DEAE-Cellulose is a positively charged ion exchange resin commonly used in biochemical and molecular biology applications.
It is derived from cellulose, a natural polysaccharide, and contains diethylaminoethyl (DEAE) functional groups that can bind and separate biomolecules such as proteins, nucleic acids, and other charged compounds.
DEAE-Cellulose is widely utilized in purification, fractionation, and chromatographic techniques to isolate and concentrate target analytes from complex samples.
Its versatility and ease of use make it an indispensable tool in reseach laboratories studying a vareity of biological systems and processes.
The procedures described here are for 50 mL of urea-solubilized inclusion bodies originating from 4.5 L of culture, but this process can be scaled proportionally for other amounts. The urea-solubilized inclusion bodies (50 mL) were diluted with 150 mL of 10 mm Tris/HCl pH 8.0 containing 1 mm EDTA (buffer A), added to 50 mL DEAE-cellulose equilibrated in buffer A, and gently agitated for 20 min. The slurry was then applied to a Büchner funnel with filter paper on a vacuum glass bottle [alternatively, a Nalgene (Lima, OH, USA) 0.45 μm filter on a vacuum bottle can be used]. Subsequently, the resin was washed with buffer A (50 mL), followed by stepwise elution using 50 mL aliquots of buffer A with 50, 75, 100, 125, 150, 200, 250, 300 and 500 mm NaCl, respectively. Each aliquot was incubated with the resin for 5 min before collection under vacuum. Eluates were analyzed by SDS-PAGE and agarose gel electrophoresis, and fractions with highly pure Aβ were pooled and fractionated by centrifugation through a 30 kDa molecular mass cut-off filter. The washing and elution processes can also be performed as follows: the resin is washed with 50 mL buffer A, and then with 50 mL buffer A with 25 mm NaCl followed by three or four 50 mL aliquots of buffer A with 125 mm NaCl. Using SDS-PAGE, the peptide is then found in the first two (or first three) 125 mm aliquots, which are combined and used for centrifugal filtration.
Walsh D.M., Thulin E., Minogue A.M., Gustavsson N., Pang E., Teplow D.B, & Linse S. (2009). A facile method for expression and purification of the Alzheimer’s disease-associated amyloid β-peptide. The Febs Journal, 276(5), 1266-1281.
Purification of Squid Rhodopsin—All procedures were carried out at room temperature in the dark or under dim red light unless otherwise indicated. Squid rhodopsin was prepared from Todarodes pacificus caught in the Japan Sea, using previously described methods (13 ). Briefly, the rhabdomeric membranes were isolated from squid retina by repetitive sucrose flotation. The membranes were treated with V8 protease (Pierce, 50:1 w/w of rhodopsin:V8 protease) at room temperature for 1 h to remove the unique C-terminal proline-rich extension of the squid rhodopsin. The reaction was terminated by extensive washing with HEPES buffer (5 mm HEPES, pH 7.0, 1 mm EDTA, 1 mm dithiothreitol). The membranes were solubilized with 2% (w/v) dodecyl maltoside (DDM, Anatrace) for 1 h at 4 °C. After centrifugation, the supernatant was loaded onto a DEAE-cellulose column (Whatman) equilibrated with buffer A (50 mm HEPES, pH 7.0, 0.05% (w/v) DDM). The unbound fraction was collected and applied to a concanavalin A-Sepharose 4B column (Amersham Biosciences) equilibrated with buffer A. The rhodopsin was eluted with 0.2 m α-methyl mannoside solution. Fractions containing squid rhodopsin were pooled and dialyzed against buffer A and then concentrated by ultrafiltration (Amicon Ultra, Millipore). N-terminal Sequencing and Mass