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Polyethylene glycol 8000

Polyethylene glycol 8000 (PEG 8000) is a high-molecular-weight polyethylene glycol compound commonly used in biomedical and pharmaceutical applications.
It has a wide range of uses, including drug delivery, tissue engineering, and protein purification.
PEG 8000 is known for its low toxicity, high solubility, and ability to improve the stability and pharmacokinetics of various compounds.
Researchers often optimize PEG 8000 protocols to ensure reproducibility and accuracy in their studies.
PubCompare.ai, an AI-driven tool, helps researchers easily locate and identify the best PEG 8000 protocols from literature, pre-prinrts, and patents, ensuring efficient and reliable research.

Most cited protocols related to «Polyethylene glycol 8000»

1
Structural Determination of Human ACE2 Protein
Cited 49 times

Protein Expression and Purification—A truncated extracellular form of human ACE2 (residues 1-740) was expressed in baculovirus and purified as described previously (8 (link)). The signal sequence (residues 1-18) is presumably removed upon secretion from Sf9 cells. The molecular mass of the purified enzyme is 89.6 kDa by matrix-assisted laser desorption ionization time-of-flight mass spectrometry, which is greater than the theoretical molecular mass of 83.5 kDa expected from the sequence (residues 19-740). The difference of ∼6 kDa is believed to be due to glycosylation at the seven predicted N-linked glycosylation sites for this protein.
Crystallization—Briefly, 2 μl of purified ACE2 (5 mg/ml) was combined with an equal volume of reservoir solution, and crystals were grown by hanging drop vapor diffusion at 16-18 °C. The best crystallization reservoir solution conditions for native ACE2 were found to be 100 mm Tris-HCl (pH 8.5), 200 mm MgCl2, and 14% polyethylene glycol 8000. Under these conditions, it took ∼2 weeks to grow single crystals suitable for x-ray diffraction. Similarly, diffraction-quality ACE2 crystals were also grown in the presence of an ACE2 inhibitor, MLN-4760 (ML00106791; (S,S)-2-{1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol-4-yl]-ethylamino}-4-methylpentanoic acid). Compound MLN-4760 corresponds to compound 16 of Dales et al. (15 (link)). Crystallization trials used 2 μl of reservoir solution plus 2 μl of ACE2 at 5.9 mg/ml containing 0.1 mm inhibitor. The best diffracting ACE2-inhibitor complex crystals were grown in the presence of 19% polyethylene glycol 3000, 100 mm Tris-HCl (pH 7.5), and 600 mm NaCl.
Data Collection and Structure Determination—The best data set for native ACE2 was at 2.2-Å resolution and was collected at the Advanced Photon Source (Argonne National Laboratory). A total of 44 x-ray data sets were collected for native ACE2, including a large number of heavy atom soaks of atoms that had good anomalous signals. The data sets for each derivative were collected at different wavelengths to maximize the anomalous signals for the bound heavy atoms. Native ACE2 data were collected to 2.2-Å resolution at λ = 1.28 Å to maximize the anomalous signal at the zinc absorption edge.
The heavy atom positions were determined and confirmed by a combination of visual inspection of Patterson maps and automatic search procedures, which included SHAKE 'N BAKE (16 (link)) and SHELXD (17 (link)). The heavy atom parameters were refined and optimized using the computer programs SHARP (18 (link)), MLPHARE (19 ), and XHEAVY (20 ). The experimental phases were improved by solvent flattening and histogram matching.
Once the native ACE2 structure was determined, it was used to solve the inhibitor-bound structure of ACE2 to 3.0-Å resolution using molecular replacement methods that employed the program AMoRe in the CCP4 software suite (21 (link)). The native structure was split into two subdomains: subdomains I and II (see Fig. 3for definition). Subdomain II was used for molecular replacement and refined in REFMAC5, which resulted in the appearance of electron density for subdomain I. Subdomain I was then fitted into the density by hand, and the structure was refined as a whole. Final refinement was accomplished using the software suite CNX (22 (link)).

