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2-diethylaminoethanol

2-diethylaminoethanol is a chemical compound with the formula C6H15NO.
It is a secondary amine and a alcohol, commonly used as a chemical intermediate in the production of pharmaceuticals, agricultural chemicals, and other industrial products.
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Most cited protocols related to «2-diethylaminoethanol»

1
In Vitro Translation Assays for Ribosome-Associated mRNA
Cited 13 times
All transcripts utilized PCR products as templates for in vitro transcription (Sharma et al., 2010 (link)) except β-VHP-SL, which was transcribed from linearized plasmid. β-VHP-pA transcript was generated by treating β-VHP transcript with poly(A) polymerase to add an ∼200 nt poly(A) tail. 33P-labeled transcripts were generated with 33P-UTP (Perkin-Elmer) in transcription reactions. In vitro translation reactions using rabbit reticulocyte lysate (RRL), phenyl-depleted RRL, and DEAE fractionated RRL (Fr-RRL) were done as before (Sharma et al., 2010 (link); Hessa et al., 2011 (link)). ΔHbs1 RRL was generated by incubating 800 μl RRL with 200 μl of Pelota resin (immobilized via CnBr). Unconjugated and quenched CnBr resin served as a control. Unless indicated otherwise, translation reactions were for 60 min at 32°C. Where indicated, WT or DN Hbs1 was added at 10 min together with 100 μM aurin tricarboxylic acid to inhibit initiation. For direct analyses, translation reactions were denatured in 1% SDS and heated to 100°C. For downstream applications, translation reactions were cooled on ice and manipulated at 0°C–4°C for RNC isolation, sucrose gradients, and native immunoprecipitations (IPs).
Shao S., von der Malsburg K, & Hegde R.S. (2013). Listerin-Dependent Nascent Protein Ubiquitination Relies on Ribosome Subunit Dissociation. Molecular Cell, 50(5), 637-648.
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Publication 2013
2-diethylaminoethanol Aurintricarboxylic Acid Cardiac Arrest Cyanogen Bromide Immunoprecipitation isolation Plasmids Poly(A) Tail Polynucleotide Adenylyltransferase Rabbits Resins, Plant Reticulocytes Sucrose Transcription, Genetic
2
Purification of Human Hemoglobin
Cited 11 times

