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Prostaglandin M

Prostaglandin M is a primary metabolite of prostaglandin E2 (PGE2) and serves as a stable biomarker for PGE2 production in the body.
It is an important indicator of inflammation and can be used to assess the efficacy of anti-inflammatory therapies.
Accurate measurement of Prostaglandin M levels is crucial for researchers studying the role of prostaglandins in various physiological and pathological processes.
PubCompare.ai can help optimize your Prostaglandin M research protocols by providing easy access to reproducible and reliable methods from the literature, preprints, and patents.
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Most cited protocols related to «Prostaglandin M»

Cell culture and generation of stable cell lines. Human bronchial epithelial BEAS-2B cells [American Type Culture Collection (ATCC), Manassas, VA, USA] were cultured in DMEM (Dulbecco’s modified Eagle’s medium; Invitrogen, Carlsbad, CA, USA) supplemented with 10% fetal bovine serum (FBS). Human umbilical vein endothelial cells (HUVEC) (purchased from ATCC) were cultured in EBM-2 (endothelial basal medium-2) complete medium. Arsenic-transformed BEAS-2B (AsT) cells (Carpenter et al. 2011 (link)) stably overexpressing miR-199a or miR-control were generated by infecting BEAS-2B cells with lentivirus carrying miR-199a-RFP or a negative control precursor (Applied Biosystems, Carlsbad, CA, USA), followed by selection with puromycin. To establish stable cell lines overexpressing COX-2 (cyclooxygenase-2), 293T cells were transfected with lentivirus carrying the COX-2 plasmid (GeneCopoeia, Rockville, MD, USA) or an empty vector to generate infectious virus. Then AsT cells were transduced with virus, followed by the puromycin selection. We also prepared PI3K (phosphatidylinositide 3-kinase)–transformed chicken embryo fibroblast cells as was previously described (Chang et al. 1997 (link); Jiang et al. 2000 (link)).
Animal experiment. Female CrTac:NCr-Foxn1nu mice (8 weeks of age) were purchased from Taconic (Hudson, NY, USA), and maintained in pathogen-free conditions. Animals were housed in sterilized cages (5 mice/cage) with hardwood chip bedding. Standardized commercial diets were provided, and sterilized water was available at all times. The average weight of animals on arrival was 20 ± 2 g (mean ± SD). A total of 2 × 106 AsT/miR-cont cells or AsT/miR-199a cells (AsT cells stably overexpressing miR-control or miR-199a, respectively) in 80 μL were injected subcutaneously into the flanks of nude (nu/nu) mice (n = 10/group). The animals used in research were treated humanely according to the Institutional Animal Care and Use Committee of Thomas Jefferson University. The mice were euthanized by decapitation 6 weeks after injection. Tumor tissues were removed and weighed. Parts of tissues were paraffin-embedded, and other parts were snap-frozen in liquid nitrogen and stored at –80°C for immunohistochemical analysis.
Reagents and antibodies. Sodium arsenic, catalase, and H2O2 were purchased from Sigma-Aldrich (St. Louis, MO, USA). Small interfering RNA (siRNA) Smartpools (pools of four individual siRNAs) against COX-2, HIF-1α (hypoxia inducible factor 1, alpha), and a scrambled control were purchased from Dharmacon (Lafayette, CO, USA). COX-2 antibody was from Cell Signaling Technology (Beverly, MA, USA). CD31 (platelet/endothelial cell adhesion molecule 1) antibody for analyzing paraffin-embedded tissues was from Santa Cruz Biotechnology (Santa Cruz, CA, USA) and for analyzing frozen tissues, from BD Pharmingen (San Jose, CA, USA). HIF-1α antibody was from BD Biosciences (Franklin Lakes, NJ, USA), and α-SMA (smooth muscle α-actin) antibody was obtained from Abcam (Cambridge, MA, USA). Primary antibodies used for Western analysis were diluted 1:1,000 in 5% bovine serum albumin as a working concentration and were incubated on a shaker overnight at 4°C.
