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> Chemicals & Drugs > Organic Chemical > 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate

3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate

3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfnate is a zwitterionic detergent used in a variety of biological applications, including membrane protein solubilization and purification.
It has amphoteric properties, allowing it to solubilize both hydrophilic and hydrophobic molecules.
The compound is often used in biochemistry and cell biology research to maintain the native structure and function of membrane proteins during extraction and analysis.
Rigorous comparison of experimental protocols is crucial for ensuring reproducibility in 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate-based studies.

Most cited protocols related to «3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate»

1
Cell Lysis and Inhibitor Screening
Cited 22 times

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Publication 2011
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Buffers Cells Centrifugation HEPES manganese chloride Nonidet P-40 Pellets, Drug Phosphoric Monoester Hydrolases Sodium Chloride Syringes Tergitol Triton X-100 Tromethamine
2
Quantifying H1 Histone Binding Affinity
Cited 19 times
For assays used to determine the binding affinity of H1 to nucleosomes and DNA, labeled H10 was diluted into binding buffer, consisting of 10 mM Tris pH 7.5, 150 mM KCl, 1 mM DTT, 5% Glycerol, 0.01% CHAPS, 0.01% NP-40 (nonidet p40 substitute; Fluka), to a concentration 2-fold greater than the desired final reaction concentration. The final H1 reaction concentration was 0.1 nM and 0.5 nM for nucleosomes and DNA, respectively. Nucleosomes or DNA were serially diluted in binding buffer into multiple master stocks for each order of magnitude (e.g. 0.2 nM, 2 nM, 20 nM, etc.). Each master stock was then used to create an experimental titration series 2-fold greater than the desired final concentration; typically performed in 200 µl PCR tubes (Genemate) or 384-deepwell low binding polypropylene plates (Eppendorf). For each replicate titration series, 20 µl of every 2-fold substrate dilution was then pipetted into a single row of the microplate using a 12-channel pipettor followed by 20 µl of the 2× H1 stock. The microplate was then quick spun at 500–2000 rpm, shaken for 2 min (VortexGenie 2) at speed no higher than 2, allowed to incubate 15–20 min at room temperature, and then imaged on a Typhoon Trio multimode imager (GE Healthcare). Images were collected with a 488 nm excitation laser and a 520 bp40 emission filter at 600 V PMT and scanned at +3 mm with press ‘on’ at 100 µm. Images were analyzed with the Array Analysis function of ImageQuant TL software by making an array with squares slightly smaller than the dimensions of each well. The data from each well were plotted in GraphPad Prism software and fit to a single exponential binding curve with a Hill coefficient using the following equation, based upon Reaction Scheme 1, where P is protein and L is the ligand:
Hieb A.R., D'Arcy S., Kramer M.A., White A.E, & Luger K. (2011). Fluorescence strategies for high-throughput quantification of protein interactions. Nucleic Acids Research, 40(5), e33.
Publication 2011
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Biological Assay Buffers DNA Replication Glycerin Ligands nonidet Nonidet P-40 Nucleosomes Polypropylenes prisma Proteins Technique, Dilution Titrimetry TRIO protein, human Tromethamine Typhoons
3
HaloTag Ligand Absorbance Measurement
Cited 18 times
Absorbance measurements were performed in 1 mL quartz cuvettes. HaloTag protein was used as a 100 μM solution in 75 mM NaCl, 50 mM TRIS·HCl, pH 7.4 with 50% v/v glycerol (TBS–glycerol). HaloTag ligands 27 and 28 (5 μM) were dissolved in 10 mM HEPES, pH 7.3 containing 0.1 mg·mL−1 CHAPS. An aliquot of HaloTag protein (1.5 equiv) or an equivalent volume of TBS–glycerol blank was added and the resulting mixture was incubated until consistent absorbance signal was observed (~30 min). Additional HaloTag protein did not elicit an increase in absorbance (not shown). Absorbance scans are averages (n = 2).
Grimm J.B., English B.P., Chen J., Slaughter J.P., Zhang Z., Revyakin A., Patel R., Macklin J.J., Normanno D., Singer R.H., Lionnet T, & Lavis L.D. (2015). A general method to improve fluorophores for live-cell and single-molecule microscopy. Nature methods, 12(3), 244-250.
Publication 2014
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Glycerin HaloTag HEPES Ligands Proteins Quartz Radionuclide Imaging Sodium Chloride Synapsin I Tromethamine
4
HaloTag Ligand Absorbance Measurement
Cited 18 times
Absorbance measurements were performed in 1 mL quartz cuvettes. HaloTag protein was used as a 100 μM solution in 75 mM NaCl, 50 mM TRIS·HCl, pH 7.4 with 50% v/v glycerol (TBS–glycerol). HaloTag ligands 27 and 28 (5 μM) were dissolved in 10 mM HEPES, pH 7.3 containing 0.1 mg·mL−1 CHAPS. An aliquot of HaloTag protein (1.5 equiv) or an equivalent volume of TBS–glycerol blank was added and the resulting mixture was incubated until consistent absorbance signal was observed (~30 min). Additional HaloTag protein did not elicit an increase in absorbance (not shown). Absorbance scans are averages (n = 2).
Grimm J.B., English B.P., Chen J., Slaughter J.P., Zhang Z., Revyakin A., Patel R., Macklin J.J., Normanno D., Singer R.H., Lionnet T, & Lavis L.D. (2015). A general method to improve fluorophores for live-cell and single-molecule microscopy. Nature methods, 12(3), 244-250.
Publication 2014
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Glycerin HaloTag HEPES Ligands Proteins Quartz Radionuclide Imaging Sodium Chloride Synapsin I Tromethamine
5
Reconstitution of CLC-ec1 chloride channel
Cited 18 times
Chemicals and other materials were of reagent quality. Expression, His-tag cleavage, purification, and liposome reconstitution of CLC-ec1, the product of Escherichia coli gene clcA (accession P37019), were performed as previously described (Accardi et al., 2004 (link)), except that for samples used in liposome fluxes, the final purification step was gel filtration on Superdex 200 rather than anion exchange chromatography on Poros HQ, which was used exclusively for planar lipid bilayer experiments. All preparations (typically 1–10 mg/ml in 5–20 mM decylmaltoside) were checked by overloaded SDS-PAGE to be free of His-tagged and other contaminating bands. Point mutants were constructed by conventional PCR methods and were fully sequenced. All mutants reported expressed well (1–3 mg/liter culture) and gave gel filtration profiles identical to the wild-type homodimer.
Liposomes were formed within 1 d of protein preparation by 30-h dialysis of micellar solutions containing E. coli polar lipid (Avanti, 20 mg/ml), detergent (Chaps, 35 mM), and protein (0.03–50 μg/mg lipid). Protein concentration is reported throughout as protein/lipid weight ratio, denoted “protein density.” Liposomes used for planar bilayer recording were prepared at a protein density of 50 μg/mg in 450 mM KCl, 25 mM KH2PO4, 22.5 mM K3-citrate, 2.5 mM citric acid, pH 7.5. Liposomes used for flux measurements were formed with protein at 0.03–5 μg/mg, 300 mM KCl, and buffered with 25 mM citrate for Cl− flux experiments or 25 mM citrate/ 25 mM phosphate (CPi) for H+ flux experiments, adjusted with NaOH to the desired pH in the range 4.5–5.5. (Some experiments used 75 mM glutamate as buffer, with similar results.) After dialysis, liposomes were stored in aliquots at −80°C until the day of use.
Walden M., Accardi A., Wu F., Xu C., Williams C, & Miller C. (2007). Uncoupling and Turnover in a Cl−/H+ Exchange Transporter. The Journal of General Physiology, 129(4), 317-329.
Publication 2007
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Anions Buffers Chromatography Citrates Citric Acid Cytokinesis Detergents Dialysis Dialysis Solutions Escherichia coli Gel Chromatography Glutamates Lipid Bilayers Lipids Liposomes Micelles Phosphates Proteins SDS-PAGE Staphylococcal Protein A

Most recents protocols related to «3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate»