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Publication 2017
2-diethylaminoethanol Acetate Anions BLOOD Chromatography Erythrocytes Homo sapiens Normal Saline Patients Sodium Chloride Tissue, Membrane Tromethamine
3
Lentiviral Vector Production and Titration
Cited 10 times
The ViraPower™ Promoterless Lentiviral Gateway Expression system (Invitrogen, Carlsbad, CA) was used to generate lentiviral vectors. The gene encoding enhanced green fluorescent protein (EGFP) was inserted at the position of blasticidin in the pLenti6/R4R2/V5 DEST vector under the control of the SV-40 promoter resulting in the pL-EGFP transfer vector. To produce the virus, 293FT cells were plated on poly-L-lysine-coated 10-cm plates (Corning, New York) at 6.5 × 106 cells per plate in a complete DMEM medium with 10% serum and 1 mM sodium pyruvate and allowed to adhere for 16 hrs. Transfections were performed as per manufacture’s instructions with 4.5 µg of transfer vector plasmid, 18 µg packaging mixture (Invitrogen, Carlsbad, CA) and 67.5 µl of Lipofectamine ™ 2000 in serum-free Opti-MEM medium (Invitrogen). 24 hours after transfection the cells were washed with phosphate-buffered saline (PBS); fresh complete DMEM with pyruvate and 10 % FBS (Serum 4) was added and the cells were incubated for an additional 24 hours. Vector supernatants were collected 48 hrs after transfection, filtered through a 0.45 micron syringe filter (Whatman, Clifton, NJ) and concentrated by ultracentrifugation at 22,000 g for 2 hr at 4°C.
To establish the titer of viral preparations, 293FT cells were plated at 5 × 104 cells per well in 24-well tissue culture plates, allowed to adhere overnight, and a complete DMEM medium containing lentivirus at various concentrations and supplemented with 6 µg/ml of polybrene, 6 µg/ml of DEAE-dextran sulfate, 10 µg/ml of poly-L-lysine, or 10 µg/ml protamine sulfate (Sigma-Aldrich, St. Louis, MO) as indicated. Next day, equal amount of fresh media was added and the cells were incubated for an additional 24 hrs. Adherent cells were washed with warm PBS, trypsinized, and resupsended in 1% paraformaldehyde (Electron Microscopy Sciences, Hatfield, PA) in PBS prior to the analysis by flow cytometry (FACSCalibur, BD Biosciences, San Jose, CA). Vector titers (IU/ml) were calculated according to the following equation: % EGFP positive cells × 5×105 / µl of virus preparation. To ensure maximum accuracy and to compensate for multiple transduction events per cell, the titers were calculated only from transductions with dilution factors resulting in fewer than 25% transduced cells.
Denning W., Das S., Guo S., Xu J., Kappes J.C, & Hel Z. (2013). Optimization of the transductional efficiency of lentiviral vectors: effect of sera and polycations. Molecular biotechnology, 53(3), 308-314.
Publication 2012
2-diethylaminoethanol Cells Cloning Vectors DEAE-Dextran Electron Microscopy enhanced green fluorescent protein Flow Cytometry Gene Products, Protein Lentivirus lipofectamine 2000 Lysine paraform Phosphates Plasmids Poly A Polybrene Pyruvate Saline Solution Serum Simian virus 40 Sodium Sulfate, Dextran Sulfate, Protamine Sulfates, Inorganic Syringes Technique, Dilution Tissues Transfection Ultracentrifugation Virus
4
Expression and Purification of α-Synucleins
Cited 10 times
Wild-type and single Trp-containing α-synucleins were expressed51 (link),52 (link) and purified40 (link) as previously reported with minor modifications. All purification steps are now performed at 4 °C and a HiPrep 16/10 DEAE FF column (GE Healthcare) is used for the first chromatographic step. The protein was eluted with a linear gradient from 100–300 mM NaCl in 20 mM Tris buffer (pH 7.4–8.0). Protein concentrations were determined using a molar extinction coefficient estimated on the basis of amino-acid content: ε280 nm = 5,120 M−1cm−1 (wild-type); ε280 nm = 9,970 M−1cm−1 (Y39W and Y125W); ε280 nm = 10,810 M−1cm−1 (F4W and F94W). The purity of all protein samples was assessed by native- and SDS-PAGE on a Pharmacia Phastsystem (Amersham Biosciences) visualized by silver-staining methods. The protein molecular weights were confirmed by ESI-MS. All purified proteins were concentrated using Centriprep YM-3 (MWCO 3kD, Millipore) and stored at −80 °C.
Pfefferkorn C.M, & Lee J.C. (2010). Tryptophan probes at the α-synuclein and membrane interface. The journal of physical chemistry. B, 114(13), 4615-4622.
Publication 2010
2-diethylaminoethanol Amino Acids Chromatography Extinction, Psychological Molar Proteins SDS-PAGE Sodium Chloride Staining, Silver Synucleins Tromethamine
5
Generating FCoV RNA Standards for RT-PCR
Cited 10 times

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Publication 1999
2-diethylaminoethanol Ampicillin Buffers Chloroform Cloning Vectors Deoxyribonuclease I Diethyl Pyrocarbonate Digestion DNA, Complementary Electrophoresis Endoribonucleases Escherichia coli Freezing Isopropyl Alcohol Oligonucleotide Primers Phenols Plasmids Reverse Transcriptase Polymerase Chain Reaction Sepharose Spectrophotometry Strains Technique, Dilution Tissue, Membrane Transcription, Genetic Transfer RNA

Most recents protocols related to «2-diethylaminoethanol»

1
Extraction and Identification of Chili Pepper Peptides
Not available on PMC !

Example 1

In this example, the oligopeptide FTLE in chili pepper seeds was extracted as follows:

1) deseeding: fresh chili peppers were taken, and the flesh was separated from the seeds to obtain chili pepper seeds;

2) pulverizing: the chili pepper seeds were pulverized and sieved by an 80 mesh to obtain chili pepper seed powder ;