RT-qPCR analysis. Total RNAs were extracted using Trizol (Life Technologies, Carlsbad, CA, USA). The synthesis of cDNA was performed using oligo (dT)18 primers and M-MLV (Moloney Murine Leukemia Virus) reverse transcriptase (Promega, Madison, WI, USA). The amplification was performed by polymerase chain reaction (PCR). SYBR-green reverse transcription PCR (RT-qPCR) was performed to detect COX-2 and GADPH (glyceraldehyde-3-phosphate dehydrogenase) mRNA levels using the Power SYBR Green PCR Master Mix Kit (Applied Biosystems). Taqman RT-qPCR was performed to detect miRNA expression levels using the Taqman miRNA Reverse Transcription kit and Taqman universal PCR Master Mix (Applied Biosystems). The sequences of primer used for SYBR-green RT-qPCR were as follows:
Immunohistochemistry and immunofluorescence. Paraffin-embedded tissue sections and frozen tissue sections were prepared by routine methods (Fero Lab, Fred Hutchinson Cancer Research Center 2011 ). For immunohistochemistry, the Dako Envision two-step method of immunohistochemistry was used to stain CD31 (1:100 dilution) and α-SMA (1:150 dilution) in xenograft tumor tissues as described previously (He et al. 2012a (link)). Tissue sections were incubated with primary antibodies in a humid chamber overnight at 4°C. The microvessel density reflected by CD31-positive staining was counted in three different fields per section. For immunofluorescence staining, frozen sections were incubated with primary antibodies overnight. Goat anti-rabbit or anti-mouse IgG conjugated with fluorescein isothiocyanate or Texas Red (both from Santa Cruz Biotechnology) (1:200 dilution) were used as secondary antibodies and incubated for 2 hr at room temperature. Slides were mounted with anti-fade DAPI reagent (Invitrogen, Grand Island, NY, USA).
Chromatin immunoprecipation (ChIP)–quantitative PCR (qPCR). ChIP-qPCR was performed using the EpiTect ChIP OneDay Kit (QIAGEN, Valencia, CA, USA) according to the manufacturer’s instructions. HIF-1α antibody (Abcam) was used to pull down the protein–chromatin complexes. Rabbit IgG was used as a negative control. The immunoprecipated DNA was quantified using SYBR Green qPCR (Applied Biosystems). All results were normalized to 1% input value of the same sample. COX-2 primers flanking the hypoxia-response elements (HRE) for SYBR Green qPCR were as follows:
Prostaglandin E2 (PGE2) ELISA. Cells were plated at 0.1 × 106 cells/well of a 24-well plate and allowed to recover overnight. The following day, the media were replaced with fresh media, and then the cells were cultured in normoxia or hypoxia (1% O2) for 24 hr. The conditioned media were then collected and cleared of cellular debris by centrifugation at 2,000 rpm for 2 min. PGE2 concentrations were determined using the Prostaglandin E2 EIA Kit–Monoclonal ELISA kit (no. 514010; Cayman Chemical, Ann Arbor, MI, USA) according to the manufacturer’s instructions.
miRNA luciferase reporter constructs and luciferase activity assay. The 3´UTR-luciferase reporter constructs containing the 3´UTR regions of COX-2 with wild-type and mutant binding sites of miR-199a were amplified using the PCR method (GoTaq® G2 Flexi DNA Polymerase; Promega) according to the manufacturer’s instructions. The PCR products were cloned into the pMiR-luc luciferase reporter vector (Ambion, Grand Island, NY, USA). The mutant 3´UTR constructs were made by introducing four point mutations into the putative seed regions of COX-2. All the constructs containing 3´UTR inserts were sequenced and verified. The luciferase activity assay was performed as previously described (He et al. 2013a (link)).
Site-directed mutagenesis. The human full-length COX-2 reporter used was a generous gift from J. Li (Harvard University, Boston, MA, USA) (Wu et al. 2006 (link)). To generate the HRE-mutant COX-2 reporter, we performed site-directed mutagenesis on the wild-type COX-2 reporter at the potential HIF-1α binding sites with 3 base pair substitutions as previously described (Jiang et al. 1996 (link)). The mutant COX-2 reporter construct was validated by DNA sequencing.
Tube formation assay. HUVEC were cultured in EBM-2 complete medium, and switched to EBM-2 basal medium containing 0.2% FBS for 24 hr before performing the tube formation assay. The conditioned media were prepared from different cells by replacing normal culture medium with serum-reduced medium (1% FBS). After culture for 24 hr, the serum-reduced media were collected and stored at –20°C for later use. The HUVEC were trypsinized, counted, and resuspended in EBM-2 basic medium; then they were mixed with an equal volume of the conditioned medium and seeded on Matrigel-pretreated 96-well plates at 2 × 104 cells/well. After culture for 6-12 hr, tube formation was observed under a light microscope and photographed. The total lengths of the tubes in each well were measured using CellSens Standard software (Olympus; Hamburg, Germany).