Overview of the native ACE2 crystal structure.A, α-carbon trace of the native ACE2 structure looking down into the metallopeptidase active site cleft. The metallopeptidase catalytic domain is colored red. The active site zinc ion is shown as a yellow sphere, and the single bound chloride ion is shown as a green sphere. The S1′ subsite for inhibitor and substrate binding is to the right of the zinc ion, and the S1 subsite is to the left. The collectrin homology domain at the C terminus is disordered and denoted by the green dotted line. B, ribbon diagram of native ACE2 showing the secondary structure and also the two subdomains (I and II) that form the two sides of the active site cleft. The two subdomains are defined as follows: the N terminus- and zinc-containing subdomain I (red), composed of residues 19-102, 290-397, and 417-430; and the C terminus-containing subdomain II (blue), composed of residues 103-289, 398-416, and 431-615. This definition is based on motion observed upon inhibitor binding (see Fig. 4). Zinc and chloride ions are denoted as described for A.

Towler P., Staker B., Prasad S.G., Menon S., Tang J., Parsons T., Ryan D., Fisher M., Williams D., Dales N.A., Patane M.A, & Pantoliano M.W. (2004). ACE2 X-Ray Structures Reveal a Large Hinge-bending Motion Important for Inhibitor Binding and Catalysis. The Journal of Biological Chemistry, 279(17), 17996-18007.
Publication 2004
2
CUT&RUN Chromatin Profiling Protocol
Cited 42 times
CUT&RUN begins with crude nuclei prepared according to published procedures. The following protocol is provided in step-by-step format (Appendix 2). Nuclei from ~5 × 108 cells at OD600 ~0.7 were prepared as described (Orsi et al., 2015 (link)), divided into 10 600 µL aliquots, snap-frozen and held at −80°C, then thawed on ice before use. Bio-Mag Plus Concanavalin A (lectin) coated beads were equilibrated with HNT (20 mM HEPES pH7.5, 100 mM NaCl and 0.1% Tween 20) that was supplemented with 1 mM each MgCl2, CaCl2 and MnCl2. Only Ca++ and Mn++ are needed to activate lectins, and omitting MgCl2 had no effect on binding of permeabilized cells to beads. The beads (300 µL) were rapidly mixed with a thawed nuclei aliquot and held at room temperature (RT) ≥5 min, placed on a magnet stand to clear (<1 min), and decanted on a magnet stand. The beads were then incubated 5 min RT in HNT supplemented with protease inhibitors (Roche Complete tablets) and 1 mM phenylmethylsulfonyl fluoride (PMSF) (=HNT-PPi) containing 3% bovine serum albumen (BSA) and 2 mM EDTA pH 8, then incubated 5’ with HNT-PPi +0.1% BSA (blocking buffer), using the magnet stand to decant. The beads were incubated 2 hr at 4°C with mouse anti-FLAG antibody (1:200–1:350), decanted, washed once in HNT + PMSF, then incubated 1 hr at 4°C with rabbit anti-mouse IgG antibody (1:200) in blocking buffer. The beads were washed once in HNT + PMSF, then incubated 1 hr at 4°C with pA-MN (600 µg/ml, 1:200) in blocking buffer. The beads were washed twice in HNT + PMSF and once in 20 mM HEPES pH 7.5, 100 mM NaCl (Digestion buffer), optionally including 10% polyethylene glycol 8000 for Sth1 and Mot1. The beads were brought up in 1.2 ml Digestion buffer, divided into 8 × 150 µL aliquots, equilibrated to 0°C, then quickly mixed with CaCl2, stopping the reaction with 150 µL 2XSTOP [200 mM NaCl, 20 mM EDTA, 4 mM EGTA, 50 µg/ml RNase A (Thermo Scientific, Waltham, MA, Catalog #EN0531) and 40 µg/ml glycogen (Sigma, Catalog #10901393001), containing 5-50 pg/ml heterologous mostly mononucleosome-sized DNA fragments extracted from formaldehyde crosslinked MNase-treated Drosophila chromatin as a spike-in]. After incubating at 37°C for 20 min, the beads were centrifuged 5 min at 13,000 rpm at 4°C, the supernatant was removed on a magnet stand and mixed