3) degreasing: the chili pepper seed powder was mixed with n-hexane at a ratio of 1:10 (g/ml); the mixture was stirred and degreased overnight; n-hexane was removed by suction filtration after the degreasing was completed to obtain a chili pepper seed meal;

4) protein extraction: the degreased chili pepper seed meal was dissolved in water at a ratio of 1:10 (w/v, g/mL); the pH value of the solution was adjusted to 9.5 with a NaOH solution to conduct dissolving for 4 h; then the pH value of the solution was adjusted to 4.5 with HCl to conduct precipitating for 2 h; the reaction solution was centrifuged at 8,000 rpm for 20 min, and the precipitate was collected as a crude protein extract;

5) ultra-high pressure assisted enzymolysis: the protein isolated was dissolved in water, and was subjected to an ultra-high pressure treatment at 300 MPa for 30 min; then the product obtained by the ultra-high pressure treatment was subjected to an enzymolysis treatment, in which the enzyme was Bacillus licheniformis, the mass ratio of the enzyme to the substrate was 1:20 (w/w, g/g), the temperature was 40° C., the pH value was adjusted to 8 with 1 mol/L NaOH, and the enzymolysis treatment was performed for 3 h;

6) enzyme inactivation: at the end of the enzymolysis, the enzyme was inactivated at 90° C. for 10 min to obtain a chili pepper seed zymolyte solution;

7) isolation and purification of zymolyte: the chili pepper seed zymolyte solution was passed through a DEAE anion chromatography column, where the mobile phase included deionized water and NaCl; the eluent in a periodfrom 35 min to 45 min was collected; then, isolation and purification were conducted by an ODS-A reverse phase C18 column (hydrophobic column), where the mobile phase included deionized water and 50% methanol, and the eluent in a periodfrom 75 min to 90 min was collected. The peptide fragments in the obtained eluate were subjected to mass spectrometry identification analysis, and information of multiple peptide sequences was obtained.

Example 2

Chemical systhesis was conducted in accordance with the peptide sequences obtained by mass spectrometry identification analysis of Example 1 to obtain synthetic peptides. The effect of each peptide on HepG2 cell proliferation was studied, and the specific steps were as follows:

1) HepG2 cell culture: hepG2 cells were obtained from the ATCC cell bank and were cultured in a DMEM medium containing 10% FBS at 37° C. in a 5% CO2 cell incubator. Cells were cultured in a 25 cm 2 flask, passaged when cells were grown to a density of 70% to 90%, and seeded in a 96-well plate.

2) Peptide fragment treatment: after 24 hours of cell culture in the 96-well plate, the original DMEM medium was aspirated from the wells. DMEM containing peptide fragments at concentrations of 0.1, 0.3, and 0.6 mM were added to each well to continue culturing for 24 hours.

3) Cell proliferation rate measured by MTT method: MTT at a concentration of 5 mg/mL was added to a 96-well plate in 20 μL per well. After incubation for 4 hours, the liquid was aspirated from each well. 150 μL DMSO was added to each well. The absorbance was measured after reacting for 20 min.

The results are shown in the figure. It can be seen that the oligopeptide FTLE has a better HepG2 cell inhibition rate than other oligopeptides, which is helpful for the prevention or treatment of liver cancer.

In the description of this specification, descriptions with reference to the terms “one embodiment”, “some embodiments”, “example”, “specific examples”, or “some examples”, etc. mean that a particular feature, structure, material, or characteristic described in connection with the embodiment or example is included in at least one embodiment or example of the present disclosure. In this description, schematic representations of the terms above do not necessarily refer to the same embodiment or example. Furthermore, the particular features, structures, materials, or characteristics described may be combined in any suitable manner in any one or more embodiments or examples. The different embodiments or examples and the features of the different embodiments or examples described in this description can be integrated and combined by a person skilled in the art without contradicting each other.

While embodiments of the present disclosure have been shown and described, it will be understood that the above-described embodiments are illustrative and not restrictive and that changes, modifications, substitutions, and variations may be made to the embodiments by those skilled in the art without departing from the scope of the present disclosure.