The chorioallantoic membranes (CAM) assay. White Leghorn fertilized chicken eggs (Charles River, Malvern, PA, USA) were incubated at 37°C under constant humidity. Cells were transfected with miRNA precursors, or treated as specifically indicated in the figure legends. After transfection for 12 hr, the cells were trypsinized, counted, and resuspended in the serum-free medium. The cell suspensions were mixed with Matrigel at a 1:1 ratio, and implanted onto the CAM of chicken eggs on day-9 embryos. Tumor angiogenesis responses were analyzed 5 days after the implantation. The tumor/Matrigel plugs were trimmed off the CAM and photographed. The number of blood vessels as the index of angiogenesis was analyzed by counting the branches of blood vessels in three representative areas (each 1.0 mm2) by two observers in a double blind manner.
miRNA transfection. Cells were cultured in 6-well plates to reach a 60% confluency, and transfected using miR-199a or a negative-control precursor (both from Applied Biosystems) at 30 nM using Lipofectamine RNAiMAX reagent (Invitrogen, Grand Island, NY, USA) according to the manufacturer’s instructions. Total proteins and RNAs were prepared from the cells 60–70 hr after the transfection, followed by Western blotting or RT-PCR analysis.
Hypoxia treatment. A hypoxia incubator chamber (Stemcell, Vancouver, British Columbia, Canada) was used to generate the hypoxia environment for cell culture. Cells were cultured in hypoxia conditions (1% O2) for 24 hr at 37°C.
Reactive oxygen species (ROS) study. Cells were treated with ROS scavenger catalase (1,500 U) or with H2O2 (50 μM) for 12 hr. Then cells were harvested, and total proteins were extracted for Western blotting analysis.
Statistical analysis. All the results were obtained from at least three independent experiments. Results are presented as mean ± SE and were analyzed by Student’s t-test or one-way analyis of variance (ANOVA). All results were analyzed by SPSS for Windows, version 11.5 (IBM, Chicago, IL, USA). Differences were considered significant with p < 0.05.
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Publication 2014
Osteoblasts obtained from the calvaria of newborn ddY mice and bone marrow cells from ddY mice were cocultured in αMEM containing 10% fetal bovine serum, 1α,25-dihydroxyvitamin D3 [1α,25(OH)2D3] (10−8 M) (Wako Pure Chemical Co.), and prostaglandin E2 (10−6 M) (Sigma Chemical Co.) in 100-mm–diameter dishes coated with Type I collagen gels (Nitta Gelatin Co.) as described previously 38. Osteoclasts formed within 6 d were recovered from the dishes by treating with 0.2% collagenase (crude osteoclasts). To purify osteoclasts, the crude osteoclast preparation was replated and cultured for 8 h. Osteoblasts were then removed by treating with PBS containing 0.001% pronase E and 0.02% EDTA 38. Some of the cultures were then stained for TRAP. The other cultures were further incubated for 36 h in the presence or absence of mouse TNF-α (20 ng/ml), human TNF-α (20 ng/ml), IL-1α (10 ng/ml), or sODF/sRANKL (100 ng/ml), and stained for TRAP. TRAP-positive multinucleated cells containing more than three nuclei were counted as living osteoclasts.
Publication 2000
Bone Marrow Cells Calvaria Cell Nucleus Cells Collagen Type I dihydroxy-vitamin D3 Dinoprostone Edetic Acid Fetal Bovine Serum Gelatins Gels Homo sapiens Hyperostosis, Diffuse Idiopathic Skeletal Infant, Newborn Mus Neutrophil Collagenase Osteoblasts Osteoclasts Pronase E Tumor Necrosis Factor-alpha
Male adult Sprague-Dawley rats (200–250 g) were housed in Plexiglass cages (40 cm × 25 cm × 15 cm), two rats per cage, in climatized colony rooms (22 ± 1 °C; 60% humidity), on a 12 h/12 h light/dark cycle (light phase: 07:00–19:00 h), with free access to tap water and food, 24 h/day throughout the study, with no fasting periods. Rats were fed a standard laboratory diet (3.5% fat, 63% carbohydrate, 14% protein, 19.5% other components without caloric value; 3.20 kcal/g).