with 3 µL 10% SDS and 2 µL Proteinase K (Invitrogen, Carlsbad, CA, Catalog #25530049), incubated at 70°C 10 min, then extracted at room temperature once with buffered phenol-chloroform-isoamyl alcohol (25:24:1, Sigma P2069), transferred to a phase-lock tube (Qiagen, Hilden, Germany, Catalog #129046), re-extracted with one vol CHCl3, transferred to a fresh tube containing 2 µL 2 mg/ml glycogen, precipitated by addition of 2–2.5 vol ethanol, chilled in ice and centrifuged 10 min at 13,000 rpm at 4°C. The pellet was rinsed with 100% ethanol, air-dried and dissolved in 25 µL 0.1 x TE8 (=1 mM Tris pH 8, 0.1 mM EDTA).
To extend CUT&RUN for high-salt extraction, digestions were performed in a 50 µL volume, stopped with 50 µL 2XSTOP, omitting RNase and substituting the standard 200 mM NaCl with 4 M NaCl. After 20 min at 37°C, 200 µL 67 µg/ml RNase A was added, incubated 20 min, then centrifuged 13,000 rpm to clarify the supernatant.
Skene P.J, & Henikoff S. (2017). An efficient targeted nuclease strategy for high-resolution mapping of DNA binding sites. eLife, 6, e21856.
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Publication 2017
3
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
4
Quantifying Cholesterol Efflux Pathways
Cited 22 times
J774 cells, maintained in RPMI plus 10% FBS and antibiotics in 5% CO2, were plated in 24-multi well plates (70,000 cells/well) and labeled for 24h in the presence of an ACAT inhibitor (2μg/ml CP113,818, a gift from Pfizer) using 0.5ml/well of 2μCi/ml [1,2-3H] cholesterol (Perkin Elmer) in RPMI plus 1% FBS. To up-regulate ABCA1 in J774 cells we incubated an additional 16h with 0.5ml/well medium containing 0.3mM Cpt-cAMP (Sigma) and 0.2% BSA in RPMI. The relative contribution of various efflux pathways was measured by 2h pretreatment of replicate wells of cAMP treated J774 cells with RPMI-0.2% BSA alone or this medium plus 20μM Probucol, 1μM BLT-1 or both to specifically inhibit ABCA1 and SR-BI15 (link). The contribution of ABCG1 to total efflux capacity was directly measured by 4h incubation of ABCG1 transfected BHK-1 cells with the same specimens used with J774 cells. In BHK-I cells transfected with ABCG1, receptor expression is regulated by mifepristone; the difference between cells treated overnight with mifepristone (10nM) and untreated cells represents ABCG1 efflux19 (link). Sera for these studies were aliquots stored at -70°C, used after a single thaw, and chosen to have similar HDL-C (HDL-C± 6%) at either the 25th (low HDL=45, n=22) or 75th (high HDL=73, n=18) percentile of the HDL-C distribution. Efflux was the fraction of total cellular cholesterol released in 4h to apoB-depleted serum, obtained after removal of apoB lipoproteins with Polyethylene Glycol (PEG, MW 8000, Sigma)18 (link), and diluted to 2.8% (equivalent to 2% serum) in MEM-HEPES (0.5ml/well). We have routinely used this dilution to promote release of radioactive cholesterol to the medium in 4h that is well above background. Supplementary figure I shows the dependence of the various receptor-mediated efflux pathways expressed in J774 cells on the dose of apoB-depleted serum. In this figure, ABCA1 efflux is the difference between cAMP treated and control J774 cells, SR-BI is the efflux measured from Fu5AH cells where SR-BI is the major efflux pathway and ABCG1 efflux is the difference between mifepristone treated and untreated transfected BHK-1 cells. SR-BI and ABCG1 efflux show linear dose dependence; the dose-dependence for ABCA1 mediated efflux fits a non-linear regression that tends to plateau but a concentration of 2.8% apoB-depleted serum is below this point (GraphPad Prism 5, GraphPad Software Inc., San Diego, CA). To further validate our macrophage model, we measured ABCA1 efflux using BHK-1 cells transfected