US11858970B1. Chili pepper seed isolated oligopeptide FTLE and application thereof in preventing or treating cancer (2024-01-02). CHINA AGRICULTURAL UNIVERSITY [CN]. Inventors: Liang Zhao [CN], Xiaojun Liao [CN], Fengzhang Wang [CN], Yongtao Wang [CN], Lei Rao [CN].
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Patent 2024
2-diethylaminoethanol Anions Bacillus licheniformis Cancer of Liver Cell Culture Techniques Cell Proliferation Cells Chromatography Enzymes Filtration Hep G2 Cells Hexanes isolation Malignant Neoplasms Mass Spectrometry Methanol n-hexane Oligopeptides Peppers, Chile Peptide Fragments Peptides Powder Pressure Proteins Psychological Inhibition Sodium Chloride Staphylococcal Protein A Suction Drainage Sulfoxide, Dimethyl Temporal epilepsy, familial Vision
2
Purification of Lysosomal Enzymes from Conditioned Media
Culture media were centrifuged at 500 × g for 20 min and filtered (0.45 μm). For AGA, 20% v/v of conditioning buffer (70 mM Tris-HCl, pH 7.0) was added to the media and loaded on column packed with Q-FastFlow Sepharose (GE Healthcare) pre-equilibrated with 5 column volume (CV) equilibration buffer (20 mM Tris-HCl, 20 mM sodium acetate, 70 mM sodium chloride, pH 6.8). After washing the column with 6 CV of wash buffer (20 mM Tris-HCl, 20 mM sodium acetate, 70 mM sodium chloride, pH 6.8), the enzyme was one-step eluted with elution buffer (25 mM sodium acetate, 250 mM NaCl, pH 4.5) into a tube containing 300 mM sodium phosphate (pH 7.3). The eluates were diluted with 50% v/v of 4 M (NH4)2SO4 and further loaded on a Phenyl-Sepharose Fast Flow (high substitution) column (GE Healthcare). After washing and equilibrating the column with 5 CV of 2 M (NH4)2SO4, 20 mM Tris-HCl, pH 7.0, the enzyme was eluted with elution buffer in gradient (2–0 M (NH4)2SO4, 20 mM Tris-HCl, pH 7.0). For GUSB, medium was diluted 3-fold with conditioning buffer (10 mM Tris-HCl, 1 mM β-glycerophosphate, pH 8.0) and loaded on HiTrap DEAE Sepharose Fast Flow column (GE Healthcare) pre-equilibrated with 2 CV conditioning buffer. After washing the column with wash buffer (10 mM Tris-HCl, 1 mM β-glycerophosphate, 50 mM NaCl, pH 8.0), the enzyme was eluted in elution buffer (10 mM Tris-HCl, 1 mM β-glycerophosphate, 300 mM NaCl, pH 8.0). Eluates were diluted in 3-fold volume of conditioning buffer (10 mM Tris-HCl, 1 mM β-glycerophosphate, pH 8.0) and loaded on Mono-Q column (GE Healthcare) and eluted with elution buffer in gradient (0–1 M NaCl, 10 mM Tris-HCl, 1 mM β-glycerophosphate, pH 8.0). For CTSD, medium was diluted 3:1 (v/v) with conditioning buffer (100 mM Tris, 40 mM imidazole 1.2 M NaCl, pH 8.0) and loaded on a 1 mL packed Histrap column (GE Healthcare) pre-equilibrated with 5 CV of conditioning buffer (25 mM Tris, 10 mM imidazole, 300 mM NaCl, pH 8.0). The column was washed with 5CV of conditioning buffer and the enzyme was eluted with 4CV of elution buffer (250 mM imidazole, 25 mM Tris, 300 mM NaCl, pH8.0). For TPP1, medium was diluted 3:1 (v/v) with conditioning buffer (20 mM Tris–HCl, pH 7.6) and loaded on DEAE-Sepharose Fast Flow column pre-equilibrated with 5 CV of conditioning buffer. The enzyme was eluted stepwise with 25, 100, 200 mM, 400 mM NaCl in 2 CV of conditioning buffer. Eluates were diluted with 3X volume of conditioning buffer and thereafter loaded onto Mono-Q column and eluted with gradient NaCl (0-1 M NaCl, 20 mM Tris–HCl, pH 7.6). For GAA, medium was dialysed over night and loaded on a DEAE-Sepharose Fast Flow column pre-equilibrated with 5 CV of 25 mM MES, pH 6.5. The enzyme was eluted in one step with 200 mM NaCl in 2 CV of 25 mM MES, pH 6.5. Eluates were adjusted to 1 M (NH4)2SO4 and loaded on a Phenyl-Sepharose Fast Flow column pre-equilibrated with 25 mM MES, 1 M (NH4)2SO4, pH 6,5. The enzyme was eluted one step at 50 mM (NH4)2SO4 in 25 mM MES. The eluates were buffer exchanged and further loaded on Mono-Q column and eluted in gradient in 0–1 M NaCl, 25 mM MES, pH 6.5. For IDS, medium was dialysed overnight and loaded on a DEAE-Sepharose Fast Flow column pre-equilibrated with 5 CV of 25 mM MES, pH 6.5. The enzyme was eluted one step with 200 mM NaCl in 2 CV of 25 mM MES, pH 6.5. Eluates were adjusted to 2 M NaCl and loaded on a Phenyl-Sepharose Fast Flow column pre-equilibrated with 25 mM MES, 2 M NaCl, pH 6,5. The enzyme was eluted one step at 150 mM NaCl in 25 mM MES, pH 6,5. The eluates were buffer exchanged and further loaded on Mono-Q column and eluted in gradient in 0–1 M NaCl, 25 mM MES, pH 6.5.
Chen Y.H., Tian W., Yasuda M., Ye Z., Song M., Mandel U., Kristensen C., Povolo L., Marques A.R., Čaval T., Heck A.J., Sampaio J.L., Johannes L., Tsukimura T., Desnick R., Vakhrushev S.Y., Yang Z, & Clausen H. (2023). A universal GlycoDesign for lysosomal replacement enzymes to improve circulation time and biodistribution. Frontiers in Bioengineering and Biotechnology, 11, 1128371.
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Publication 2023
2-diethylaminoethanol beta-glycerol phosphate Buffers CTSD protein, human Enzymes imidazole Mono Q phenyl-sepharose Sepharose Sodium Acetate Sodium Chloride sodium phosphate Tromethamine