Housing conditions and experimentation procedures were strictly in accordance with the European Union ethical regulations on the care of animals for scientific research.
According to the recognized ethical principles of “Replacement, Refinement, and Reduction of Animals in Research”, colon, liver, heart, and prefrontal cortex specimens were obtained as residual material from vehicle-treated rats randomized in our previous experiments approved by the Local Ethical Committee of University “G. d’Annunzio” and the Italian Health Ministry (Italian Health Ministry authorization N. 880, delivered on 24th August 2015). Rats were sacrificed by CO2 inhalation (100% CO2 at a flow rate of 20% of the chamber volume per min) and colon, liver, heart, and prefrontal cortex specimens were immediately collected and maintained in a humidified incubator with 5% CO2 at 37 °C for 4 h, in DMEM buffer with added bacterial LPS (10 μg/mL) (incubation period).
During the incubation period, tissues were treated with scalar concentrations of MOMAST(®) HY100 (10, 50, and 100 µg/mL) and MOMAST(®) HP30 (22, 110, and 220 µg/mL). Tissue supernatants were collected, and the PGE2 and 8-iso-PGF levels (ng/mg wet tissue) were measured by radioimmunoassay (RIA), as previously reported [13 (link),53 (link)]. Briefly, specific anti-8-iso-PGF and anti-PGE2 were developed in the rabbit; the cross-reactivity against other prostanoids is <0.3%. One hundred microliters of prostaglandin standard or sample were incubated overnight at 4 °C with the 3H-prostaglandin (3000 cpm/tube; NEN) and antibody (final dilution: 1:120,000; kindly provided by Prof. G. Ciabattoni), in a volume of 1.5 mL of 0.025 M phosphate buffer. Free and antibody-bound prostaglandins were separated by the addition of 100 μL 5% bovine serum albumin and 100 μL 3% charcoal suspension, followed by centrifuging for 10 min at 4,000× g at 5 °C and decanting off the supernatants into scintillation fluid (Ultima Gold™, Perkin Elmer, Waltham, MA, USA) for β emission counting. The detection limit of the assay method was 0.6 pg/mL. Additionally, tissue supernatants were assayed for lactate dehydrogenase (LDH) activity [54 (link)]. LDH activity was measured by evaluating the consumption of nicotinamide adenine dinucleotide dehydrogenase (NADH) in 20 mM HEPES-K+ (pH 7.2), 0.05% bovine serum albumin, 20 μM NADH, and 2mM pyruvate using a microplate reader (excitation 340 nm, emission 460 nm) according to manufacturer′s protocol (Sigma-Aldrich, St. Louis, MO). LDH activity was measured by evaluating the consumption of NADH in 20 mM HEPES-K+ (pH 7.2), 0.05% bovine serum albumin, 20 μM NADH and 2 mM pyruvate using a microplate reader (excitation 340 nm, emission 460 nm) according to manufacturer′s protocol. In addition, individual prefrontal cortex, colon, liver, and heart specimens were quickly dissected to evaluate cyclooxygenase (COX)-2, tumor necrosis factor α (TNFα), and inducible nitric oxide synthase (iNOS) gene expression, as previously reported [55 (link),56 (link)]. Tissue specimens were dissected and stored in RNAlater solution (Life Technologies, Carlsbad, CA, USA) at −20 °C until further processed. Total RNA was extracted from the tissues using TRI Reagent (Sigma-Aldrich, St. Louis, MO, USA) according to manufacturer’s protocol. One microgram of total RNA extracted from each sample in a 20-μL reaction volume was reverse transcribed using a high capacity cDNA reverse transcription kit (Life Technologies, Carlsbad, CA, USA). Reactions were incubated in a 2720 thermal cycler (Life Technologies, Carlsbad, CA, USA) initially at 25 °C for 10 min, then at 37 °C for 120 min, and finally at 85 °C for 5 s. Gene expression was determined by quantitative real-time PCR using TaqMan probe-based chemistry (Life Technologies, Carlsbad, CA, USA). Reactions were performed in MicroAmp Fast Optic 96-well Reaction Plates (Life Technologies, Carlsbad, CA, USA) on an ABI PRISM 7900 HT fast real-time PCR system (Life Technologies, Carlsbad, CA, USA). PCR primers and TaqMan probes were obtained from Life Technologies (Assays-on-Demand Gene Expression Products, Rn01483828_m1 for COX-2 gene, Rn01525859_g1 for TNFα, Rn00561646_m1 for iNOS. β-actin (Life Technologies, Carlsbad, CA, USA, Part No. 4352340E) was used as the housekeeping gene. The real-time PCR was carried out in triplicate. Data were elaborated with the sequence detection system (SDS) software version 2.3 (Applied Biosystems, Foster City, CA, USA). The comparative 2−ΔΔCt method was used to quantify the relative abundance of mRNA and then determine the relative changes in individual gene expression (relative quantification) [57 (link)].