1
Quantitative ER-Mitochondria Interaction Assay
Mouse monoclonal anti ACTIN, Sigma-Aldrich, A5441; Mouse monoclonal anti c-myc, Sigma-Aldrich, M4439; Rabbit polyclonal anti Calnexin, Enzo, ADI-SPA-865-F; Mouse monoclonal anti CYTC, BD Bioscience, 556433; Rabbit DyLight 680, Thermo Fisher Scientific, 35569; Mouse DyLight 680 Thermo Fisher Scientific, 35519; Mouse DyLight 800 Thermo Fisher Scientific, 35521; Rabbit DyLight 800 Thermo Fisher Scientific, 35571; Mouse monoclonal anti eIF2α, Cell Signaling, 2103S; Rabbit polyclonal anti-E-Syt1, Sigma-Aldrich, HPA016858; Rabbit polyclonal anti-GFP, Cell Signaling, 2555S; Mouse monoclonal anti-GFP,Life technologies, A11122; HRP Mouse Bioké, Cell Signaling, 7076; HRP Rabbit Bioké, Cell Signaling, 7074; Mouse monoclonal anti IP3R3, BD Bioscience, 610312; Rabbit polyclonal anti-PERK, Cell signaling, 3192S; Rabbit polyclonal anti PERK, Cell signaling, 5683S; Rabbit monoclonal anti Phospho-eIF2α (Ser51), Cell signaling, 3597S; Rabbit polyclonal anti PDI Genetex, GTX30716; Mouse monoclonal anti PSD, Santa Cruz, sc-390070; Rabbit polyclonal anti, PSS1 (B-5), Santa Cruz, sc-515376; Rabbit polyclonal anti PSS2, Sigma-Aldrich, SAB1303408; Rabbit polyclonal VDAC1, Cell Signaling, 4866S; Rabbit polyclonal VDAC1, Abcam, ab15895; Veriblot antibody Abcam, ab131366.
The reagents used were: Antimycin A, Sigma-Aldrich, A8674; Calcium Chloride dihydrate, Sigma-Aldrich, C3881; CHAPS hydrate, Sigma-Aldrich, C3023; Conjugated GFP antibody beads, Laboratory of Chris Ulens; D-Galactose, Sigma-Aldrich, G0750; D-glucose, Sigma-Aldrich, G7021-1KG; DAPI, Thermo Fisher Scientific, 62248; Dulbecco’s Modified Eagle’s Medium - high glucose, Sigma-Aldrich, D0422; EGTA, AppliChem, A0878; FCCP, Sigma-Aldrich, C2920; Gibco DMEM/F-12, Thermo Fisher Scientific, 11320074; Glucose, Agilent Seahorse, 103577; Glutamine, Sigma-Aldrich, G7513; Glutamine, Agilent Seahorse, 103579; GSK PERK Inhibitor, Toronto Research Company, G797800; Hygromycin B, Invivogen, ant-hg-1; Lipofectamine 2000 Transfection Reagent, Thermo Fisher Scientific, 11668019; MitoTracker FarRed, Thermo Fisher Scientific, M22426; NBD-PS, Avanti Polar Lipids, 810194C; SE Cell Line 4D-Nucleofector X Kit L, V4XC-1024; Oligomycin, Sigma-Aldrich, 75351; Penicillin and streptomycin, Sigma-Aldrich, P0781; Percoll, Sigma-Aldrich, P1644; Pierce ECL Western Blotting Substrate, Thermo Fisher Scientific, 32106X4; Pierce Protein A/G Magnetic Beads, Thermo Fisher Scientific, 88802; Pierce Protease Inhibitor Tablets, EDTA-free, Thermo Fisher Scientific, 88266; Potassium Chloride, Janssen Chimica, 7447407; Protease inhibitor, Thermo Fisher Scientific, A32953; Puromycin, Thermo Fisher Scientific, A11138-03; Protein A/G PLUS-Agarose, Santa Cruz, sc-2003; XF DMEM pH7 7.4, Agilent Seahorse, 103575; Sodium Chloride, Sigma-Aldrich, A0431796; Sodium Pyruvate Solution, Agilent Seahorse, 103578; Sucrose, Acros, A0333146; Thapsigargin, Enzo Life Sciences, BML-PE180; TransIT-X2 Dynamic Delivery System, Mirus Bio, MIR 6000; Tris base, Sigma-Aldrich, 77861; Triton, Sigma-Aldrich, T9234; Tween, Sigma Aldrich, P4780.
Sassano M.L., van Vliet A.R., Vervoort E., Van Eygen S., Van den Haute C., Pavie B., Roels J., Swinnen J.V., Spinazzi M., Moens L., Casteels K., Meyts I., Pinton P., Marchi S., Rochin L., Giordano F., Felipe-Abrio B, & Agostinis P. (2023). PERK recruits E-Syt1 at ER–mitochondria contacts for mitochondrial lipid transport and respiration. The Journal of Cell Biology, 222(3), e202206008.
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Publication 2023