3
Purification and Characterization of Heparan Sulfate
1 g (wet weight) C57/Bl6 embryonic day 18 mouse embryos or D. melanogaster 1st–3rd instar embryos were homogenized and digested overnight in 320 mM NaCl and 100 mM sodium acetate (pH 5.5) containing 1 mg/mL pronase at 40°C. The digested samples were diluted 1:3 in water and 2.5-mL aliquots were applied to DEAE Sephacel columns. HS was eluted and applied to PD-10 (Sephadex G25) columns (GE Healthcare), lyophilized, redissolved in 20 μL water, digested with chondroitinase ABC overnight as indicated, and again purified by DEAE chromatography. Samples were diluted and again applied to PD-10 columns prior to lyophilization. β-elimination of peptides was omitted from this purification protocol to allow for HS coupling to NHS-activated Sepharose via the attached peptides. We confirmed efficient HS coupling to NHS-activated Hi-Trap FPLC columns by using soluble alkaline phosphatase-coupled Fgf8 and VEGF as previously described (Farshi et al., 2011 (link)). HS binding of Shh/Hh was then determined by FPLC (Äkta protein purifier). Samples were applied to the columns in the absence of salt, and bound material was eluted with a linear 0–1 M NaCl gradient in 0.1 M phosphate buffer (pH 7.0). Eluted fractions were quantified as described above. Shh and Hh binding to heparin columns (GE Healthcare) was carried out with the same protocol, except for elution in a linear 0–1.5 M NaCl gradient in 0.1 M sodium phosphate buffer (pH 7.0).
Manikowski D., Steffes G., Froese J., Exner S., Ehring K., Gude F., Di Iorio D., Wegner S.V, & Grobe K. (2023). Drosophila hedgehog signaling range and robustness depend on direct and sustained heparan sulfate interactions. Frontiers in Molecular Biosciences, 10, 1130064.
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Publication 2023
2-diethylaminoethanol Alkaline Phosphatase Buffers Chondroitin ABC Lyase Chromatography Drosophila melanogaster Embryo FGF8 protein, human Freeze Drying Heparin Mice, House Peptides Phosphates Pronase Proteins sephadex Sepharose Sodium Acetate Sodium Chloride sodium phosphate Vascular Endothelial Growth Factors
4
Evaluating MERS-CoV Infection in Huh7 and MRC5 Cells
Huh7 cells (JCRB, No. JCRB0403) were infected with wt or modified rMERS-CoV at a multiplicity of infection (MOI) of 0.01 or 5, to analyze multi- or single-cycle infections, respectively. MOI 0.01 or 1 was used to infect MRC5 cells (CCL-171, ATCC). The rMERS-CoV inoculum was prepared in PBS containing DEAE (0.005% w/v) and 2% FCS, which was put on the cells after removing the medium. Inocula were removed after 1 h at 37 °C and EMEM supplemented with antibiotics, and 2% FCS was added to the cells. Following a high-MOI infection, cells were first washed three times with PBS before adding medium. Supernatants were harvested at various time points and rMERS-CoV titers were determined by plaque assay on Huh7 cells (JCRB, No. JCRB0403). Significance relative to the wt virus control was calculated using an unpaired Student’s t test and P values of less than 0.05 were considered statistically significant.
Myeni S.K., Bredenbeek P.J., Knaap R.C., Dalebout T.J., Morales S.T., Sidorov I.A., Linger M.E., Oreshkova N., van Zanen-Gerhardt S., Zander S.A., Enjuanes L., Sola I., Snijder E.J, & Kikkert M. (2023). Engineering potent live attenuated coronavirus vaccines by targeted inactivation of the immune evasive viral deubiquitinase. Nature Communications, 14, 1141.
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Publication 2023
2-diethylaminoethanol Antibiotics Biological Assay Cells Infection Senile Plaques Student Virus
5
Purification of hOAT Recombinant Variants
hOAT recombinant variants were purified from E. coli expression and subsequent cell lysis following the steps previously described [5 (link)]. The soluble fraction of the lysate was loaded on a DEAE Sepharose 26/20 equilibrated with 20 mM sodium phosphate buffer, pH 7.6. Then, a gradient from 20 to 200 mM sodium phosphate buffer, pH 7.6, was applied. Under these conditions, both hOAT wild-type and pathogenic variants eluted at a concentration of sodium phosphate between 110 and 160 mM. By using an Amicon Ultra 15 unit (Merck & Co, Rahway, NJ, USA), fractions containing the hOAT enzymes were concentrated and then loaded on a Superdex 200XK 16/60 column (GE Healthcare, Chicago, IL, USA) equilibrated in 50 mM HEPES pH 8.0, 200 mM NaCl. Purified proteins were finally concentrated and stored at −20 °C. The purity of each preparation assessed by SDS-PAGE was >95%.
Floriani F., Borri Voltattorni C., Cellini B, & Montioli R. (2023). Biochemical and Bioinformatic Studies of Mutations of Residues at the Monomer–Monomer Interface of Human Ornithine Aminotransferase Leading to Gyrate Atrophy of Choroid and Retina. International Journal of Molecular Sciences, 24(4), 3369.
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Publication 2023
2-diethylaminoethanol Buffers Cells Enzymes Escherichia coli HEPES Pathogenicity Proteins SDS-PAGE Sepharose Sodium Chloride sodium phosphate