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Publication 2019
Cyclooxygenase activity of ovine COX-1 or human COX-2 was assayed by a method that quantifies conversion of [1-14C]arachidonic acid to [1-14C]prostaglandin products. Reaction mixtures of 200 µL consisted of hematin-reconstituted protein in 100 mM Tris-HCl, pH 8.0, 500 µM phenol, and [1-14C]arachidonic acid (50 µM, ~55–57 mCi/mmol, Perkin Elmer). For the time-dependent inhibition assay, hematin-reconstituted COX-1 (44 nM) or COX-2 (66 nM) was preincubated at 25°C for 17 min and 37 °C for 3 min with varying inhibitor concentrations in DMSO followed by the addition of [1-14C]arachidonic acid (50 µM) for 30 s at 37 °C. Reactions were terminated by solvent extraction in Et2O/CH3OH/1 M citrate, pH 4.0 (30:4:1). The phases were separated by centrifugation at 2000g for 2 min and the organic phase was spotted on a TLC plate (EMD Kieselgel 60, VWR). The plate was developed in EtOAc/CH2Cl2/glacial AcOH (75:25:1) at 4 °C. Radiolabeled products were quantified with a radioactivity scanner (Bioscan, Inc., Washington, D.C.). The percentage of total products observed at different inhibitor concentrations was divided by the percentage of products observed for protein samples preincubated for the same time with DMSO.
Publication 2010
Arachidonic Acid Biological Assay Centrifugation Citrate Hematin Homo sapiens Phenol Prostaglandin-Endoperoxide Synthase Prostaglandins Proteins Psychological Inhibition PTGS1 protein, human PTGS2 protein, human Radioactivity Sheep Solvents Sulfoxide, Dimethyl Tromethamine
C57Bl/6 and OPN−/− mice were purchased from Jackson Laboratories. B6.SJL-PtrcAPep3B/BoyJ mice were bred in-house. CXCR4flox/flox mice were generated as described 23 (link) and were a kind gift from Y. Zou, Columbia University. EP1−/−, EP2−/−, EP3−/−, and EP4flox/flox mice were generated as described 24 (link)–26 (link). Conditional mice were bred to Ubc-Cre/ERT2 mice from Jackson. Female olive baboons, Papio anubis, were housed individually in conventional caging of the Biological Resources Laboratory, University of Illinois (UI) at Chicago. Primate research was approved by the UI Animal Care and Use Committee (IACUC). The IACUC of IUSM approved all protocols. The IRB of IUSM approved human subject research and informed consent was acquired from all volunteers.
Publication 2013
Animals Biopharmaceuticals Females Homo sapiens Institutional Animal Care and Use Committees Mice, House mitogen-activated protein kinase 3, human Papio anubis Primates Voluntary Workers

Most recents protocols related to «Prostaglandin M»

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Chemical treatments were adapted from previously described studies (Marra et al., 2019a; Chambers et al., 2020; Wesselman et al., 2023) (link). In short, 16,16-Dimethyl-prostaglandin E2 (Santa Cruz Biotechnology) was dissolved in 100% DMSO (American Bioanalytical) to create 1 M stock. Then 1 M stock was diluted to the treatment dose. Treatments were performed in triplicate with n > 30 embryos per replicate.
Publication 2024
Fresh mulberry (M. alba) leaves were collected from the Ondo State Ministry of Agriculture Sericulture Centre, Akure while fresh P. maximum was sourced from the pasture within the FUTA campus. The experimental concentrate was formulated using dried crushed cassava peel with other feed ingredients such as wheat offal, brewer-dried grains, palm kernel cake (PKC), bone meal, premix and salt. Five diets T1, T2, T3, T4 and T5 were made to contain 100 % P. maximum (P100M0), 75 % P. maximum + 25% M. alba (P75M25), 50 % P. maximum + 50 % M. alba (P50M50), 25 % P. maximum + 75 % M. alba (P25M75) and 100 % M. alba (P0M100) respectively.
