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Polyethylene glycol 3350

Polyethylene Glycol 3350 is a commonly used osmotic laxative and bowel preparation agent.
It is a polyether compound with a typical molecular weight of 3,350 Daltons, composed of repeating ethylene glycol units.
PEG 3350 works by drawing water into the intestines, softening stool and facilitating bowel movements.
It is used to treat constipation and prepare the bowel for medical procedures.
Reserachers can optimize the use of PEG 3350 with the help of PubCompare.ai, an AI-driven tool that identifies the most accurate and reproducible protocols from literature, preprints, and patents.
With intelligent comparisons, PubCompare.ai ensures reserachers find the best products and procedures to enhance their effeciency.

Most cited protocols related to «Polyethylene glycol 3350»

Structural Determination of CRISPR-Cas9 Complexes

Cited 31 times

Full details of experimental procedures are provided in the supplementary materials. SpyCas9 and its point mutants were expressed in Escherichia coli Rosetta 2 strain and purified essentially as described (8 (link)). SpyCas9 crystals were grown using the hanging drop vapor diffusion method from 0.1 M tris-Cl (pH 8.5), 0.2 to 0.3 M Li₂SO₄, and 14 to 15% (w/v) PEG 3350 (polyethylene glycol, molecular weight 3350) at 20°C. Diffraction data were measured at beamlines 8.2.1 and 8.2.2 of the Advanced Light Source (Lawrence Berkeley National Laboratory), and at beamlines PXI and PXIII of the Swiss Light Source (Paul Scherrer Institut) and processed using XDS (50 (link)). Phasing was performed with crystals of selenomethionine (SeMet)–substituted SpyCas9 and native Cas9 crystals soaked individually with 10 mM Na₂WO₄, 10 mM CoCl₂, 1 mM thimerosal, and 1 mM Er(III) acetate. Phases were calculated using autoSHARP (51 (link)) and improved by density modification using Resolve (52 (link)). The atomic model was built in Coot (53 (link)) and refined using phenix.refine (54 (link)).
A. naeslundii Cas9 (AnaCas9) was expressed in E. coli Rosetta 2 (DE3) as a fusion protein containing an N-terminal His₁₀ tag followed by MBP and a TEV (tobacco etch virus) protease cleavage site. The protein was purified by Ni-NTA (nickel–nitrilotriacetic acid) and heparin affinity chromatography, followed by a gel filtration step. Crystals of native and SeMet-substituted AnaCas9 were grown from 10% (w/v) PEG 8000, 0.25 M calcium acetate, 50 mM magnesium acetate, and 5 mM spermidine. Native and SeMet single-wavelength anomalous diffraction (SAD) data sets were collected at beamline 8.3.1 of the Advanced Light Source, processed using Mosflm (55 (link)), and scaled in Scala (56 (link)). Phases were calculated in Solve/Resolve (52 (link)), and the atomic model was built in Coot and refined in Refmac (57 (link)) and phenix.refine (54 (link)).
For biochemical assays, crRNAs were synthesized by Integrated DNA Technologies, and tracrRNA was prepared by in vitro transcription as described (8 (link)). The sequences of RNA and DNA reagents used in this study are listed in table S2. Cleavage reactions were performed at room temperature in reaction buffer [20 mM tris-Cl (pH 7.5), 100 mM KCl, 5 mM MgCl₂, 5% glycerol, 1 mM dithiothreitol] using 1 nM radio-labeled dsDNA substrates and 1 nM or 10 nM Cas9:crRNA:tracrRNA. Cleavage products were resolved by 10% denaturing (7 M urea) PAGE and visualized by phosphorimaging. Cross-linked peptide-DNA heteroconjugates were obtained by incubating 200 pmol of catalytically inactive (D10A/H840A) Cas9 with crRNA:tracrRNA guide and 10-fold molar excess of BrdU containing dsDNA substrate for 30 min at room temperature, followed by irradiation with UV light (308 nm) for 30 min. S1 nuclease and phosphatase–treated tryptic digests were analyzed using a Dionex UltiMate3000 RSLCnano liquid chromatograph connected in-line with an LTQ Orbitrap XL mass spectrometer equipped with a nanoelectrospray ionization source (Thermo Fisher Scientific).
For negative-stain EM, apo-SpyCas9, SpyCas9: RNA, and SpyCas9:RNA:DNA complexes were reconstituted in reaction buffer, diluted to a concentration of ~25 to 60 nM, applied to glow-discharged 400-mesh continuous carbon grids, and stained with 2% (w/v) uranyl acetate solution. Data were acquired using a Tecnai F20 Twin transmission electron microscope operated at 120 keV at a nominal magnification of either ×80,000 (1.45 Å at the specimen level) or ×100,000 (1.08 Å at the specimen level) using low-dose exposures (~20 e⁻ Å⁻²) with a randomly set defocus ranging from −0.5 to −1.3 μm. A total of 300 to 400 images of each Cas9 sample were automatically recorded on a Gatan 4k × 4k CCD (charge-coupled device) camera using the MSI-Raster application within the automated macromolecular microscopy software Leginon (58 (link)). Particles were preprocessed in Appion (45 (link)) before projection matching refinement with libraries from EMAN2 and SPARX (59 (link), 60 (link)) using RCT reconstructions (34 (link)) as initial models.

