Better in Assessing Warfarin-induced Changes in Coagulation Factors. Annals of Laboratory Medicine, 43(4), 337-344.
Publication 2023
Blood Coagulation Factor Buffers Capillaries Centrifugation Coagulation, Blood Factor VIII Fibrinogen Fluorescence Fluorogenic Substrate HEPES Patients Phospholipids Plasma Protein C Prothrombin Sodium Citrate Tests, Blood Coagulation Thrombin Thromboplastin Veins
3
Quantification of ACE2 Activity in Tissue Lysates
ACE2 activity in tissue lysates was measured using specific fluorogenic ACE2 substrate (Mca-APK-(Dnp) (AnaSpec, San Jose, CA) in the presence or absence of the ACE2 inhibitor (MLN-4760) (Sigma-Aldrich, St. Louis, MO) as previously described [85 (link)]. Tissue samples were homogenized in lysis buffer (75 mM Tris-HCl, pH 7.5, 1 M NaCl, 0.5 mM ZnCl2, 0.01 mM Captopril, 0.1 mM Z-Pro-Prolinal, 1mM PMSF, EDTA-free inhibitor cocktail tablet from Roche, and 0.5% Triton X-100) and centrifuged at 14,000 x g for 10 minutes at 4°C. Protein concentration in tissue lysates was measured using the Bradford method. Tissue lysates (10 μg of protein for kidney extracts and 40 μg of protein for heart, lung, trachea, and sinus extracts) were pre incubated with 70 μL of assay buffer (75 mM Tris-HCl, pH 7.5, 1 M NaCl, 0.5 mM ZnCl2, 0.01 mM Captopril, 0.1 mM Z-Pro-Prolinal, and EDTA-free inhibitor cocktail tablet from Roche) with or without ACE inhibitor MLN-4760 (10 μM final) for 30 minutes at room temperature. After the incubation with ACE2 inhibitor, 30 μL of ACE2 substrate buffer (75 mM Tris-HCl, pH 7.5, 1 M NaCl, 0.5 mM ZnCl2, 0.01 mM Captopril, 0.1 mM Z-Pro-Prolinal, and 0.167 mM Mca-APK-Dpn) was added to each well to initiate the reaction. Samples were incubated in the dark for 1 hour at room temperature, and fluorescence values were measured at an excitation wavelength of 320 nm and emission wavelength of 420 nm using a BioTek Cytation5 plate reader (BioTek instruments, Winooski, VT). Results were expressed as ΔRFU (Relative Fluorescence Unit) after subtraction of RFU values obtained in the presence of MLN-4760. BALF was collected from mice as previously described, and urine was collected during necropsy.
Snouwaert J.N., Jania L.A., Nguyen T., Martinez D.R., Schäfer A., Catanzaro N.J., Gully K.L., Baric R.S., Heise M., Ferris M.T., Anderson E., Pressey K., Dillard J.A., Taft-Benz S., Baxter V.K., Ting J.P, & Koller B.H. (2023). Human ACE2 expression, a major tropism determinant for SARS-CoV-2, is regulated by upstream and intragenic elements. PLOS Pathogens, 19(2), e1011168.
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Publication 2023
ACE2 protein, human Angiotensin-Converting Enzyme Inhibitors Autopsy Biological Assay Buffers Captopril Edetic Acid Fluorescence Fluorogenic Substrate Heart Kidney Lung MLN 4760 Mus N-benzyloxycarbonylprolylprolinal Proteins Sinuses, Nasal Sodium Chloride Tablet Tissues Trachea Triton X-100 Tromethamine Urine
4
Biosensor Assay for Antimicrobial Activity
CWBIs and negative control compounds were either from Sigma–Aldrich or the sources listed in Table S2. Susceptibility testing29 was used to define appropriate concentrations of control compounds for assay. Biosensor strains were cultured in tryptone soya broth (TSB; Oxoid) at 37°C with vigorous aeration to an OD600 of 0.2 and challenged with antimicrobial agents for 60 min. In the case of biosensor constructs in Ts mutants, strains were grown at 30°C to an OD600 of 0.2, before shifting the temperature to 42°C for 60 min. Post-challenge, OD600 was measured to allow changes in cell density to be accounted for in calculating biosensor induction. An aliquot of culture (typically 200 µL) was centrifuged, and the washed cells resuspended in 0.5 volumes of AB buffer30 (link) containing lysostaphin (15 mg/L) and the fluorogenic β-galactosidase (β-gal) substrate, 4-methylumbelliferyl β-D-galactopyranoside (MUG, 500 mg/L; Sigma–Aldrich), and incubated at 25°C with shaking for 90 min. Production of β-gal was determined as described.30 (link)
Galarion L.H., Mitchell J.K., Randall C.P, & O’Neill A.J. (2023). An extensively validated whole-cell biosensor for specific, sensitive and high-throughput detection of antibacterial inhibitors targeting cell-wall biosynthesis. Journal of Antimicrobial Chemotherapy, 78(3), 646-655.
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Publication 2023
beta-Galactosidase Biological Assay Biosensors Cells Fluorogenic Substrate Galactose Lysostaphin Microbicides Soybeans Strains Susceptibility, Disease
5
Synthesis and Purification of Fluorogenic Peptide Substrates
The pentapeptide and tetrapeptide fluorogenic substrates were synthesized as described previously using the SPPS method.23 (link) All substrates were purified and analyzed on an HPLC system and dissolved in DMSO to a concentration of 20 mM.
Groborz K.M., Kalinka M., Grzymska J., Kołt S., Snipas S.J, & Poręba M. (2023). Selective chemical reagents to investigate the role of caspase 6 in apoptosis in acute leukemia T cells. Chemical Science, 14(9), 2289-2302.
Publication 2023
Fluorogenic Substrate High-Performance Liquid Chromatographies stable plasma protein solution Sulfoxide, Dimethyl