Analyses—The identity and integrity of the purified protein were assessed by N-terminal amino acid sequencing by Edman degradation and various mass spectrometric analyses, including MALDI-TOF/MS, MALDI-TOF/TOF-MS/MS, nano-liquid chromatographyquadrapole TOF-MS/MS, and high performance liquid chromatography-electrospray ionization-iontrap-MS/MS as described in the supplemental materials (14 (link)). Crystallization—Crystals were grown by the hanging-drop vapor diffusion method. One microliter of protein sample (10 mg/ml) in a solution of 10 mm HEPES, pH 7.0, 200 mm NaCl, 2 mm dodecyldimethylamine oxide, 0.03% (w/v) DDM was mixed with 1 μl of reservoir solution (0.1 m HEPES, pH 7.0, 8% (v/v) ethylene glycol, 28% (w/v) polyethylene glycol 400) and left to equilibrate at 20 °C. Crystals appeared after 5 days and stopped growing within 2 weeks. Structure Determination and Refinement—X-ray diffraction data were collected at 100 K on beam line BL45XU at SPring-8. Data were reduced using the program HKL2000 (15 ). The structure was determined by molecular replacement with the program MOLREP in the CCP4 program suite (16 (link)) using a monomer of the trigonal crystal structure of the bovine rhodopsin (PDB code: 1GZM) (17 ) as a search model. Refinement and model building were performed iteratively with the programs CNS (18 (link)), REFMAC5 in CCP4 (16 (link)), and O (19 (link)). During refinement, we used grouped, unrestrained B-factor refinement with a single group for the entire molecule. All refinements were carried out with 10% of the reflections for cross validation. Despite the low resolution data and the low sequence homology between squid and bovine rhodopsins (24%), the structure was well refined thanks to the structural similarity of the transmembrane helices and the positions for a disulfide bridge, an 11-cis-retinal chromophore in the Schiff base linkage, and the conserved residues. B-factor sharpening was used to generate detailed maps using the CNS program with Bsharp values ranging from –50 to –150 Å2 (20 ). Data collection and refinement statistics are shown in Table 1. All figures including electrostatic potential surfaces were prepared using PyMOL (DeLano Scientific LLC). The coordinates have been deposited in the Protein Data Bank (PDB) with the accession code 2ZIY.
Data collection and refinement statistics
Data collection
Wavelength (Å)
0.97950
Resolution (Å)
43.2-3.7
Measured reflections
43,571
Unique reflections
6,680
Completeness (%)a
93.3 (74.3)
Rmerge (%)b
6.4 (77.5)c
Space group
C2221
Unit cell (Å)
a = 84.3, b = 108.7, c = 142.2
Refinement
Resolution (Å)
43.2-3.7
Reflections used
6,647
Rwork/Rfree (%)d,e
30.2/33.0 (41.4/43.2)
r.m.s.f deviation
bond (Å)
0.014
angle (°)
2.01
Ramachandran statistics
Most favored region (%)
70.4
Additional allowed region (%)
27.1
Generously allowed region (%)
2.1
Disallowed region (%)
0.3
Values in parentheses are for the highest-resolution shell (3.83-3.70 Å).
Rmerge = ∑i|I(h)i — 〈I(h)〉|/∑i|I(h)i|, where 〈I(h)〉 is the mean intensity of equivalent reflections.
The last shell Rmerge is rather high as a result of strong anisotropy.
Rwork = ∑|Fo — Fc|/∑|Fo|, where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.
Rfree = ∑|Fo — Fc|/∑|Fo|, calculated using a test data set, 10% of total data randomly selected from the observed reflections.
r.m.s., root mean square.
Shimamura T., Hiraki K., Takahashi N., Hori T., Ago H., Masuda K., Takio K., Ishiguro M, & Miyano M. (2008). Crystal Structure of Squid Rhodopsin with Intracellularly Extended Cytoplasmic Region. The Journal of Biological Chemistry, 283(26), 17753-17756.