with ABCA1 where receptor expression is regulated with mifepristone and found that the dose dependence of ABCA1 efflux measured with BHK-1 cells was identical to that measured with J774 cells (Supplementary Fig. I). In every experiment, we monitored up-regulation of ABCA1 in J774 cells as increased efflux to apoA-I (20μg/ml) from cells treated with cAMP compared to untreated cells (11±4 fold stimulation, n=10 experiments) and used an aliquot of a standard serum pool at 2% to monitor inter-assay variability in total efflux from cAMP J774 cells and ABCG1 efflux from BHK-1 cells. Transfected BHK-1 cells were a kind gift from Dr. J. Oram. All cellular incubations were done at 37°C and expression of cholesterol transporters was confirmed by western blot in initial experiments. Sera from subjects with similar high or low HDL-C were defined as having low or high efflux capacity based on total J774 efflux below or above the average efflux for each group. The same analysis was done using a subset of these specimens chosen to have similar apoA-I at either the 25th (low apoA-I 127mg/dl, n=11) or 75th (high apoA-I=163mg/dl, n=10) percentile of the apoA-I distribution.
de la Llera-Moya M., Drazul-Schrader D., Asztalos B.F., Cuchel M., Rader D.J, & Rothblat G.H. (2010). The Ability to Promote Efflux via ABCA1 Determines the Capacity of Serum Specimens with Similar HDL-C to Remove Cholesterol from Macrophages. Arteriosclerosis, thrombosis, and vascular biology, 30(4), 796-801.
Publication 2010
5
Structural Studies of mTOR-mLST8 Complexes
Cited 20 times
Crystals were grown by the hanging-drop vapour diffusion method at 4 °C. Apo-crystals of the mTORΔN–mLST8 complex were grown from 100 mM Tris-Cl, 6-8% (w/v) polyethylene glycol (PEG) 8000, 500 mM NaCl, 10% (v/v) glycerol, 10 mM DTT, pH 8.5. Crystals of the mTORΔN-mLST8 bound to ADP-MgF3-Mg2 were grown similarly, except the well-buffer contained 10 mM MgCl2, 3 mM ADP, and 20 mM NaF. The mTORΔN-mLST8-ATPγS-Mg2 complex was prepared by soaking apo-crystals for one hour in a stabilization buffer of 50 mM Tris-Cl, pH 8.5, 10 mM Tris-Cl, 8.0, 10% PEG8000, 0.1 M NaCl, 6% glycerol, supplemented with 5 mM MgCl2 and 1 mM ATPγS. The mTORΔN-mLST8-AMPPNP-Mn2 complex was prepared by soaking apo-crystals similarly, except the stabilization buffer had a pH of 7.5 and it was supplemented with 1 mM AMPPNP and 2 mM MnCl2, and the data was collected at the Manganese absorption edge. Crystals of mTORΔN-mLST8-Torin2 and mTORΔN-mLST8-PI-103 were prepared by mixing 1 mM of the inhibitors with the protein. Co-crystals appeared from the same condition as the apo-crystals. Crystals of mTORΔN-mLST8-PP242 were prepared by soaking apo-crystals for 2.5 hours in the stabilization buffer supplemented with 0.2 mM PP242. Apo-crystals were harvested in stabilization buffer, transferred to 50 mM Tris-Cl, pH 8.5, 10 mM Tris-Cl, pH 8.0, 0.1 M NaCl, 14% (w/v) PEG8000, 22% (v/v) glycerol, and were flash-frozen in liquid nitrogen. Crystals with ADP-MgF3-Mg2, ATPγS-Mg2, Torin2, PI103 and PP242 were flash-frozen similarly, except for the presence of the corresponding cofactors or inhibitors (0.1 mM) in the buffers. Diffraction data were collected at -170 °C at the ID24C and ID24E beamlines of the Advanced Photon Source, and they were processed with the HKL suite49 .
Yang H., Rudge D.G., Koos J.D., Vaidialingam B., Yang H.J, & Pavletich N.P. (2013). mTOR kinase structure, mechanism and regulation by the rapamycin-binding domain. Nature, 497(7448), 217-223.
Publication 2013
adenosine 5'-O-(3-thiotriphosphate) Adenylyl Imidodiphosphate Buffers Diffusion Freezing Glycerin inhibitors Magnesium Chloride Manganese manganese chloride MLST8 protein, human Nitrogen PI103 polyethylene glycol 8000 PP242 Proteins Sodium Chloride Tromethamine