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Actins Antimycin A Calcium Chloride Dihydrate Calnexin Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone DAPI Eagle Edetic Acid Egtazic Acid G-substrate Galactose Glucose Glutamine Hygromycin B Immunoglobulins L Cells Lipids lipofectamine 2000 Mus N-(7-nitro-2,1,3-benzoxadiazol-4-yl)phosphatidylserine Obstetric Delivery Oligomycins Peeling Skin Syndrome Peeling skin syndrome, acral type Penicillins Percoll Potassium Chloride Protease Inhibitors Puromycin Pyruvate Rabbits Seahorses Sepharose Sodium Sodium Chloride Staphylococcal Protein A Streptomycin Sucrose SYT1 protein, human Thapsigargin Transfection Tromethamine Tweens VDAC1 protein, human
2
Co-immunoprecipitation of E-Syt1 and PERK
48 h after transfection with the selected plasmids, cells were collected and lysed at 4°C for 30 min in CHAPS buffer (1% CHAPS, 100 mM KCl, 50 mM Tris HCl, 150 mM NaCl, 1x protease inhibitor [Pierce Protease Inhibitor Tablets, Thermo Fisher Scientific Inc.]) in MQ water. Cells were centrifuged to remove debris and 500 μg of proteins from the supernatant was combined with primary antibody/conjugated GFP antibody beads overnight (ON) at 4°C. Proteins were eluted with sample buffer (62.5 μM Tris-HCl, 10% glycerol, 2% SDS, 1x protease inhibitor, 1x phosphatase inhibitor (Pierce phosphatase Inhibitor Tablets, Thermo Fisher Scientific Inc.) in MQ water and loaded on gel for Western blot analysis. For developing IPs, ChemiDoc MP Imaging system and Rabbit DyLight 680/Mouse DyLight 800 secondary antibodies were used in cells transiently co-transfected with eGFP-empty vector or eGFP-tagged E-Syt1 and myc-tagged PERK-FL or myc-tagged PERKk618A; for the rest of the experiments, HRP-based detection using as secondary antibody the Veriblot antibody was used in order to avoid the detection of the long and short chains of the IgG.
Sassano M.L., van Vliet A.R., Vervoort E., Van Eygen S., Van den Haute C., Pavie B., Roels J., Swinnen J.V., Spinazzi M., Moens L., Casteels K., Meyts I., Pinton P., Marchi S., Rochin L., Giordano F., Felipe-Abrio B, & Agostinis P. (2023). PERK recruits E-Syt1 at ER–mitochondria contacts for mitochondrial lipid transport and respiration. The Journal of Cell Biology, 222(3), e202206008.
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Publication 2023
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Antibodies Buffers Cells Cloning Vectors Glycerin Immunoglobulins Mus Phosphoric Monoester Hydrolases Plasmids Protease Inhibitors Proteins Rabbits Sodium Chloride SYT1 protein, human Transfection Tromethamine Western Blot
3
Telomerase Activity Measurement by TRAP Assay
The activity of telomerase was tested based on the classical TRAP method (Kim and Wu, 1997 (link)) with minor modification. Briefly, cultured cells were washed with PBS and the cell numbers were counted. A total of 1 × 106 cells were lysed with CHAPS lysis buffer for 30 min on ice. After centrifugation at 12,000 ×g for 20 min, the supernatant was removed into a new prechilled tubes and the concentration was determined by the Pierce BCA Protein Assay Kit (Thermo Scientific). Two steps were applied for TRAP assay. The first reaction system contained 1 μl cell lysate, 1 μl dNTP (2.5 mM), 1 μmol/l TS primer (5‘-AATCCGTCGAGCAGAGTT-3’), 1 μl 10 × TRAP buffer (200 mM Tris–HCL, 15 mM MgCL2, 630 mM KCL, 0.5% Tween 20, 10 mM EGTA, and 0.1% BSA, pH 8.3), and 6.5 μl ddH2O. The mixture were incubated at 30°C for 40 min, inactivated at 95°C 5 min, and stored at 4°C. The second step was PCR reaction, each 20 μl reaction system contained 2 μl of products from the first step, 2 