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4-aminophenylphosphate

4-Aminophenylphospahe is a chemical compound with the formula C6H8NO2P.
It is a white crystalline solid used in various applications, such as in the synthesis of pharmaceuticals and other organic compounds.
Researchers can utilize PubCompare.ai's AI-driven platform to easily locate and compare protocols from literature, pre-prints, and patents, enabling the identification of the best methods and products for 4-aminophenylphosphate research needs.
This streamlines the research process and optimizes experiments with intelligent protocol comparison tools.

Most cited protocols related to «4-aminophenylphosphate»

1
Structural Insights into ABA Signaling Regulation
Cited 40 times
PYL2, PYL1, and HAB1 were expressed as H6-GST or H6Sumo fusion proteins in E. coli. Proteins were purified by Ni-NTA chromatography, followed by proteolytic release of tags and size-exclusion chromatography. For formation of PYL2-ABA and HAB1-PYL2-ABA complexes, ABA was mixed with PYL2 and HAB1-PYL2 at 5:1 ratios. Crystals were grown by vapor diffusion and diffraction data were collected from cryo-protected crystals at beamlines 21-ID-D and 21-ID–F at the Advanced Photon Source at Argonne National Laboratories. Structures were solved by molecular replacement in PHASER 26 (link) using the structure of the plant START protein Bet v 1 as model for PYL2 and the structure of the human PP2C PPM1B as model for HAB1. Models were manually fitted using O and Coot 27 (link),28 (link) and further refined using CNS and Refmac5 29 (link),30 (link).
Mutant proteins were expressed as H6GST-fusion proteins and purified by glutathione sepharose chromatography. Protein-protein interactions were determined by luminescence proximity AlphaScreen assay and by yeast two-hybrid assay. Biotinylated HAB1 for the luminescence proximity assay was generated by in vivo biotinylation of an avitag-HAB1 fusion protein. ABA binding was determined by scintillation proximity assay using 3H-labelled ABA. HAB1 phosphatase activity was measured by phosphate release from a SnRK2.6 phosphoprotein (Fig. 1-5) or from a generic pNPP phosphate substrate (Fig. 6b).
For transgenic studies, wildtype and mutant 35S::GFP-PYR1 constructs were transformed by the floral dip method into pyr1/pyl1/pyl2/pyl3 quadruple mutants. Mutant complementation of GFP+ seedlings was assayed by root length measurements. The ABA signal transduction pathway was reconstituted in protoplasts by transient transfection of PYL2, PP2C, SnRK2.6, and ABF2 expression plasmids. Activation of an ABA-inducible CBF3promoter-LUC reporter by PYL2 mutant proteins was determined by luciferase assays normalized for β-glucuronidase activity from a UQ10-GUS reporter. Full Methods accompany this paper at www.nature.com/nature.
Melcher K., Ng L.M., Zhou X.E., Soon F.F., Xu Y., Suino-Powell K.M., Park S.Y., Weiner J.J., Fujii H., Chinnusamy V., Kovach A., Li J., Wang Y., Li J., Peterson F.C., Jensen D.R., Yong E.L., Volkman B.F., Cutler S.R., Zhu J.K, & Xu H.E. (2009). A Gate-Latch-Lock Mechanism for Hormone Signaling by Abscisic Acid Receptors. Nature, 462(7273), 602-608.
Publication 2009
4-aminophenylphosphate Animals, Transgenic beta-Glucuronidase Biological Assay Biotinylation Chromatography Chromatography, Agarose Diffusion Escherichia coli Proteins Gel Chromatography Generic Drugs Glutathione Homo sapiens Luciferases Luminescent Measurements Mutant Proteins myotrophin Phosphates Phosphoproteins Phosphoric Monoester Hydrolases Plant Roots Plant Structures Plasmids Proteins Proteolysis Protoplasts Seedlings Signal Transduction Pathways Transfection Transients Yeast Two-Hybrid System Techniques
2
Structural Insights into ABA Signaling Regulation
Cited 40 times
PYL2, PYL1, and HAB1 were expressed as H6-GST or H6Sumo fusion proteins in E. coli. Proteins were purified by Ni-NTA chromatography, followed by proteolytic release of tags and size-exclusion chromatography. For formation of PYL2-ABA and HAB1-PYL2-ABA complexes, ABA was mixed with PYL2 and HAB1-PYL2 at 5:1 ratios. Crystals were grown by vapor diffusion and diffraction data were collected from cryo-protected crystals at beamlines 21-ID-D and 21-ID–F at the Advanced Photon Source at Argonne National Laboratories. Structures were solved by molecular replacement in PHASER 26 (link) using the structure of the plant START protein Bet v 1 as model for PYL2 and the structure of the human PP2C PPM1B as model for HAB1. Models were manually fitted using O and Coot 27 (link),28 (link) and further refined using CNS and Refmac5 29 (link),30 (link).