Top products related to «2-diethylaminoethanol»

1
Deae sepharose fast flow by GE Healthcare
Sourced in United States, Sweden, China, United Kingdom
DEAE Sepharose Fast Flow is a pre-swollen, high-flow agarose-based ion exchange medium suitable for the purification of biomolecules. It has a positively charged diethylaminoethyl (DEAE) functional group and a high dynamic binding capacity.
2
Deae sepharose by GE Healthcare
Sourced in United States, United Kingdom, Sweden
DEAE-Sepharose is a chromatography resin used for the purification and separation of biomolecules, such as proteins, enzymes, and nucleic acids. It is an anion exchange material that can be used in a variety of applications, including protein purification, enzyme isolation, and DNA/RNA separation.
3
Deae sepharose fast flow column by GE Healthcare
Sourced in Sweden, United States
The DEAE Sepharose fast flow column is a versatile chromatography media used for the purification of biomolecules. It is composed of cross-linked agarose beads with diethylaminoethyl (DEAE) functional groups, which enable the separation and purification of charged molecules such as proteins, enzymes, and nucleic acids based on their ionic interactions with the column resin.
4
Deae filtermat by PerkinElmer
The DEAE filtermat is a laboratory equipment designed for the filtration and separation of biomolecules. It is a diethylaminoethyl (DEAE) cellulose matrix that can be used for the purification of proteins, nucleic acids, and other macromolecules. The DEAE filtermat provides a high surface area for efficient adsorption and separation of target molecules.
5
Hitrap deae ff column by GE Healthcare
Sourced in Sweden
The HiTrap DEAE FF column is an ion exchange chromatography column designed for the purification of biomolecules. It features a diethylaminoethyl (DEAE) resin that operates at a high flow rate, enabling efficient separation and purification. The column's core function is to facilitate the capture and separation of charged molecules, such as proteins, nucleic acids, and other biomolecules, based on their interactions with the DEAE functional groups.
6
Deae sepharose column by GE Healthcare
Sourced in United States
The DEAE Sepharose column is a chromatography column used for the purification and separation of biomolecules. It is composed of Sepharose, a cross-linked agarose-based matrix, which has been functionalized with diethylaminoethyl (DEAE) groups. The DEAE groups provide a positively charged ion exchange functionality that can interact with negatively charged molecules, enabling their separation and purification from complex mixtures.
7
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.
8
Hitrap deae ff by GE Healthcare
Sourced in United States, United Kingdom
HiTrap DEAE FF is a pre-packed column for ion exchange chromatography. It is designed for rapid and easy purification of biomolecules, such as proteins, peptides, and nucleic acids. The column contains diethylaminoethyl (DEAE) ion exchange media, which allows for the separation and purification of molecules based on their charge characteristics.
9
Deae sepharose by Merck Group
Sourced in United States, Germany
DEAE-Sepharose is a chromatography matrix used for the purification and separation of biomolecules. It is composed of cross-linked agarose beads with diethylaminoethyl (DEAE) functional groups. DEAE-Sepharose is an anion-exchange material that can be used to purify proteins, nucleic acids, and other charged molecules based on their different affinities to the positively charged DEAE groups.
10
Deae sephacel by GE Healthcare
Sourced in Sweden, United States
DEAE-Sephacel is a strong anion exchange resin used for the purification and separation of biomolecules, such as proteins and nucleic acids, in laboratory settings. It is a matrix made of cross-linked agarose beads with diethylaminoethyl (DEAE) functional groups attached, which allows for the reversible binding of negatively charged molecules. The core function of DEAE-Sephacel is to facilitate the chromatographic separation and purification of target biomolecules from complex mixtures.