Most recents protocols related to «Polyethylene glycol 8000»

1
Exosome Isolation Using PEG Precipitation
The ECM was supplemented with 50% polyethylene glycol (PEG) 8000 solution (in ddH2O) to a final concentration of 10% PEG, mixed well by inversion, supplemented with NaCl to a final concentration of 75 mM, and mixed again by inversion (Fig. 2a). This mixture was then incubated at 4°C for 4–16 h. Note that longer incubation times may increase exosome yield compared to very short incubation times. The sample was then centrifuged at 16 000g for 1 h at 4°C to precipitate the exosomal fraction. The pellet was then resuspended in 1× PBS. To remove any remaining contaminants in the pellet, this procedure was repeated once more. Final exosome-enriched fraction preparations were stored in 1× PBS, with short-term storage (days) at 4°C or longer-term storage (months) at −20°C or more preferably at −80°C [41 (link)], although in the latter scenario, caution should be used to employ low protein binding tubes.
Aliakbari F., Stocek N.B., Cole-André M., Gomes J., Fanchini G., Pasternak S.H., Christiansen G., Morshedi D., Volkening K, & Strong M.J. (2024). A methodological primer of extracellular vesicles isolation and characterization via different techniques. Biology Methods & Protocols, 9(1), bpae009.
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Publication 2024
2
Synthesis of Biodegradable Polymer Scaffolds
Glycerol, 4-dimethylaminopyridine and triethylamine were obtained from Fisher Scientific (Loughborough, Leicestershire, UK). Sebacic acid was obtained from Alfa Aesar (Ward Hill, MA, USA). Dichloromethane, polyethylene glycol (Mw 8000), stannous octanoate, p-toluenesulfonic acid monohydrate, lactic acid (85%), polycaprolactone (Mw 80,000), 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP), polyethylene glycol diacrylate (Mw 8000) (PEGDA8000), 2-hydroxy-4′-(2-hydroxyethoxy)-2-methylpropiophenone (Irgacure 2959) and anhydrous magnesium sulphate (MgSO4) were obtained from Sigma Aldrich (Burlington, MA, USA).
Phillips M., Tronci G., Pask C.M, & Russell S.J. (2024). Nonwoven Reinforced Photocurable Poly(glycerol sebacate)-Based Hydrogels. Polymers, 16(7), 869.
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Publication 2024
3
Template-Switch Reaction with PEG
Not available on PMC !
The template-switch reaction was conducted following the procedure previously described [43] .
Additionally, to enhance the efficiency of this reaction, we incorporated polyethylene glycol (PEG 8000; Promega) at a concentration of 10% w/v in each reaction, as previously mentioned. This inclusion of polyethylene glycol aids in promoting optimal reaction conditions acting as a molecular crowding agent and thereby facilitates the successful transformation of ssDNA into dsDNA.
Emili E., Rodríguez-Fernández D., Pérez-Posada A., García-Castro H., & Solana J. (2024). Multiplex single-cell analysis of serotonergic neuron function in planarians reveals widespread effects in diverse cell types.
Publication 2024
4
HBV Purification and Infection Protocol
HBV was purified from HepAD38 cells using heparin-affinity chromatography as previously reported (95 ). HepG2-NTCP cells were infected with HBV MOI 300 with 4% polyethylene glycol-8000, washed after 6 h and treatments applied.
Harris J.M., Magri A., Faria A.R., Tsukuda S., Balfe P., Wing P.A, & McKeating J.A. (2024). Oxygen-dependent histone lysine demethylase 4 restricts hepatitis B virus replication. The Journal of Biological Chemistry, 300(3), 105724.
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Publication 2024
5
Formulation and Characterization of Canagliflozin
Not available on PMC !
Canagliflozin (CFZ) was purchased from Wuhan Senwayer Century Chemical. Co. Ltd, China; Soluplus® was gifted from BASF pharma, Germany; Sodium lauryl sulfate (SLS) was purchased from Sd Fine-Chem Limited Mumbai, India; Ethanol 99 % (HPLC grade) purchased from Merck, USA; Poloxamer 338 purchased from SIGMA, Germany; and Polyethylene glycol 8000 (PEG 8000) from Glentham, UK. All other reagents in this research were of analytical grade.
Jassem N.A., & Alhammid S.N.A. (2024). Ex vivo permeability study and in vitro solubility characterization of oral Canagliflozin self-nanomicellizing solid dispersion using Soluplus® as a nanocarrier. Acta Marisiensis. Seria Medica, 70(2), 42-49.
Publication 2024