Mutant proteins were expressed as H6GST-fusion proteins and purified by glutathione sepharose chromatography. Protein-protein interactions were determined by luminescence proximity AlphaScreen assay and by yeast two-hybrid assay. Biotinylated HAB1 for the luminescence proximity assay was generated by in vivo biotinylation of an avitag-HAB1 fusion protein. ABA binding was determined by scintillation proximity assay using 3H-labelled ABA. HAB1 phosphatase activity was measured by phosphate release from a SnRK2.6 phosphoprotein (Fig. 1-5) or from a generic pNPP phosphate substrate (Fig. 6b).
For transgenic studies, wildtype and mutant 35S::GFP-PYR1 constructs were transformed by the floral dip method into pyr1/pyl1/pyl2/pyl3 quadruple mutants. Mutant complementation of GFP+ seedlings was assayed by root length measurements. The ABA signal transduction pathway was reconstituted in protoplasts by transient transfection of PYL2, PP2C, SnRK2.6, and ABF2 expression plasmids. Activation of an ABA-inducible CBF3promoter-LUC reporter by PYL2 mutant proteins was determined by luciferase assays normalized for β-glucuronidase activity from a UQ10-GUS reporter. Full Methods accompany this paper at www.nature.com/nature.
Melcher K., Ng L.M., Zhou X.E., Soon F.F., Xu Y., Suino-Powell K.M., Park S.Y., Weiner J.J., Fujii H., Chinnusamy V., Kovach A., Li J., Wang Y., Li J., Peterson F.C., Jensen D.R., Yong E.L., Volkman B.F., Cutler S.R., Zhu J.K, & Xu H.E. (2009). A Gate-Latch-Lock Mechanism for Hormone Signaling by Abscisic Acid Receptors. Nature, 462(7273), 602-608.
Publication 2009
4-aminophenylphosphate Animals, Transgenic beta-Glucuronidase Biological Assay Biotinylation Chromatography Chromatography, Agarose Diffusion Escherichia coli Proteins Gel Chromatography Generic Drugs Glutathione Homo sapiens Luciferases Luminescent Measurements Mutant Proteins myotrophin Phosphates Phosphoproteins Phosphoric Monoester Hydrolases Plant Roots Plant Structures Plasmids Proteins Proteolysis Protoplasts Seedlings Signal Transduction Pathways Transfection Transients Yeast Two-Hybrid System Techniques
3
SARS-CoV-2 Spike Protein ELISA Assay
Cited 11 times
Direct ELISA33 consisted of coating microtiter plates with 2 μg/ml of recombinant SARS-CoV-2 spike, S1 domain, RBD or NTD subunits. For phage ELISA, HRP-conjugated anti-M13 antibody (Sino Biological, USA, Cat# 11973-MM05T-H lot HO13AU601; used at 1:5000 working dilution) was used following detection with TMB substrate (Millipore, USA). ELISA of both sera and recombinant scFv-Fc human antibodies was applied with AP-conjugated Donkey anti-human IgG (Jackson ImmunoResearch, USA, Cat# 709-055-149 lot 130049; used at 1:2000 working dilution) following detection using PNPP substrate (Sigma, Israel).
Noy-Porat T., Makdasi E., Alcalay R., Mechaly A., Levy Y., Bercovich-Kinori A., Zauberman A., Tamir H., Yahalom-Ronen Y., Israeli M., Epstein E., Achdout H., Melamed S., Chitlaru T., Weiss S., Peretz E., Rosen O., Paran N., Yitzhaki S., Shapira S.C., Israely T., Mazor O, & Rosenfeld R. (2020). A panel of human neutralizing mAbs targeting SARS-CoV-2 spike at multiple epitopes. Nature Communications, 11, 4303.