Recombinant Aβ(Met1–42), here referred to as Aβ42, was produced in BL21*(DE3) pLysS E. coli (B strain) cells and purified by ion exchange18 (link). Briefly, the IPTG-induced cells were lysed on ice by sonication for 3 min (2 s on and 2 s off, 65% maximum amplitude), and the pellets were collected by 24,000×g centrifugation at 4 °C for 10 min. The pellets were dissolved by 8 M urea in 10 mM Tris-HCl pH 8.0, which was then diluted with 10 mM Tris−HCl pH 8.0 to 2 M urea for co-incubation (about 20 min in cold room) with DEAE cellulose (GE Healthcare, UK). The DEAE cellulose with bound proteins was washed with 10 mM Tris-HCl pH 8.0 and 10 mM Tris-HCl pH 8.0 containing 25 mM NaCl, respectively, and the recombinant Aβ42 was finally eluted by 125 mM NaCl in 10 mM Tris-HCl pH 8.0. The eluate was passed through a 30 kDa concentration filter, and the filtrate (crude Aβ42) was concentrated by a 5 kDa concentration filter. The crude Aβ42 proteins were lyophilized overnight and re-dissolved in 7 M Gdn-HCl and then injected into a Superdex 75 column (GE Healthcare, UK) for monomer isolation in 20 mM sodium phosphate pH 8.0 with 0.2 mM EDTA and 0.02% NaN3. The Aβ42 concentration was calculated by measuring the absorbance at 280 and 300 nm with an extinction coefficient of 1,424 M−1 cm−1 for (A280-A300). Purified Aβ42 monomers were aliquoted in low-binding Eppendorf tubes (Axygene). For analysis of the kinetics of amyloid fibril formation, 80 µL solution containing 3 µM Aβ42 monomer, 10 µM ThT and different concentrations of various rh Bri2 BRICHOS species were added to each well of half-area 96-well black polystyrene microplates with clear bottom and nonbinding surface (Corning Glass 3881, USA), and incubated under quiescent conditions at 37 °C. The aggregation kinetics of Aβ42 monomer with different concentrations in presence of a constant concentration (0.9 µM) of various Bri2 BRICHOS species were measured in the same manner. The fluorescence was recorded using a 440 nm excitation filter and a 480 nm emission filter (FLUOStar Galaxy from BMG Labtech, Offenberg, Germany). For preparation of Aβ42 seeds, 3 µM Aβ42 monomer was incubated at 37 °C for about 20 h, and the fibrils were then sonicated in a water bath for 3 min. For analysis of Aβ42 fibril formation kinetics in the presence of seeds, 80 µL solution containing 3 µM Aβ42 monomer, 10 µM ThT, different concentrations of rh Bri2 BRICHOS species, and 0.6 µM seeds (calculated from the original Aβ42 monomer concentration) were added at 4 °C to each well in triplicate of half-area 96-well plates and incubated under quiescent conditions at 37 °C. The fluorescence was recorded as described above. The initial slope of the concave aggregation traces was determined by a linear fit to the first 30 min. Aggregation traces were normalized and averaged using 3–4 replicates for all the experiments. For Aβ42 alone, averages were performed using two different runs with 3 replicates each.
Chen G., Abelein A., Nilsson H.E., Leppert A., Andrade-Talavera Y., Tambaro S., Hemmingsson L., Roshan F., Landreh M., Biverstål H., Koeck P.J., Presto J., Hebert H., Fisahn A, & Johansson J. (2017). Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state. Nature Communications, 8, 2081.
Mutagenesis of the human L-PYK gene was performed with Quikchange (Stratagene). Many of the included mutations were created using site-directed random mutagenesis via primers that were degenerate at the target codon. Other mutations were generated with specifically designed primers. Wild type and mutant proteins were expressed in the FF50 strain of Escherichia coli (15 (link)). Wild type protein used for analogue studies was purified using the cell lysis, ammonium sulfate fractionation and DEAE-cellulose column as previously described (15 (link)). Mutant proteins were partially purified using ammonium sulfate fractionation followed by dialysis (16 (link)). Estimates of ligand binding/affinity and allostery were equivalent whether evaluated using purified or ammonium sulfate partially purified protein (Supplemental Figure S1). Therefore, mutant proteins were only partially purified before evaluation, a method that allowed an assessment of considerably more mutations than would have been possible if purification of each was required.
Ishwar A., Tang Q, & Fenton A.W. (2015). Distinguishing the interactions in the fructose-1,6-bisphosphate binding site of human liver pyruvate kinase that contribute to allostery. Biochemistry, 54(7), 1516-1524.
Methanol (p.a.) was purchased from VWR International AB. Ethanol (>99.5%) was purchased from Solveco AB. Toluene (HPLC grade, >99.8%) was purchased from RCI Labscan. Chloroform (≥99.8%), lithium chloride (≥99%), potassium hydroxide, sulfuric acid (95–97%), acetic acid glacial (100%), dichloromethane (anhydrous, stabilized with amylene, ≥99.8%), acetic anhydride (p.a., >99.5%), pyridine (>99.5%), anisaldehyde (4-methoxybenzaldehyde, for synthesis), and resorcinol were purchased from Sigma-Aldrich, Merck KGaA (Darmstadt, Germany). Silica gel S (particle size: 32–63 μm, 230–400 mesh ASTM) were purchased from Riedel-de Haën. DEAE-cellulose 23 was purchased from Whatman. Polyisobutylmethacrylate was purchased from Sigma-Aldrich. Deionized water (Milli Q) was prepared with Purelab Flex 2 water purification system (AB Ninolab) and all organic solvents were redistilled prior to use.