Jinek M., Jiang F., Taylor D.W., Sternberg S.H., Kaya E., Ma E., Anders C., Hauer M., Zhou K., Lin S., Kaplan M., Iavarone A.T., Charpentier E., Nogales E, & Doudna J.A. (2014). Structures of Cas9 Endonucleases Reveal RNA-Mediated Conformational Activation. Science (New York, N.Y.), 343(6176), 1247997.

Publication 2014

Structural Analysis of COVA1-16 Fab-RBD Complex

Cited 10 times

The COVA1-16 Fab complex with RBD was formed by mixing each of the protein components in an equimolar ratio and incubating overnight at 4°C. The COVA1-16 Fab–RBD complex and COVA1-16 Fab apo (unliganded) protein were adjusted to around 11 mg/mL and screened for crystallization using the 384 conditions of the JCSG Core Suite (QIAGEN) on our custom-designed robotic CrystalMation system (Rigaku) at Scripps Research. Crystallization trials were set-up by the vapor diffusion method in sitting drops containing 0.1 μL of protein and 0.1 μL of reservoir solution. Crystals used for X-ray data collection were harvested from drops containing 0.2 M sodium iodide and 20% (w/v) polyethylene glycol 3350 for the COVA1-16 Fab–RBD complex and from drops containing 0.08 M acetate pH 4.6, 20% (w/v) polyethylene glycol 4000, 0.16 M ammonium sulfate and 20% (v/v) glycerol for the COVA1-16 Fab. Crystals appeared on day 3, were harvested on day 7, pre-equilibrated in cryoprotectant containing 20% glycerol, and then flash cooled and stored in liquid nitrogen until data collection. Diffraction data were collected at cryogenic temperature (100 K) at Stanford Synchrotron Radiation Lightsource (SSRL) on the Scripps/Stanford beamline 12-1 with a beam wavelength of 0.97946 Å, and processed with HKL2000 (Otwinowski and Minor, 1997 ). Structures were solved by molecular replacement using PHASER (McCoy et al., 2007 (link)). The models for molecular replacement of RBD and COVA1-16 were from PDB: 6XC4 (Yuan et al., 2020a (link)), 4IMK (Fenn et al., 2013 (link)) and 2Q20 (Baden et al., 2008 (link)). Iterative model building and refinement were carried out in COOT (Emsley et al., 2010 (link)) and PHENIX (Adams et al., 2010 (link)), respectively. Ramachandran statistics were calculated by MolProbity (Chen et al., 2010 (link)). Epitope and paratope residues, as well as their interactions, were identified by accessing PISA software server (https://www.ebi.ac.uk/pdbe/prot_int/pistart.html; Krissinel and Henrick, 2007 (link)).