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Publication 2020
4-aminophenylphosphate anti-IgG Antibodies, Anti-Idiotypic Bacteriophages Biopharmaceuticals Enzyme-Linked Immunosorbent Assay Equus asinus Homo sapiens isononanoyl oxybenzene sulfonate Protein Subunits SARS-CoV-2 Serum Single-Chain Antibodies Technique, Dilution
4
Isolation and Characterization of Osteosarcoma and Osteoblast Cells
Cited 6 times
The tissue (naïve chemotherapy) was immediately subjected to primary cell extraction after biopsy. Primary osteosarcoma cells were extracted by incubating minced tissue in 5 mg/ml collagenase type I solution (Gibco, MA, USA) at 37°C for 18 h. The cells were then isolated by centrifugation and cultured in 10% FBS-DMEM (Gibco). The healthy participants were patients who had been diagnosed with other, non-cancer, orthopedic conditions, and required the use of an autologous bone grafts for substitution procedure. Some bone graft was immediately subjected to perform osteoblast extraction after harvested. Osteoblasts were isolated with sequential collagenase type I-trypsin digestion. The cells were isolated and expanded in 10% FBS-DMEM (6 (link),7 (link)). The cells from the 2–4 passages were used for cellular characterization, proteomics study, and protein validation. Doubling time of primary cells was estimated using proliferation analysis by using a hemocytometer with time-course measurement. Molecular marker expression was monitored by quantitative real-time polymerase chain reaction (RT-PCR) (8 ). Collagen type I, osteonectin, bonesialoprotein were selected as the osteogenic markers. MMP-9, collagen type X were selected as the cancer markers (7 (link)). Alkaline phosphatase (ALP) activity assay was conducted kinetically by monitoring the conversion of p-nitrophenyl phosphate (pNPP) to p-nitrophenol (9 (link)). Alizarin red-S histochemistry was performed to measure mineralization ability (10 (link)). Activity of MMP-9 in the culture media was measured by gelatin zymographic assay (11 (link)).
Pruksakorn D., Teeyakasem P., Klangjorhor J., Chaiyawat P., Settakorn J., Diskul-Na-Ayudthaya P., Chokchaichamnankit D., Pothacharoen P, & Srisomsap C. (2016). Overexpression of KH-type splicing regulatory protein regulates proliferation, migration, and implantation ability of osteosarcoma. International Journal of Oncology, 49(3), 903-912.
Publication 2016
4-aminophenylphosphate 4-nitrophenol Alizarin Red S Alkaline Phosphatase Biological Assay Biological Markers Biopsy Bone Transplantation Cells Centrifugation Collagenase Collagenase, Clostridium histolyticum Collagen Type I Collagen Type X Culture Media Digestion Gelatins Healthy Volunteers Histocytochemistry Malignant Neoplasms MMP9 protein, human nitrophenylphosphate Osteoblasts Osteogenesis Osteonectin Osteosarcoma Patients Pharmacotherapy Physiologic Calcification Proteins PRSS1 protein, human Real-Time Polymerase Chain Reaction Reverse Transcriptase Polymerase Chain Reaction Tissues Trypsin
5
SARS-CoV-2 Antibody Detection Assay
Cited 5 times

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Publication 2021
4-aminophenylphosphate anti-IgA anti-IgG Antibodies Antigens COVID 19 Donors Goat Homo sapiens Patients Peroxidase Phosphates Plasma prisma Streptavidin Technique, Dilution Tweens

Most recents protocols related to «4-aminophenylphosphate»

1
Colorimetric Assay for CN Activity
CN activity was measured following a modification of the procedures as previous studies.49 (link) Briefly, the basal wells contained 25 mM MOPS (pH 7.0), 2 mM p-nitrophenol phosphate (pNPP), 1 mM DTT, 2 mM EGTA, and 2 mM EDTA. Other than that, the maximum wells contained 2 mM MnCl2. The final volumes of all wells were 100 μL. Brain region homogenate (200 μg/mL) was added to start the reaction at 37 °C for 0.5 h. The reaction was then terminated by placing on ice and OD was measured at 405 nm. The absorbance units were converted to the concentrations of p-nitrophenol (pNP) through comparing with a standard absorption curve of pNP concentration.