μl 10 × TRAP buffer, 3 μl dNTP (2.5 mM), 0.5 μmol/l TS primer, 0.5 μmol/l ACX primer (5‘-GCGCGGCTTACCCTTACCCTTACCCTAACC-3’), 0.5 μmol/l NT primer (5‘-ATCGCTTCTCGGCCTTTT-3′), 0.5 amol/μl TSNT (5‘-AATCCGTCGAGCAGAGTTAAAAGGCCGAGAAGCGAT-3′), and 11 μl ddH2O. PCR was performed at 95°C for 3 min, 30 cycles of 94°C for 30 s, 59°C for 30 s, 72°C for 1 min, and 72°C for 5 min. PCR products were separated on a 15% native-PAGE gel in TBE buffer. After electrophoresis, the gel was stained with GelRed for 30 min and the images were captured under UV light with reverse processing.
Liu J., Zhao S., Li Z., Zhang Z., Zhao B., Guan G., Yin H, & Luo J. (2023). Activation of telomerase activity and telomere elongation of host cells by Theileria annulata infection. Frontiers in Microbiology, 14, 1128433.
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Publication 2023
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Acute Monocytic Leukemia Biological Assay Buffers Cells Centrifugation Cultured Cells Egtazic Acid Electrophoresis Magnesium Chloride Native Polyacrylamide Gel Electrophoresis Oligonucleotide Primers Proteins Telomerase Tris-borate-EDTA buffer Tromethamine Tween 20 Ultraviolet Rays
4
Cell Lysis and Protein Quantification
The target cell samples were washed with phosphate-buffered saline (PBS) two times, and the cell number was counted using Countstar cell analysis system (Alit Biotech, Shanghai, China). A total of 1 × 106 cells were re-suspended in 200 μl CHAPS lysis buffer (Merck-Millipore) and incubated on ice for 30 min. The cell lysate was then centrifuged at 12,000 ×g for 20 min at 4°C. The protein concentration was determined by using Pierce BCA protein assay kit (Thermo Fisher Scientific). The supernatant were then transferred into new sterile tubes and stored at −80°C.
Liu J., Zhao S., Li Z., Zhang Z., Zhao B., Guan G., Yin H, & Luo J. (2023). Activation of telomerase activity and telomere elongation of host cells by Theileria annulata infection. Frontiers in Microbiology, 14, 1128433.
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Publication 2023
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Biological Assay Buffers Cells Phosphates Proteins Saline Solution Sterility, Reproductive
5
Co-Immunoprecipitation of Signaling Proteins
Samples were harvested in CHAPS buffer and subjected to co-immunoprecipitation (co-IP) using Dynabeads magnetic protein A agarose beads (Life Technologies) according to the manufacturer’s protocol. Immunoprecipitation antibodies were crosslinked to the beads using the Pierce BS3 crosslinker (ThermoFisher, cat. 21580). 1 mg of protein lysate was used as input material for co-IP reactions. Antibodies were acquired from Cell Signaling Technology unless noted otherwise. Antibodies were used for MEK (#8727), ERK (#9102), pMEK (#9154), pERK (#4376), BCL-2 (#4223), BCL-XL (#2764), MCL-1 (#4572), BIM (#2933), α-tubulin (#3873) and β-actin (Abcam, Ab6276).
Eleveld T.F., Vernooij L., Schild L., Koopmans B., Alles L.K., Ebus M.E., Dandis R., van Tinteren H., Caron H.N., Koster J., van Noesel M.M., Tytgat G.A., Eising S., Versteeg R., Dolman M.E, & Molenaar J.J. (2023). MEK inhibition causes BIM stabilization and increased sensitivity to BCL-2 family member inhibitors in RAS-MAPK-mutated neuroblastoma. Frontiers in Oncology, 13, 1130034.
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Publication 2023
3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate Actins alpha-Tubulin Antibodies BCL2 protein, human Buffers Co-Immunoprecipitation Immunoprecipitation Proteins Sepharose Staphylococcal Protein A