Hořejší K., Jin C., Vaňková Z., Jirásko R., Strouhal O., Melichar B., Teneberg S, & Holčapek M. (2023). Comprehensive characterization of complex glycosphingolipids in human pancreatic cancer tissues. The Journal of Biological Chemistry, 299(3), 102923.
Using our previous literature as a guide, we extracted polysaccharides from LTC [18 ]. Dried crushed whole Pyrola corbieri Levl (4.5 kg) was refluxed three times for two hours with 80% ethanol (22 L) to remove some potential impurities, such as monosaccharides, oligosaccharides and fat-soluble substances. After alcohol extraction, the residues were extracted with distilled water (30 L) and refluxed every 2 h three times. The aqueous extract was vacuum-concentrated and treated with four volumes of ethanol overnight. The resulting precipitate was collected via filtration, washed with anhydrous ethanol and acetone, and then vacuum-dried. The precipitates were dissolved in ultrapure water and deproteinized by the Sevag method. After resolving the crude polysaccharide in distilled water, it was precipitated with anhydrous ethanol. The resulting precipitate (named LTC) was vacuum-dried at 60 ℃ and yielded a grayish power. The LTC was eluted with distilled water using a DEAE-cellulose column (4.5 × 30 cm), and then a gradient of NaCl solution (0.05, 0.1, 0.2, 0.5, 1.0 M, respectively). The samples were further purified and eluted with 0.2 M NaCl on a Sephacryl-300 column (2.6 × 100 cm). The main fraction was gathered, concentrated, dialyzed, and lyophilized to produce LTC-1, a purified polysaccharide sample.
Li L., Yu K., Mo Z., Yang K., Chen F, & Yang J. (2023). In Vitro Neurotrophic Properties and Structural Characterization of a New Polysaccharide LTC-1 from Pyrola corbieri Levl (Luticao). Molecules, 28(4), 1544.
Pyrola corbieri Levl was collected in Guiyang city, Guizhou Province, PR China, in June 2018 and was authenticated by Prof. Qingwen Sun, Guizhou University of Traditional Chinese Medicine. A voucher specimen (No. 201806LTC) was deposited at the Key Laboratory of Chemistry for Natural Products of Guizhou Province and Chinese Academy of Sciences. DEAE-cellulose was supplied by Shanghai Hengxin Chemical Reagent Co., Ltd. (Shanghai, China), and Sephacryl-300 was purchased from Amersham Biosciences (Uppsala, Sweden). Galacturonic acid and the standards dextrans T-40 (Mw: 40 kDa), T-25 (Mw: 25 kDa), T-12 (Mw: 12 kDa), T-5 (Mw: 5 kDa) and T-1 (Mw: 1 kDa) were provided by Sigma Chemical Co. (MO, USA). D-mannose, D-glucose, D-galactose, D-xylose, D-fucose, L-rhamnose and L-arabinose were purchased from Shanghai Chemical Reagents Company (Shanghai, China). The pheochromocytoma cell line (PC12) was purchased from Shanghai Institute of Biochemistry and Cell Biology (Shanghai, China). The acetylcholinesterase kit and Pierce BCA protein kit were purchased from Shanghai Genmed Scientifics Co., Ltd. (Shanghai, China). GAP-43 (7B10) antibody was obtained from Santa Cruz Biotechnology, Inc. (Dallas, TX, USA). An Enhanced ECL Chemiluminescent Substrate Kit was purchased from PerkinElmer Life Sciences (Boston, MA, USA). Green fluorescent protein (GFP) transgenic mice (18 days gestation) were a kind gift from Professor Zhenggang Yang (Institute of Brain Science, Fudan University, Shanghai, China). Trypsin was acquired from Gibco-Life Technologies (Grand Island, NY, USA). DNAase and Trolox were purchased from Sangon Biotech Co., Ltd. (Shanghai, China).
Li L., Yu K., Mo Z., Yang K., Chen F, & Yang J. (2023). In Vitro Neurotrophic Properties and Structural Characterization of a New Polysaccharide LTC-1 from Pyrola corbieri Levl (Luticao). Molecules, 28(4), 1544.
The specific separation and purification process was shown in Supplementary Materials Figure S1. Tersely, the dried Black bean was decorticated, smashed, defatted, and then extracted 3 times using the distilled water at 80 °C for two hours. The supernatant was collected and precipitated with alcohol. The collected sediment was again dissolved by the distilled water to be dialyzed and lyophilized to get the Black bean crude extraction. Finally, a polysaccharide was separated from the crude extraction by using distilled water as the eluent through the DEAE-52 cellulose (Cl− form) and Sephadex G-100 columns.