Liu H., Wu N.C., Yuan M., Bangaru S., Torres J.L., Caniels T.G., van Schooten J., Zhu X., Lee C.C., Brouwer P.J., van Gils M.J., Sanders R.W., Ward A.B, & Wilson I.A. (2020). Cross-Neutralization of a SARS-CoV-2 Antibody to a Functionally Conserved Site Is Mediated by Avidity. Immunity, 53(6), 1272-1280.e5.

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Publication 2020

Acetate Binding Sites, Antibody COVA1-16 Cryoprotective Agents Crystallization Diffusion Epitopes Glycerin Nitrogen polyethylene glycol 3350 polyethylene glycol 4000 Proteins Radiation Radiography Sodium Iodide Sulfate, Ammonium

Transformation of Aspergillus fumigatus Protoplasts

Cited 9 times

Transformation of A. fumigatus protoplasts was carried out according to a standard protocol (56 (link)), with minor modifications. Briefly, conidia were inoculated into 100 to 150 ml of liquid YG (5 g/liter yeast extract and 20 g/liter d-glucose) at a final concentration of 1 × 10⁶ conidia/ml and cultivated for 16 h at 30°C with shaking at 250 rpm. Mycelia were harvested by filtration, washed with sterile water, resuspended in protoplasting buffer (5% [wt/vol] VinoTastePro lytic enzyme mix, 1.2 M MgSO₄⋅7H₂O, 10 mM sodium phosphate buffer, pH 6.5), and incubated at 32°C with shaking at 75 rpm until protoplasts were produced (approximately 2 to 5 h, depending on the strain). Protoplasts were separated from mycelial debris by overlaying the protoplast mixture with trapping buffer (0.6 M sorbitol, 100 mM Tris-HCl, pH 7.0) and centrifuging for 15 min at 3,500 rpm and 4°C. The protoplast layer was transferred to a new tube, washed with 3 volumes of STC buffer (1.2 M sorbitol, 7.55 mM CaCl₂⋅H₂O, 10 mM Tris-HCl, pH 7.5), and centrifuged for 10 min at 3,500 rpm and 4°C. The protoplast pellet was then resuspended in STC buffer to a final concentration of 5 × 10⁷ protoplasts/ml. To proceed with Cas9-mediated transformation, 200 µl of protoplasts was transferred to a sterile 15-ml tube containing the full 26.5-µl reaction mixture of the dual RNPs, prepared as described above (Fig. 1). Immediately, 2 or 10 µg of the purified repair template (described above) and 25 µl of polyethylene glycol (PEG)-CaCl₂ buffer (60% [wt/vol] PEG 3350, 50 mM CaCl₂⋅H₂O, 450 mM Tris-HCl, pH 7.5) were added, and the mixture was incubated on ice for 50 min. Afterward, 1.25 ml PEG-CaCl₂ buffer was added, and the mixture was incubated at room temperature for 20 min. Subsequently, the mixture was diluted to a total volume of 3 ml with STC buffer and plated on SMM agar plates (GMM supplemented with 1.2 M sorbitol and 1.5% [wt/vol] agar). The plates were incubated overnight at room temperature to allow regeneration of the fungal cell wall. Finally, all transformation plates were overlaid with SMM top agar (GMM supplemented with 1.2 M sorbitol and 0.7% [wt/vol] agar) containing hygromycin (final concentration of 150 µg/ml), and the plates were incubated at 37°C for 3 days.

Al Abdallah Q., Ge W, & Fortwendel J.R. (2017). A Simple and Universal System for Gene Manipulation in Aspergillus fumigatus: In Vitro-Assembled Cas9-Guide RNA Ribonucleoproteins Coupled with Microhomology Repair Templates. mSphere, 2(6), e00446-17.