More about "2-diethylaminoethanol"

2-Diethylaminoethanol (DEAE) is a versatile chemical compound with the formula C6H15NO.
It is a secondary amine and an alcohol, commonly used as a chemical intermediate in the production of pharmaceuticals, agricultural chemicals, and other industrial products.
DEAE is a key component in various chromatography techniques, such as DEAE Sepharose Fast Flow, DEAE-Sepharose, DEAE Sepharose fast flow column, DEAE filtermat, HiTrap DEAE FF column, and DEAE Sepharose column.
These ion exchange resins are widely used in the purification and separation of biomolecules, including proteins, nucleic acids, and other compounds.
In addition to its industrial applications, DEAE is also used in cell culture media, such as FBS (Fetal Bovine Serum), to maintain cellular growth and differentiation.
The HiTrap DEAE FF column is a popular choice for the purification of recombinant proteins and other biomolecules.
Whether you're working with pharmaceuticals, agricultural chemicals, or biomolecules, PubCompare.ai's AI-driven protocol comparison tool can help you optimize your 2-diethylaminoethanol (DEAE) research.
Quickly locate relevant protocols from literature, pre-prints, and patents, and use our AI-powered comparisons to identify the best protocols and products for your needs.
Streamline your research with PubCompare.ai's intelligent platform and take your DEAE-related work to the next level.