Top products related to «Fluorogenic Substrate»

1
Synergy h1 by Agilent Technologies
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The Synergy H1 is a multi-mode microplate reader designed for a variety of applications. It is capable of absorbance, fluorescence, and luminescence detection.
2
Dq gelatin by Thermo Fisher Scientific
Sourced in United States, United Kingdom
DQ gelatin is a laboratory product used for the measurement and quantification of enzymatic activity. It is a substrate that can be cleaved by specific enzymes, allowing for the assessment of their catalytic properties and function.
3
Prism 5 by GraphPad
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GraphPad Prism 5 is a data analysis and graphing software. It provides tools for data organization, statistical analysis, and visual representation of results.
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Fluoroskan ascent by Thermo Fisher Scientific
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The Fluoroskan Ascent is a microplate fluorometer and luminometer designed for sensitive and versatile fluorescence and luminescence detection. It is capable of measuring a wide range of fluorescent and luminescent assays in multi-well microplates.
5
Spectramax m5 by Molecular Devices
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The SpectraMax M5 is a multi-mode microplate reader designed for absorbance, fluorescence, and luminescence measurements. It provides a diverse range of capabilities to support various applications in life science research and drug discovery.
6
Infinite 200 pro by Tecan
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The Infinite 200 PRO is a multimode microplate reader by Tecan. It is capable of performing absorbance, fluorescence, and luminescence measurements on microplates. The instrument features a flexible filter-based optical system and uses monochromator-based technology to provide a wide wavelength range.
7
Infinite m200 by Tecan
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The Infinite M200 is a multi-mode microplate reader that provides high-performance absorbance, fluorescence, and luminescence detection. It offers precise and versatile measurement capabilities for a wide range of applications in life science research and drug discovery.
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Synergy ht by Agilent Technologies
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The Synergy HT is a multi-mode microplate reader from Agilent Technologies. It is designed to perform absorbance, fluorescence, and luminescence measurements on microplates. The Synergy HT provides reliable data for a wide range of applications, including cell-based assays, ELISA, and other microplate-based experiments.
9
Suc llvy amc by Merck Group
Sourced in United States, Italy, Germany, United Kingdom
Suc-LLVY-AMC is a fluorogenic substrate used for the detection and measurement of chymotrypsin-like activity in proteasomes. It consists of the amino acid sequence succinyl-leucine-leucine-valine-tyrosine linked to the fluorescent dye 7-amino-4-methylcoumarin (AMC). When cleaved by the chymotrypsin-like activity of the proteasome, the AMC moiety is released, resulting in a measurable fluorescent signal.
10
Fetal bovine serum (fbs) by Thermo Fisher Scientific
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.

More about "Fluorogenic Substrate"

Fluorogenic substrates are a powerful tool in biomedical research, enabling sensitive detection and quantification of enzymatic activity, cell signaling, and other dynamic cellular processes.
These chemically engineered compounds undergo a fluorescent change upon interaction with a specific target, such as an enzyme, providing a real-time readout of the biological event of interest.
Fluorogenic substrates have a wide range of applications, from monitoring the activity of proteases like caspases and matrix metalloproteinases to tracking the dynamics of second messengers like calcium and cyclic nucleotides.
They are commonly used in conjunction with fluorometric detection platforms, such as plate readers like the Synergy H1, SpectraMax M5, Infinite 200 PRO, and Infinite M200, as well as the Fluoroskan Ascent system.
When designing fluorogenic substrate experiments, researchers often optimize their protocols using resources like published literature, preprints, and patents.
AI-powered tools like PubCompare.ai can help streamline this process by conducting intelligent comparisons across these resources, identifying the most effective methods and products.
This can include exploring the use of specialized substrates like Suc-LLVY-AMC for proteasome activity or leveraging DQ gelatin to monitor matrix metalloproteinase function.
By integrating the insights from fluorogenic substrate research, scientists can take their work to new heights, unlocking a deeper understanding of complex biological systems and accelerating the development of innovative therapies and diagnostic tools.
Experince the future of research protocol enhancement with the power of PubCompare.ai.