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Publication 2017

Agar Buffers Cell Wall Conidia Enzymes Filtration Glucose hygromycin A Mycelium polyethylene glycol 3350 Polyethylene Glycols Protoplasts Regeneration Ribonucleoproteins sodium phosphate Sorbitol Sterility, Reproductive Strains Sulfate, Magnesium Tromethamine Yeast, Dried

Structural Insights into Bcl-xL Complexes

Cited 8 times

Bcl-x_L Δ27–82 and A142L (both without the membrane anchor) were produced as described previously.[7a (link), 15a (link)] The synthesis of 1 has been described.[7a (link)] Crystals of Bcl-x_L Δ27–82 and 1 were obtained by mixing at a molar ratio of 1:1.3 then concentrating the sample to 10 mg/ml. Crystals were grown by the sitting drop method at room temperature in 0.2 M lithium nitrate, 20% (w/v) polyethylene glycol 3350. Prior to flash freezing in liquid N₂, crystals were equilibrated into cryoprotectant consisting of reservoir solution plus increasing concentrations of ethylene glycol to a final concentration of 20%. Data collection and refinement methods are detailed in Table S1.

Lee E.F., Sadowsky J.D., Smith B.J., Czabotar P.E., Peterson-Kaufman K.J., Colman P.M., Gellman S.H, & Fairlie W.D. (2009). High-Resolution Structural Characterization of a Helical α/β-Peptide Foldamer Bound to the Anti-Apoptotic Protein Bcl-xL. Angewandte Chemie (International ed. in English), 48(24), 4318-4322.

Publication 2009

Anabolism Cryoprotective Agents Glycol, Ethylene Lithium Molar Nitrates polyethylene glycol 3350 Tissue, Membrane

Structural Insights into Insulin Receptor

Cited 7 times

IR310.T was produced by proteolysis of an engineered mini-receptor precursor cIR485 expressed from a stable Chinese hamster ovary Lec8 cell line and purified by ion-exchange and size-exclusion chromatography (SEC), followed by combination with 83-7, re-purification by SEC and finally combination with excess αCT peptide and insulin (or analogue). Crystallization conditions for IR310.T-derived complexes A, B and C were 0.9–1.1M tri-sodium citrate, 0.1 M imidazole-HCl (pH 8.0) + 0.02% sodium azide (NaN₃). IR593.αCT was expressed from a stable Chinese hamster ovary Lec8 cell line followed by insulin affinity chromatography and then SEC of the resultant bovine insulin complex. Samples were combined with 83-14 and re-purified by SEC. The crystallization condition for the IR593.αCT-derived complex D was 9% polyethylene glycol 3350, 200 mM proline, 100 mM HEPES-NaOH (pH 7.5). Diffraction data were collected at the Australian Synchrotron (beamline MX2) and Diamond Light Source (DLS; beamline I24). Structures were solved by molecular replacement. Introduction of Pap residues into the αCT segment used orthogonal tRNA/amber suppression technology. Mutant holoreceptors were expressed transiently using co-transfected 293PEAK rapid cells in Pap-containing medium. Cell detergent lysates were then subjected to wheat-germ agglutinin chromatography; eluates containing the receptor were concentrated before photo-crosslinking to ¹²⁵I-[Tyr^A14] insulin. Photo-crosslinked products were resolved by gel electrophoresis and auto-radiographed. IR468 was produced by transient expression in HEK293 cells. ¹²⁵I-photo-activatable insulin analogues were incubated with IR468 in the presence of 10⁻⁵ M αCT(703–719)– Myc and then photo-crosslinked. Samples were resolved by gel electrophoresis and auto-radiographed. For ITC, Ala-substituted αCT peptides (80 µM concentration) were titrated into a sample cell containing IR485 (10 µM concentration); and zinc-free porcine insulin (32–48 µM concentration) was titrated into a sample cell containing IR485 (4–6 µM concentration) pre-incubated with Ala-substituted αCT peptide (10× molar concentration). All samples were in Tris-buffered saline (pH 8.0) plus azide (TBSA).
Full Methods and any associated references are available in the online version of the paper.

