Total protein was isolated from approximately 25 mg of frozen, crushed liver tissue using a radioimmunoprecipitation assay lysis buffer solution consisting of 25 mM HEPES, 2 mM EDTA (Invitrogen), 10 mM dithiothreitol, 50 mM sodium fluoride (Alfa Aesar), 50 mM β-glycerophosphate pentahydrate (Alfa Aesar), 3 mM benzamidine, 1 mM sodium orthovanadate, 0.5% (w/v) sodium deoxycholate, 1% (w/v) sodium dodecyl sulfate (Fisher), 5 nM microcystin, and 1x protease inhibitor cocktail (P8340, Millipore-Sigma. All reagents were purchased from Millipore-Sigma unless otherwise stated. Samples were homogenized in a 1:30 (w:v) ratio in 1.5 ml microcentrifuge tubes with a motorized pestle on ice. Lysates were centrifuged at 10,000g for 10 min at 4 °C. The supernatant was removed and mixed with an equal amount (v:v) of 2x sample buffer solution containing 20% (v/v glycerol), 60 mM Tris (pH 6.8), 2% (w/v) SDS, 5% (v/v) β-mercaptoethanol, and 0.01% (w/v) bromophenol blue. Samples were subsequently heated at 95 °C for 3 min and stored at −80 °C. Gel electrophoresis was performed by loading equal volumes of samples onto SDS-polyacrylamide gels. Proteins were transferred to PVDF membranes that were then blocked in 5% (w/v) non-fat milk for 1 h at room temperature. Membranes were washed and incubated with a primary antibody overnight at 4 °C on a tabletop rocker. The following day, membranes were washed and incubated in a secondary antibody for 1 h at room temperature in a 5% (w/v) non-fat milk solution. Membranes were then incubated for 1 min in enhanced chemiluminescence solution (RPN2235, Cytvia Amersham ECL Select Western Blotting Detection Agent, Cytvia) to image the targeted proteins (FluorChem M; ProteinSimple). Densitometry was performed with ImageJ software (Fiji). Values were normalized to total protein (Coomassie stain), except for phosphorylated proteins which were normalized to their respective total forms and expressed as fold change of Atg7-intact control mice. All antibodies were purchased from commercial vendors and details are listed in Table S1 .
Sodium dodecyl sulfate (sds)
Manufactured by Merck Group
Sourced in United States, Germany, United Kingdom, France, Italy, Canada, China, Poland, Spain, India, Japan, Sao Tome and Principe, Switzerland, Macao, Belgium, Australia, Austria, Ireland, Sweden, Hungary, Brazil, Czechia, Singapore, Malaysia, Portugal, Denmark, Netherlands, Finland, Argentina, Lithuania, Indonesia, Romania, New Zealand, Morocco
About the product
Sodium dodecyl sulfate (SDS) is a commonly used anionic detergent for various laboratory applications. It is a white, crystalline powder that has the ability to denature proteins by disrupting non-covalent bonds. SDS is widely used in biochemical and molecular biology techniques, such as protein electrophoresis, Western blotting, and cell lysis.
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Dimethyl sulfoxide (dmso), by Merck Group (306 mentions)
Dithiothreitol (dtt), by Merck Group (230 mentions)
Fetal bovine serum (fbs), by Thermo Fisher Scientific (222 mentions)
Ethylene diamine tetraacetic acid (edta), by Merck Group (211 mentions)
Glycine, by Merck Group (211 mentions)
Sodium hydroxide (naoh), by Merck Group (204 mentions)
Tween 20, by Merck Group (203 mentions)
Hydrochloric acid (hcl), by Merck Group (190 mentions)
Glycerol, by Merck Group (190 mentions)
Methanol, by Merck Group (181 mentions)
Sodium deoxycholate, by Merck Group (171 mentions)
Tris hcl, by Merck Group (153 mentions)
Bromophenol blue, by Merck Group (131 mentions)
Ethanol, by Merck Group (131 mentions)
β mercaptoethanol, by Merck Group (123 mentions)
Ammonium persulfate, by Merck Group (122 mentions)
Urea, by Merck Group (121 mentions)
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Market Availability & Pricing
Sodium dodecyl sulfate (SDS) is a widely used laboratory reagent available through authorized distributors like Merck Group and Sigma-Aldrich. Merck's EMPROVE® ESSENTIAL Ph Eur grade SDS is commercialized in 1 kg quantities, while Sigma-Aldrich provides SDS suitable for electrophoresis and molecular biology applications.