Han Q.T., Yang W.Q., Zang C., Zhou L., Zhang C.J., Bao X., Cai J., Li F., Shi Q., Wang X.L., Qu J., Zhang D, & Yu S.S. (2023). The toxic natural product tutin causes epileptic seizures in mice by activating calcineurin. Signal Transduction and Targeted Therapy, 8, 101.
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Publication 2023
2-nitrophenol 4-aminophenylphosphate Brain Edetic Acid Egtazic Acid manganese chloride morpholinopropane sulfonic acid Nitrophenols Phosphates
2
Antibody Avidity Assay Protocol
Antibody avidity (functional affinity), defined as the overall binding strength of an antibody to an antigen was measured by competitive inhibition45 (link). Briefly, 96 well microtiter plates were coated with 5 µg/mL of SF2a LPS incubated for 1 h at 37 °C and blocked with 150 µl of blocking buffer (containing 0.5% BSA and 0.5% Casein) for another 1 h. Double dilutions of SF2a LPS, here as free antigen, in blocking buffer were added to the microtiter plate (initial concentration 5 µg/mL). The last well was covered only with blocking buffer (control well). Sera at O.D. of approx. 1.0 at A405 were added to the wells containing free antigen or blocking buffer and plates were incubated ON. After washing plates six times, 100 µl of AP-conjugated anti-human IgG (KPL Inc. USA) was added followed by ON incubation. Wells were washed four times, 100 µl of pNPP one component substrate was added and the plates were incubated in the dark for 15 min at RT. Plates were read at 405 nm until the O.D. of control wells reaches 0.8 to 1.2. The results of relative avidity, avidity index (AI), represent the free antigen concentration that was required to inhibit antibody binding to the coated SF2a LPS wells by 50%. This value could also be expressed as the log of the free antigen concentration that is necessary to cause 50% inhibition (I50).
Meron-Sudai S., Asato V., Adler A., Bialik A., Goren S., Ariel-Cohen O., Reizis A., Mulard L.A., Phalipon A, & Cohen D. (2023). A Shigella flexneri 2a synthetic glycan-based vaccine induces a long-lasting immune response in adults. NPJ Vaccines, 8, 35.
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Publication 2023
4-aminophenylphosphate anti-IgG Antibody Avidity Antigens Buffers Cardiac Arrest Caseins Homo sapiens Immunoglobulins Psychological Inhibition Serum Technique, Dilution
3
ELISA Detection of Serum IgG and IgA Antibodies
Serum IgG and IgA antibodies were measured by an ELISA in-house protocol. Briefly, 96 well microtiter plates (Corning) were coated with 5 µg/mL of SF2a LPS (extracted from SF2a 454) in carbonate buffer for 1 h at 37 °C. Unbound sites were blocked with 150 µl of blocking buffer containing 0.5% bovine serum albumin (BSA) (Merck Millipore Corp.) and 0.5% Casein for 1 h at 37 °C. Wells were washed twice (PBS Tween) and duplicates of tested samples were serially 2-fold diluted (initial dilution 1:200) in blocking buffer, added to the wells and incubated overnight (ON) at room temperature (RT). Plates were washed four times and 100 µl/well of alkaline phosphatase (AP) conjugated anti-human IgG or IgA (KPL, Inc. USA) was added and incubated ON at RT. Wells were washed four times and 100 µl/well of phosphatase substrate, para-nitrophenyl phosphate (pNPP) one component (SouthernBiotech) was added and plates were incubated in the dark for 15 min at RT. The reaction was stopped by the addition of 50 µl/well of Stop solution (3 M NaOH). Absorbance was measured at 405 nm using an ELISA plate reader (Multiskan FC, Thermo Scientific). Results were expressed in endpoint titers (the last serum dilution yielding an optical density (O.D.) of 0.2 or higher).
Meron-Sudai S., Asato V., Adler A., Bialik A., Goren S., Ariel-Cohen O., Reizis A., Mulard L.A., Phalipon A, & Cohen D. (2023). A Shigella flexneri 2a synthetic glycan-based vaccine induces a long-lasting immune response in adults. NPJ Vaccines, 8, 35.