Menting J.G., Whittaker J., Margetts M.B., Whittaker L.J., Kong G.K., Smith B.J., Watson C.J., Žáková L., Kletvíková E., Jiráček J., Chan S.J., Steiner D.F., Dodson G.G., Brzozowski A.M., Weiss M.A., Ward C.W, & Lawrence M.C. (2013). How insulin engages its primary binding site on the insulin receptor. Nature, 493(7431), 241-245.

Publication 2013

Amber Azides Bos taurus Cells CHO Cells Chromatography Chromatography, Affinity Crystallization Detergents Diamond Electrophoresis Gel Chromatography HEK293 Cells HEPES imidazole Insulin insulin pork Ion Exchange Lente Insulin Light Molar Peptides Pigs polyethylene glycol 3350 Proline Proteolysis Saline Solution Sodium Azide Sodium Citrate Transfer RNA Transients Wheat Germ Agglutinins Zinc

Most recents protocols related to «Polyethylene glycol 3350»

Optimized Crystallization Conditions for Protein Complexes

Crystallization trials were performed at 18 °C using commercially available kits and were carried out by the sitting-drop vapor diffusion method with mixing 1 μL reservoir solution and 1 μL protein sample. Diffraction-quality crystals were obtained under the following conditions:
GATA18-SAP05: 0.2 M Lithium acetate dehydrate and 20% (w/v) polyethylene glycol 3350;
SPL5-SAP05: 0.2 M Sodium fluoride and 20% (w/v) polyethylene glycol 3350;
RPN10-SAP05: 0.2 M Lithium acetate dehydrate, 18% (w/v) polyethylene glycol 3350 and 0.1 M guanine hydrochloride;
SPL13-SAP05: 0.2 M Ammonium acetate, 0.1 M HEPES pH 7.5 and 25% (w/v) polyethylene glycol 3350.
Crystals were mounted directly in the respective well solutions supplemented with 25% (v/v) glycerol and flash frozen in liquid nitrogen for data collection.

Yan X., Yuan X., Lv J., Zhang B., Huang Y., Li Q., Ma J., Li Y., Wang X., Li Y., Yu Y., Liu Q., Liu T., Mi W, & Dong C. (2024). Molecular basis of SAP05-mediated ubiquitin-independent proteasomal degradation of transcription factors. Nature Communications, 15, 1170.

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Publication 2024

Structural Insights into SARS-CoV-2 3CLpro Mutants

The SARS-CoV-2 3CLpro mutants were concentrated to 10 mg/mL, followed by centrifugation at 21,000× g for 5 min to remove the precipitate. DTT was added to a final concentration of 5 mM before crystallization for M49K/S301P. For crystallization, 0.2 µL of the protein was mixed with 0.2 µL of well buffer in a 96-well plate by a protein crystallization robot (Mosquito) using the sitting drop method (M165V and S301P) or hanging drop method (M49K, M49K/165V and M49K/S301P), then the drop was equilibrated against 90 µL of the well buffer at 20 °C. The well buffer for the crystallization of the M49K mutant contained 0.2 M BIS-TRIS, pH 6.0, 20% w/v polyethylene glycol 4000. The well buffer for the crystallization of the M165V mutant contained 0.2 M BICINE, pH 8.1, 20% polyethylene glycol 4000. The well buffer for the crystallization of the S301P mutant contained 0.2 M BIS-TRIS, pH 6.6, 20% polyethylene glycol 4000. The well buffer for the crystallization of the M49K/M165V double mutant contained 0.2 M BIS-TRIS propane, pH 7.3, 20% polyethylene glycol 4000. The well buffer for the crystallization of the M49K/S301P double mutant contained 0.2 M LiSO4, 0.1 M BIS-TRIS, pH 6.6, 17.5% polyethylene glycol 3350. The complex of the M49K/S301P double mutant with WU-04 was prepared by incubating the M49K/S301P double mutant (10 mg/mL in 20 mM HEPES, pH7.4, 150 mM NaCl) with 1.5 mM WU-04 (the stock used is 50 mM in DMSO) at room temperature for 2 h, followed by centrifugation at 21,000× g for 5 min to remove the precipitate. Then, 0.2 µL of the complex was mixed with 0.2 µL of the well buffer in a 96-well plate using the sitting drop method and the drop was equilibrated against 90 µL of the well buffer at 20 °C. The well buffer contains 0.1 M sodium formate, 12% polyethylene glycol 3350.