Top products related to «3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate»

1
Chaps by Merck Group
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CHAPS is a zwitterionic detergent used in biochemical applications. It is commonly employed for protein solubilization and purification. CHAPS exhibits a critical micelle concentration of approximately 8-10 mM in aqueous solutions.
2
2 d quant kit by GE Healthcare
Sourced in United States, United Kingdom, Sweden, Germany, China, Japan, Italy, Australia, France
The 2-D Quant Kit is a laboratory equipment used for protein quantification. It provides a simple and accurate method for determining the concentration of proteins in complex biological samples.
3
Protease inhibitor cocktail by Merck Group
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The Protease Inhibitor Cocktail is a laboratory product designed to inhibit the activity of proteases, which are enzymes that can degrade proteins. It is a combination of various chemical compounds that work to prevent the breakdown of proteins in biological samples, allowing for more accurate analysis and preservation of protein integrity.
4
Protease inhibitor cocktail by Roche
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Protease inhibitor cocktail is a laboratory reagent used to inhibit the activity of proteases, which are enzymes that break down proteins. It is commonly used in protein extraction and purification procedures to prevent protein degradation.
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2 d clean up kit by GE Healthcare
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The 2-D Clean-Up Kit is a laboratory equipment product designed to prepare protein samples for two-dimensional (2D) gel electrophoresis. The kit provides reagents and materials to remove interfering substances, such as salts, lipids, and detergents, from protein samples prior to 2D gel analysis.
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Dithiothreitol (dtt) by Merck Group
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Dithiothreitol (DTT) is a reducing agent commonly used in biochemical and molecular biology applications. It is a small, water-soluble compound that helps maintain reducing conditions and prevent oxidation of sulfhydryl groups in proteins and other biomolecules.
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Bradford assay by Bio-Rad
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The Bradford assay is a colorimetric protein assay used to measure the concentration of protein in a solution. It is based on the color change of the Coomassie Brilliant Blue G-250 dye in response to various concentrations of protein.
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Thiourea by Merck Group
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Thiourea is a chemical compound with the formula (NH2)2CS. It is a white crystalline solid that is soluble in water and organic solvents. Thiourea has a variety of applications in research and industrial processes, but its core function is as a reagent or intermediate in chemical synthesis.
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Urea is a chemical compound with the formula CO(NH2)2. It is a colorless, odorless, and crystalline solid that is highly soluble in water. Urea's core function is to serve as a source of nitrogen and a key component in many biochemical processes.
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Protean ief cell by Bio-Rad
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The Protean IEF Cell is a laboratory equipment designed for isoelectric focusing (IEF), a technique used to separate and analyze proteins based on their isoelectric point. The device provides a controlled environment for the IEF process, allowing for the effective separation and characterization of proteins.