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Publication 2023
4-aminophenylphosphate 4-nitrophenyl Alkaline Phosphatase anti-IgG Carbonates Cardiac Arrest Caseins Enzyme-Linked Immunosorbent Assay Homo sapiens Immunoglobulin A Phosphates Phosphoric Monoester Hydrolases Serum Serum Albumin, Bovine Technique, Dilution Tweens
4
Standardized Anti-Nucleosome and Anti-RNA ELISAs
Anti-nucleosome ELISAs were performed by coating Immulon 2HB plates with 10 μg/ml poly-L-lysine (Sigma-Aldrich) in PBS. Plates were washed and coated with 15 μg/ml dsDNA prepared by digestion of calf thymus DNA (Sigma-Aldrich) with S1 nuclease (Promega) for 30 min at 37 deg followed by ethanol precipitation. Plates were subsequently washed and coated with 10 μg/ml calf thymus histones type IIAS (Sigma-Aldrich). Plates were blocked with ELISA buffer (1× PBS 1% BSA 0.05% sodium azide) and serum samples diluted 1:200 in the same buffer were applied to the top row and diluted threefold down the plate down to 1:5,400. Bound antibody was detected with alkaline-phosphatase conjugated goat anti-mouse IgG (Southern Biotech) or goat anti-mouse IgG2a (Southern Biotech) and developed with pNPP (Sigma-Aldrich). Autoantibody concentrations were determined relative to PL2-3 anti-nucleosome monoclonal antibody standard using DeltaSoft 2.8.11 software (Biometallics). Anti-RNA ELISAs were performed in a similar fashion, except plates were coated first with poly-L-lysine then with 15 μg/ml total yeast RNA (Sigma-Aldrich) before blocking and concentrations were determined relative to BWR4 standard. Total IgG and IgM ELISAs were performed by coating plates with unconjugated goat anti-mouse IgG or IgM antibody (Southern Biotech), followed by serum sample diluted 1:10,000 (IgM) or 1:50,000 (IgG) in the top row, followed by goat anti-mouse IgG-AP or IgM-AP (Southern Biotech), relative to purified IgG or IgM standards.
Nickerson K.M., Smita S., Hoehn K.B., Marinov A.D., Thomas K.B., Kos J.T., Yang Y., Bastacky S.I., Watson C.T., Kleinstein S.H, & Shlomchik M.J. (2023). Age-associated B cells are heterogeneous and dynamic drivers of autoimmunity in mice. The Journal of Experimental Medicine, 220(5), e20221346.
Publication 2023
4-aminophenylphosphate Alkaline Phosphatase anti-IgG Autoantibodies Buffers calf thymus DNA Digestion DNA, Double-Stranded Enzyme-Linked Immunosorbent Assay Ethanol Goat Histones IgG2A Immunoglobulin M Immunoglobulins Lysine Mice, House Monoclonal Antibodies Nucleosomes Poly A Promega Serum Sodium Azide Thymus Plant Yeast, Dried
5
ELISA for Gut Immunoglobulins
Immunoglobulins in the culture supernatants or luminal gut were measured by direct ELISA. Briefly, samples or standards were used to coat the 96-well plate overnight at 4°C. After washing and blocking (1-hr, RT) with 1% BSA in PBS on a shaking platform (400 rpm), the samples were then incubated with AP–conjugated goat anti-mouse IgA, IgG or IgM (Southern Biotech, Birmingham, AL, USA) for 2-hrs RT on a shaking platform). Samples were subsequently washed and PNPP substrate (Sigma-Aldrich) was added. The reaction was stopped upon addition of 1M NaOH. Samples were analyzed on a microplate spectrophotometer (Perkin Elmer) at 405 nm (OD). Antibody concentrations were determined by linear regression of standard curves.
Pearson J.A., Peng J., Huang J., Yu X., Tai N., Hu Y., Sha S., Flavell R.A., Zhao H., Wong F.S, & Wen L. (2023). NLRP6 deficiency expands a novel CD103+ B cell population that confers immune tolerance in NOD mice. Frontiers in Immunology, 14, 1147925.