Zhang L., Xie X., Luo H., Qian R., Yang Y., Yu H., Huang J., Shi P.Y, & Hu Q. (2024). Resistance mechanisms of SARS-CoV-2 3CLpro to the non-covalent inhibitor WU-04. Cell Discovery, 10, 40.

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Publication 2024

Obtaining Ddl-Acetate Complex Crystals

The crystals of Ddl in complex with acetate were obtained by co-crystallization experiments using the hanging drop vapor diffusion method. The 10 mg/mL of protein was incubated with 30 mM potassium acetate, 5 mM magnesium chloride hexahydrate, and 1 mM ADP for 20 min before the crystallization experiments. The co-crystals were achieved in crystallization drop against a well solution consisting of 0.2 M sodium thiocyanate and 20 % polyethylene glycol monomethyl ether 2000. The crystals were flash cooled in liquid nitrogen immediately after adding 40% polyethylene glycol 3350 to the crystallization drop for cryoprotection. The data were collected at the Advance Photon Source Argonne National Laboratory (APS-ANL, IL), LS-CAT ID-F beamline.

Panda S., Jayasinghe Y.P., Shinde D.D., Bueno E., Stastny A., Bertrand B.P., Chaudhari S.S., Kielian T., Cava F., Ronning D.R, & Thomas V.C. (2024). Staphylococcus aureus counters organic acid anion-mediated inhibition of peptidoglycan cross-linking through robust alanine racemase activity. bioRxiv.

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Publication Preprint 2024

Structural Determination of Metallo-β-Lactamases

The purified IMP-1 (60 mg/mL) was mixed with an equal volume reservoir solution [0.2 M sodium acetate, 0.1 M HEPES-NaOH (pH 7.7), and 35% polyethylene glycol 3350] and crystallized with sitting-vapor diffusion method. The IMP-1 crystals were clashed and subjected to microseeding. The crystals obtained after microseeding were soaked in a reservoir solution containing 10-HHIA before collecting X-ray diffraction data. The purified VIM-2 (15 mg/mL) was mixed with an equal volume reservoir solution (0.2 M magnesium formate and 25% polyethylene glycol 3350) and crystallized. The crystals were soaked in a reservoir solution containing 10-HHIA before collecting X-ray diffraction data. The X-ray diffraction data were collected at the BL-5A beamline (Photon Factory, Ibaraki, Japan) and the BL2S1 beamline (Aichi Synchrotron Radiation Center, Aichi, Japan). Diffraction data were processed using iMosflm (48 (link)) in the CCP4 suite (49 (link)). The crystal structure was solved via molecular replacement using the MOLREP program (50 (link)) in the CCP4 suite (49 (link)). Model building was performed using COOT (51 (link)), and model refinement was performed using REFMAC5 (52 (link)) in the CCP4 suite (49 (link)).

Wachino J.I., Jin W., Norizuki C., Kimura K., Tsuji M., Kurosaki H, & Arakawa Y. (2024). Hydroxyhexylitaconic acids as potent IMP-type metallo-β-lactamase inhibitors for controlling carbapenem resistance in Enterobacterales. Microbiology Spectrum, 12(3), e02344-23.