More about "3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate"

3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate, also known as CHAPS, is a widely used zwitterionic detergent in the field of biological and biochemical research.
This amphoteric compound is particularly effective in solubilizing both hydrophilic and hydrophobic molecules, making it a versatile tool for membrane protein extraction and purification.
CHAPS is often employed in conjunction with other reagents such as the 2-D Quant Kit for protein quantification, Protease inhibitor cocktail to prevent protein degradation, and the 2-D Clean-Up Kit to prepare samples for 2D gel electrophoresis.
Additionally, Dithiothreitol (DTT) is frequently used as a reducing agent to maintain protein structure, while the Bradford assay is a common method for determining protein concentration.
In some cases, Thiourea and Urea may be added to the sample buffer to improve protein solubilization and separation in 2D gel electrophoresis experiments.
The Protean IEF Cell is a specialized instrument used for the isoelectric focusing (IEF) step in 2D gel electrophoresis, a crucial technique for analyzing complex protein mixtures.
Rigorous comparison of experimental protocols is essential for ensuring reproducibility in CHAPS-based studies.
The PubCompare.ai platform can be a valuable tool in this regard, allowing researchers to easily locate and compare protocols from literature, pre-prints, and patents, and identify the optimal approach for their specific research needs.
By leveraging the insights and capabilities of PubCompare.ai, researchers can streamline their workflow, improve the consistency of their results, and enhance the reproducibility of their 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate-related studies.