Li P., Hu Y., Zhan L., He J., Lu J., Gao C., Du W., Yue A., Zhao J, & Zhang W. (2023). A Natural Glucan from Black Bean Inhibits Cancer Cell Proliferation via PI3K-Akt and MAPK Pathway. Molecules, 28(4), 1971.
As previously described, Ln. pseudomesenteroides was cultured in 1 L MRS-S fermentation medium at 30 °C for 48 h [14 (link)]. Cell-free supernatant (CFS) containing crude glucansucrase from the bacterial strain was obtained by centrifugation at 8000× g for 15 min at 4 °C. Crude glucansucrase was separated and purified by ammonium sulfate precipitation, dialysis and ion exchange chromatography (DEAE-cellulose FF, S8800, Sigma, St. Louis, MI, USA) and gel filtration (Sephadex G-75, S8186, Sigma, St. Louis, MI, USA). The purified glucansucrase fraction was concentrated using ultrafiltration centrifuge tubes and subsequently characterized further. The SDS-PAGE was used to determine the molecular weight. Glucansucrase activity was determined in 50 mM pH 5.4 sodium acetate buffer including 1 mM CaCl2 and 100 mM sucrose at 37 °C [15 (link)]. One glucansucrase unit (U) was defined as the amount of enzyme capable of releasing 1 mmol/min of fructose from sucrose.
Du R., Yu L., Sun M., Ye G., Yang Y., Zhou B., Qian Z., Ling H, & Ge J. (2023). Characterization of Dextran Biosynthesized by Glucansucrase from Leuconostoc pseudomesenteroides and Their Potential Biotechnological Applications. Antioxidants, 12(2), 275.
DEAE-cellulose is a type of ion-exchange chromatography media. It is composed of cellulose that has been derivatized with diethylaminoethyl (DEAE) groups. DEAE-cellulose is used for the purification and separation of biomolecules, such as proteins and nucleic acids, based on their ionic interactions with the DEAE functional groups.
DEAE-52 cellulose is a chromatography medium used for the separation and purification of biomolecules. It is a diethylaminoethyl (DEAE) cellulose derivative with a strong anion exchange functionality. The core function of DEAE-52 cellulose is to facilitate the separation and isolation of various biomolecules, such as proteins, nucleic acids, and other charged species, based on their differences in charge interactions with the DEAE groups.
DEAE-52 cellulose is an ion exchange chromatography media used for the purification of various biomolecules, such as proteins, enzymes, and nucleic acids. It consists of diethylaminoethyl (DEAE) functional groups covalently bound to a cellulose matrix. The DEAE groups provide a positive charge, allowing for the adsorption and separation of negatively charged molecules based on their charge differences.
Sephadex G-100 is a size-exclusion chromatography media used for the separation and purification of molecules based on their size and molecular weight. It is a porous, cross-linked dextran gel that allows smaller molecules to penetrate the pores while larger molecules are excluded, enabling their separation. Sephadex G-100 is commonly used in various applications such as protein purification, desalting, and molecular weight determination.
Sourced in United States, Germany, United Kingdom, China, Italy, Japan, France, Sao Tome and Principe, Canada, Macao, Spain, Switzerland, Australia, India, Israel, Belgium, Poland, Sweden, Denmark, Ireland, Hungary, Netherlands, Czechia, Brazil, Austria, Singapore, Portugal, Panama, Chile, Senegal, Morocco, Slovenia, New Zealand, Finland, Thailand, Uruguay, Argentina, Saudi Arabia, Romania, Greece, Mexico
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.
Monosaccharide standards are reference materials used to identify and quantify monosaccharides in various samples. These standards provide known concentrations of individual monosaccharides, which can be used to calibrate analytical instruments and verify the accuracy of monosaccharide measurements.
DEAE-cellulose 52 is a chromatography resin used for the purification of biomolecules. It is made of cellulose derivatized with diethylaminoethyl (DEAE) functional groups, which allow for the separation and isolation of charged molecules through ion-exchange chromatography.
Sourced in United States, Germany, China, United Kingdom, Switzerland, Sao Tome and Principe, Italy, France, Canada, Singapore, Japan, Spain, Sweden
Galactose is a monosaccharide that serves as a core component in various laboratory analyses and experiments. It functions as a fundamental building block for complex carbohydrates and is utilized in the study of metabolic processes and cellular structures.