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Publication 2024

Crystallization of SenB and RsSenB Proteins

The purified SenB protein (7.5 mg/mL) was incubated with UDP-Glc (5 mM), UDP-GlcNAc (5 mM), or UDP-GalNAc (5 mM) for 30 min on ice, and the purified RsSenB protein (7.5 mg/mL) was incubated with UDP-GalNAc (5 mM), before set-up of the crystallization trays. Crystals of SenB/UDP-Glc/PO₄^3- were observed at 18 °C within 3-4 d using the hanging drop vapor diffusion method by mixing 0.8 μL of protein with 0.8 μL of the reservoir solution (0.2 M Ammonium sulfate, 0.1 M Hepes (pH 7.5), and 20% (w/v) polyethylene glycol 8000, 10% (v/v) 2-Propanol). The crystals of SenB/UDP-GalNAc were obtained in the reservoir solution containing 0.1 M Bis-Tris (pH 6.5), and 20% (w/v) polyethylene glycol 5000-MME. The crystals of SenB/UDP-GlcNAc were obtained in the reservoir solution containing 0.1 M Hepes (pH 7.0), and 15% (w/v) polyethylene glycol 20000. The crystals of RsSenB/UDP-GalNAc were obtained in the reservoir solution containing 0.2 M Ammonium citrate dibasic, and 20% (w/v) polyethylene glycol 3350. All crystals were harvested in the same reservoir solution supplemented with 20% (w/v) glycerol as the cryo-protectant and flash-frozen in the liquid nitrogen.

Huang W., Song J., Sun T., He Y., Li X., Deng Z, & Long F. (2024). Substrate binding and catalytic mechanism of the Se-glycosyltransferase SenB in the biosynthesis of selenoneine. Nature Communications, 15, 1659.

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Publication 2024

Top products related to «Polyethylene glycol 3350»

Polyethylene glycol 3350 by Merck Group

Sourced in Germany

Polyethylene glycol 3350 is a non-ionic polymer compound used as a multipurpose laboratory reagent. It is a water-soluble and odorless solid material that can be used in various research and analytical applications.

Peg3350 by Merck Group

Sourced in United States

PEG3350 is a polyethylene glycol compound used as a non-reactive, water-soluble polymer in various laboratory applications. It has a molecular weight of approximately 3,350 Daltons. PEG3350 is frequently employed as a component in buffer solutions, protein stabilizers, and other laboratory reagents.

Peg ion by Hampton Research

Sourced in United States, Germany, United Kingdom

The PEG/Ion is a laboratory instrument designed to facilitate the study of protein crystallization. It automates the process of screening a wide range of solution conditions, including varying concentrations of precipitants, salts, and other additives. The device can precisely control temperature and other environmental factors to create the optimal conditions for protein crystal growth.

Polyethylene glycol 3350 by Hampton Research

Sourced in United States

Polyethylene glycol 3350 is a water-soluble, non-ionic polymer. It has a molecular weight of approximately 3,350 Daltons. Polyethylene glycol 3350 is commonly used as an excipient in pharmaceutical and laboratory applications.

Sodium chloride (nacl) by Merck Group

Sourced in United States, Germany, United Kingdom, India, Italy, France, Spain, China, Canada, Sao Tome and Principe, Poland, Belgium, Australia, Switzerland, Macao, Denmark, Ireland, Brazil, Japan, Hungary, Sweden, Netherlands, Czechia, Portugal, Israel, Singapore, Norway, Cameroon, Malaysia, Greece, Austria, Chile, Indonesia

NaCl is a chemical compound commonly known as sodium chloride. It is a white, crystalline solid that is widely used in various industries, including pharmaceutical and laboratory settings. NaCl's core function is to serve as a basic, inorganic salt that can be used for a variety of applications in the lab environment.

Dimethyl sulfoxide (dmso) by Merck Group

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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.