Experimental Layout and Animal Management: Twenty-five (25) pregnant WAD does aged two years and weighing between 10 -13 kg were used in this study. The goats were randomly distributed into five treatment groups replicated five times with one goat per replicate using the completely randomised experimental design, Experimental diets and water were offered ad libitum and the concentrate was given at a constant rate (350 g/day). The goats were synchronised using prostaglandin (PGF2) at 1 Ml/10kg intramuscularly to bring all the animals to oestrous and were then exposed to a proven buck for mating.
Publication 2024

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Publication 2024
We studied the records of neonates with IAA of all types who underwent immediate postnatal echocardiogram while receiving prostaglandin E1 infusion in Nemours Cardiac Center of Nemours Children's Hospital, Delaware and Division of Cardiology at Nemours Children's Hospital, Florida from 2011 to 2022. Those with other associated structural abnormalities (e.g., truncus arteriosus), single ventricle anatomy (e.g., hypoplastic left heart syndrome), and additional aortopulmonary connections besides PDA (e.g., aortopulmonary window) were excluded. In addition to demographic data, sex, gestational age (weeks), birth weight (kg), and body surface area (BSA; m 2 ), anatomical diagnosis including aortic arch sidedness and presence of ASCA were obtained by comprehensive echocardiographic evaluation. An incidence of chromosomal anomaly (chromosome 22q11 deletion) and all causes of mortality were retrieved from the patients' medical records.
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Cytokine levels in cell culture supernatants were measured by sandwich ELISA. Microtiter plates (Costar EIA/RIA plates, Corning) were coated with a cytokine-speci c antibody. Expression levels of IL-6 and IL-10 were measured according to the manufacturer's instructions (OptEIA Sets, BD Biosciences). TNF-α level was measured according to the manufacturer's instructions (ELISA uncoated kits, Invitrogen, Waltham, MA, USA). In all cases, 10% FBS in PBS was used as a blocking solution. TMB substrate solution (Invitrogen) was used to develop a colorimetric reaction, which was stopped with 2 M sulfuric acid. Optical density was measured at 450 (570) nm using a microtiter plate reader (PowerWaveX, Bio-Tek Instruments, Winooski, VT, USA).
Prostaglandin E2 (PGE2) immunoassay PGE 2 concentration in cell supernatants was determined by a PGE2 high-sensitivity ELISA kit (Enzo Life Sciences, Farmingdale, NY, USA), according to the manufacturer's protocol.
Publication 2024

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More about "Prostaglandin M"

Prostaglandin M, also known as 15-keto-prostaglandin E2, is a primary metabolite of prostaglandin E2 (PGE2) and serves as a stable biomarker for PGE2 production in the body.
It is an important indicator of inflammation and can be used to assess the efficacy of anti-inflammatory therapies.
Accurate measurement of Prostaglandin M levels is crucial for researchers studying the role of prostaglandins in various physiological and pathological processes, such as cardiovascular health, cancer, and neurological disorders.
Prostaglandins are lipid signaling molecules that play a key role in a wide range of biological processes, including vasodilation, platelet aggregation, and the inflammatory response.
PGE2 is one of the most well-studied prostaglandins and is known to be involved in the regulation of various physiological and pathological processes.
Researchers often use Prostaglandin M as a proxy for PGE2 levels, as it is more stable and easier to measure than PGE2 itself.
This makes Prostaglandin M an important tool for studying the role of prostaglandins in various disease states and the efficacy of anti-inflammatory therapies.
PubCompare.ai can help streamline your Prostaglandin M research by providing easy access to reproducible and reliable methods from the literature, preprints, and patents.
Our AI-driven platform allows you to quickly locate and compare protocols, ensuring that you can identify the most suitable approach for your research needs.
Whether you're using FBS, RNeasy Mini Kit, Prostaglandin E2, TRIzol reagent, TRIzol, Penicillin/streptomycin, Prism 8, High-Capacity cDNA Reverse Transcription Kit, Indomethacin, or Penicillin, PubCompare.ai can help you streamline your Prostaglandin M research and ensure the accuracy and reproducibility of your results.