Sourced in United States, Germany, United Kingdom, China, France, Italy, Spain, Sao Tome and Principe, Macao, Switzerland, Poland, Japan, India, Canada, Belgium, Denmark, Australia, Sweden, Brazil, Austria, Singapore, Israel, Portugal, Argentina, Mexico, Norway, Greece, Ireland
Glucose is a laboratory equipment used to measure the concentration of glucose in a sample. It is a fundamental tool in various medical and scientific applications, including the diagnosis and monitoring of diabetes, metabolic research, and food analysis.
Sourced in United States, Germany, United Kingdom, China, Italy, Sao Tome and Principe, France, Macao, India, Canada, Switzerland, Japan, Australia, Spain, Poland, Belgium, Brazil, Czechia, Portugal, Austria, Denmark, Israel, Sweden, Ireland, Hungary, Mexico, Netherlands, Singapore, Indonesia, Slovakia, Cameroon, Norway, Thailand, Chile, Finland, Malaysia, Latvia, New Zealand, Hong Kong, Pakistan, Uruguay, Bangladesh
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.
DEAE-Cellulose is generally easy to use, but a few common challenges include ensuring proper buffer selection to maintain optimal binding/elution conditions, minimizing non-specific binding of unwanted biomolecules, and effectively regenerating and reusing the resin over multiple purification cycles. Careful optimization of parameters like pH, ionic strength, and flow rates can help overcome these hurdles.
Yes, there are several variations of DEAE-Cellulose, including different bead sizes, degrees of substitution, and matrix compositions. These can impact factors like binding capacity, flow characteristics, and compatibility with specific applications. For example, some DEAE-Cellulose resins are designed for larger-scale preparative chromatography, while others are better suited for analytical or small-scael purifications.
DEAE-Cellulose is versitle and can be used in a wide range of applications, including: Protein purification - DEAE-Cellulose can be used to isolate and concentrate target proteins from complex mixtures. Nucleic acid purification - The resin can bind and separate DNA, RNA, and oligonucleotides. Enzyme purification - Many enzymes can be effectively purified using DEAE-Cellulose chromatography. Small molecule separation - The technology can also be leveraged to isolate and purify charged low-molecular weight compounds.
PubCompare.ai's AI-driven platform can greatly assist with DEAE-Cellulose research in several ways. First, it allows you to efficiently screen the vast literature on DEAE-Cellulose protocols, including publications, preprints, and patents. The platform's advanced comparision tools can then hightlight the key differences between protocols, helping you identify the most effective and reproducible procedures for your specific needs. Theis can save valuable time and resources compared to manually reviewing the literature. Additionally, the AI analysis can reveal critical insights you may have missed, enalbing you to optimize your DEAE-Cellulose purification workflow and get better results.
Yes, generally speaking DEAE-Cellulose is relatively easy to regenerate and reuse over multiple purification cycles. The resin can typically be cleaned and recharged by washing with high-salt buffers to remove bound biomolecules, followed by re-equilibration in the starting buffer. This allows the DEAE-Cellulose to be reused, which can be cost-effextive compared to single-use disposable resins. However, it's important to monitor performance and occasionally replace the resin if binding capacity or selectivity starts to degrade over time.
More about "DEAE-Cellulose"
DEAE-Cellulose is a versatile ion exchange resin derived from the natural polysaccharide cellulose.
It contains diethylaminoethyl (DEAE) functional groups that can bind and separate a variety of biomolecules, including proteins, nucleic acids, and other charged compounds.
This makes DEAE-Cellulose an indispensable tool in biochemical and molecular biology research.
DEAE-Cellulose is commonly used in purification, fractionation, and chromatographic techniques to isolate and concentrate target analytes from complex samples.
It is available in different forms, such as DEAE-52 cellulose, which is a popular variant.
DEAE-Cellulose can be used in conjunction with other materials like Sephadex G-100, a size exclusion chromatography resin, and Bovine serum albumin, a common protein standard.
Monosaccharide standards, such as Galactose and Glucose, are often used to evaluate the performance and effectiveness of DEAE-Cellulose in separation and purification experiments.
DMSO, a versatile solvent, is also sometimes employed in DEAE-Cellulose-based protocols.
Researchers in a vareity of biological fields, from enzymology to molecular genetics, rely on DEAE-Cellulose to advance their studies.
Its ease of use and versatility make it an indispensable tool in modern research laboratories.