Morpheus by Molecular Dimensions

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Morpheus is a compact and automated crystal screening solution designed for crystallization experiments. It provides controlled environment conditions and precise sample handling to facilitate the growth and evaluation of protein crystals.

Index screen by Hampton Research

Sourced in United States

The Index screen is a lab equipment component used for indexing and aligning samples or objects. It provides a stable and precise platform to position items for further analysis or processing. The device allows for accurate and repeatable adjustment of the orientation and position of samples.

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.

What are the different types or variations of Polyethylene glycol 3350 available?

Polyethylene glycol 3350 (PEG 3350) is typically available in a few different forms or formulations. The most common are the powder form, which is mixed with water or other liquids, and the tablet form, which is taken orally. Some manufacturers may also offer liquid or solution formulations of PEG 3350 for easier consumption. It's important to follow the specific instructions for the particular PEG 3350 product you are using, as the dosage and preparation may vary slightly between different versions.

How can PubCompare.ai help optimize the use of Polyethylene glycol 3350?

PubCompare.ai is a powerful AI-driven tool that can assist researchers in identifying the most accurate and reproducible protocols for using Polyethylene glycol 3350. The platform allows you to efficiently screen protocol literature and leverage AI to pinpoint critical insights. By comparing the effectiveness of different PEG 3350 protocols from published literature, preprints, and patents, PubCompare.ai can help you choose the best option to enhance the accuracy and reproducibility of your research. With its intelligent comparisons, the tool ensures you find the most effective products and procedures related to Polyethylene glycol 3350 for your specific needs.

What are some common usage challenges with Polyethylene glycol 3350?

One of the main challenges with using Polyethylene glycol 3350 is ensuring proper hydration and preventing side effects like bloating or abdominal discomfort. It's important to follow the dosage instructions carefully and drink plenty of fluids when taking PEG 3350, as it works by drawing water into the intestines. Some people may also experience temporary changes in their bowel habits or loose stools when starting PEG 3350, but these effects typically subside as the body adjusts. Consulting with a healthcare provider can help address any usage challenges and ensure PEG 3350 is being utilized safely and effectively.

What are the specific applications of Polyethylene glycol 3350?

Polyethylene glycol 3350 has a few key applications: 1. Treating constipation: PEG 3350 is a common over-the-counter osmotic laxative used to relieve occasional constipation by drawing water into the intestines and softening stool. 2. Bowel preparation: PEG 3350 is often used as a bowel preparation agent before medical procedures like colonoscopies, to cleanse the digestive tract and improve visibility for the healthcare provider. 3. Research applications: In the laboratory setting, PEG 3350 may be used in various research protocols, such as protein purification or cell culture experiments. PubCompare.ai can help researchers optimixe the use of PEG 3350 in their studies.

More about "Polyethylene glycol 3350"

Polyethylene Glycol 3350 (PEG 3350) is a widely used osmotic laxative and bowel preparation agent.
It is a polyether compound with a typical molecular weight of 3,350 Daltons, composed of repeating ethylene glycol units.
PEG 3350 works by drawing water into the intestines, softening stool, and facilitating bowel movements.
It is commonly employed to treat constipation and prepare the bowel for medical procedures.
Researchers can optimize the use of PEG 3350 with the help of PubCompare.ai, an AI-driven tool that identifies the most accurate and reproducible protocols from literature, preprints, and patents.
With intelligent comparisons, PubCompare.ai ensures researchers find the best products and procedures to enhance their effciency.
PEG/Ion and NaCl are often used in conjunction with PEG 3350 to improve its effectiveness.
DMSO, Morpheus, and Index screen are other commonly utilized compounds and tools that can be leveraged to further optimize the use of PEG 3350.
Bovine serum albumin (BSA) may also play a role in enhancing the performance of PEG 3350-based formulations.
By exploring the synergies between PEG 3350 and these related terms, researchers can unlock new possibilities for improved bowel preparation, constipation management, and overall research efficiency.