Top products related to «Polyethylene glycol 8000»

1
Peg 8000 by Merck Group
Sourced in United States, Germany, Switzerland, Canada, China, United Kingdom, Hungary
PEG 8000 is a polyethylene glycol product manufactured by Merck Group. It is a white, waxy solid with a molecular weight of approximately 8,000 Daltons. PEG 8000 is commonly used as a component in various laboratory and industrial applications.
2
Polyethylene glycol 8000 by Merck Group
Sourced in United States, Germany, Macao
Polyethylene glycol 8000 is a high molecular weight polymer that is commonly used as a laboratory reagent. It is a white, water-soluble, and non-toxic solid. Polyethylene glycol 8000 has a range of applications in various scientific and research settings.
3
Peg 8000 by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Belgium
PEG 8000 is a polyethylene glycol with an average molecular weight of 8,000 daltons. It is a non-ionic, water-soluble polymer commonly used as a precipitating agent, cryoprotectant, and stabilizer in various laboratory applications.
4
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.
5
Sodium chloride (nacl) by Merck Group
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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.
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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.
7
Dnase 1 by Merck Group
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DNase I is a laboratory enzyme that functions to degrade DNA molecules. It catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, effectively breaking down DNA strands.
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Trizol reagent by Thermo Fisher Scientific
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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.
9
Fetal bovine serum (fbs) by Thermo Fisher Scientific
Sourced in United States, China, United Kingdom, Germany, Australia, Japan, Canada, Italy, France, Switzerland, New Zealand, Brazil, Belgium, India, Spain, Israel, Austria, Poland, Ireland, Sweden, Macao, Netherlands, Denmark, Cameroon, Singapore, Portugal, Argentina, Holy See (Vatican City State), Morocco, Uruguay, Mexico, Thailand, Sao Tome and Principe, Hungary, Panama, Hong Kong, Norway, United Arab Emirates, Czechia, Russian Federation, Chile, Moldova, Republic of, Gabon, Palestine, State of, Saudi Arabia, Senegal
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.
10
Polyethylene glycol peg 8000 by Merck Group
Sourced in United States
Polyethylene glycol (PEG) 8000 is a synthetic, water-soluble polymer compound. It is commonly used as a stabilizing and solubilizing agent in various laboratory applications.

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