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Publication 2023
4-aminophenylphosphate anti-IgA Enzyme-Linked Immunosorbent Assay Goat Immunoglobulins Mus Phenobarbital

Top products related to «4-aminophenylphosphate»

1
P nitrophenyl phosphate pnpp by Merck Group
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P-nitrophenyl phosphate (pNPP) is a colorless, water-soluble compound used as a substrate in various analytical and diagnostic applications. It serves as a versatile tool for the detection and quantification of enzymatic activity, particularly phosphatase enzymes. The hydrolysis of pNPP by phosphatases results in the formation of a yellow-colored product, p-nitrophenol, which can be measured spectrophotometrically to determine the enzyme's activity.
2
Pnpp substrate by Merck Group
Sourced in Israel, United States, Germany
PNPP substrate is a colorimetric substrate used in enzyme-linked immunosorbent assay (ELISA) applications. It serves as a detection reagent, producing a color change when acted upon by the target enzyme.
3
Sensolyte pnpp alkaline phosphatase assay kit by AnaSpec
Sourced in United States, Belgium
The SensoLyte® pNPP Alkaline Phosphatase Assay Kit is a colorimetric assay used for the detection and quantification of alkaline phosphatase activity. The kit utilizes the substrate p-nitrophenyl phosphate (pNPP), which is hydrolyzed by alkaline phosphatase to produce a yellow-colored product that can be measured spectrophotometrically.
4
Bovine serum albumin (bsa) by Merck Group
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
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P nitrophenyl phosphate by Merck Group
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P-nitrophenyl phosphate is a colorless crystalline compound used as a substrate in various biochemical assays. It is commonly used in enzyme-linked immunosorbent assays (ELISA) and other colorimetric detection methods to measure the activity of phosphatase enzymes.
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Triton x 100 by Merck Group
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Triton X-100 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent and solubilizing agent, facilitating the solubilization and extraction of proteins and other biomolecules from biological samples.
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Microplate reader by Bio-Rad
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The Microplate reader is a laboratory instrument used to measure the absorbance or fluorescence of samples in a microplate format. It can be used to conduct various assays, such as enzyme-linked immunosorbent assays (ELISA), cell-based assays, and other biochemical analyses. The core function of the Microplate reader is to precisely quantify the optical properties of the samples in a multi-well microplate.
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Microplate reader by Agilent Technologies
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The Microplate reader is a versatile laboratory instrument used to measure and analyze the optical properties of samples in microplates. It is designed to quantify absorbance, fluorescence, or luminescence signals from various assays and applications.
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β glycerophosphate by Merck Group
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β-glycerophosphate is a chemical compound that serves as a buffering agent and source of phosphate for cell culture media. It helps maintain a stable pH environment for cell growth and proliferation.
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Dexamethasone (dex) by Merck Group
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Dexamethasone is a synthetic glucocorticoid medication used in a variety of medical applications. It is primarily used as an anti-inflammatory and immunosuppressant agent.

More about "4-aminophenylphosphate"

4-Aminophenylphosphate, also known as 4-APP or 4-aminophenyl phosphate, is a chemical compound with the formula C6H8NO2P.
It is a white crystalline solid that has various applications, particularly in the synthesis of pharmaceuticals and other organic compounds.
Researchers can utilize the AI-driven platform PubCompare.ai to easily locate and compare protocols from literature, preprints, and patents, enabling the identification of the best methods and products for 4-aminophenylphosphate research needs.
This streamlines the research process and optimizes experiments with intelligent protocol comparison tools. 4-APP is closely related to P-nitrophenyl phosphate (pNPP), a commonly used substrate for alkaline phosphatase assays.
The SensoLyte® pNPP Alkaline Phosphatase Assay Kit, for example, utilizes pNPP to measure alkaline phosphatase activity.
Bovine serum albumin (BSA) is often used as a stabilizing agent in these assays, while Triton X-100 is a detergent that can be employed to solubilize membrane-bound alkaline phosphatases.
Beyond its use in assays, 4-aminophenylphosphate can also be involved in the synthesis of other organic compounds, such as those containing the β-glycerophosphate moiety.
This compound is particularly relevant in the context of dexamethasone, a synthetic glucocorticoid that is commonly used in cell culture experiments to induce the differentiation of pre-adipocytes into mature adipocytes.
By incorporating synonyms, related terms, abbreviations, and key subtopics, researchers can optimize the discoverability and relevance of their 4-aminophenylphosphate-related content through search engine optimization (SEO).
This enhanced visibility can help streamline the research process and facilitate the identification of the most suitable protocols and methods for their specific needs.