Pricing for SDS varies by distributor and product grade. Merck's 1 kg EMPROVE® ESSENTIAL Ph Eur grade SDS is priced at approximately $350 USD (excluding VAT). Sigma-Aldrich also offers SDS products, though specific pricing may require direct inquiry.
For alternative options, Thermo Scientific provides SDS suitable for electrophoresis applications.
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Get pricing insights and sourcing optionsSpelling variants (same manufacturer)
Sodium sulfate - 516 citations
SDS (sodium dodecyl sulfate) - 10 citations
Sulfate - 8 citations
Dodecyl sodium sulfate - 7 citations
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), - 6 citations
Dodecyl sulfate sodium salt (SDS) - 5 citations
Sodium dodecyl - 4 citations
Sodium dodecyl sulfate-polyacrylamide gel (SDS-PAGE, - 2 citations
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Sodium dodecyl sulfate (by Sinopharm) - 108 citations
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SDS (by neoFroxx) - 3 citations
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SDS (by Interchim) - 2 citations
Sodium dodecyl sulfate (SDS) (by Curtin Mathesin Scientific) - 2 citations
SDS (by Kelong Chemical) - 2 citations
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The spelling variants listed below correspond to different ways the product may be referred to in scientific literature.
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4 338 protocols using «sodium dodecyl sulfate (sds)»
1
Liver Tissue Protein Extraction and Western Blot
2
Synthesis and Characterization of Gemini Surfactants
Dodecyldimethylammonium chloride (99%), dodecyltrimethylammonium bromide (98%), sodium dodecyl sulfate (97%) and sodium dodecanoate (99%) were obtained from Merck (Poznan, Poland). Gemini surfactants were obtained and analyzed according to the procedure developed in our laboratory, [11 (link)] for 12-6-12 and [39 (link)] for 12-O-12.
3
Antibody and Chemical Reagents for Influenza A Virus Study
Antibodies used in this study were mouse monoclonal anti-IAV Matrix 2 (Abcam, ab5416, WB 1:1000, IF 1:100), rabbit monoclonal anti-LC3B (Novus Biologicals, NBP2-46892, WB 1:1000), rabbit polyclonal caspase-6 (Cell Signaling, 9762, WB 1:1000), mouse monoclonal anti-β-actin (Proteintech, 66009-1, WB 1:10,000), rabbit polyclonal anti-IAV NP (GeneTex, GTX125989, WB 1:10,000), rabbit polyclonal PARP-1 (Cell Signaling, 9542, WB 1:1000), and mouse monoclonal HA antibody (clone 6F6) (Cambridge Enterprises Department of Virology, (Amorim et al, 2013 (link); Wright et al, 2009 (link))).
Chemical reagents used in this study include Z-VAD-FMK (InvivoGen; tlrl-vad), Z-VEID-FMK (R&D systems; FMK006), Z-DEVD-FMK (R&D systems FMK004), and Z-IETD (Invivogen; inh-ietd) at indicated concentrations. Ammonium bicarbonate, phosphoric acid, triethylAmmonium bicarbonate (TEAB), and sodium dodecyl sulfate (SDS) were purchased from Sigma-Aldrich (St. Louis, MO). Formic acid (FA) 99%, iodoacetamide (IAA), tris(2-carboxyethyl)phosphine hydrochloride (TCEP), trypsin protease MS-grade were purchased from Thermo Scientific Inc. (Rockford, IL, USA). LCMS-grade solvents: water, acetonitrile (ACN), methanol, were purchased from Fisher Chemical. S-Trap micro columns were purchased from ProtiFi (Huntington, NY). Evotips were purchased from Evosep (Odense, Denmark).
Chemical reagents used in this study include Z-VAD-FMK (InvivoGen; tlrl-vad), Z-VEID-FMK (R&D systems; FMK006), Z-DEVD-FMK (R&D systems FMK004), and Z-IETD (Invivogen; inh-ietd) at indicated concentrations. Ammonium bicarbonate, phosphoric acid, triethylAmmonium bicarbonate (TEAB), and sodium dodecyl sulfate (SDS) were purchased from Sigma-Aldrich (St. Louis, MO). Formic acid (FA) 99%, iodoacetamide (IAA), tris(2-carboxyethyl)phosphine hydrochloride (TCEP), trypsin protease MS-grade were purchased from Thermo Scientific Inc. (Rockford, IL, USA). LCMS-grade solvents: water, acetonitrile (ACN), methanol, were purchased from Fisher Chemical. S-Trap micro columns were purchased from ProtiFi (Huntington, NY). Evotips were purchased from Evosep (Odense, Denmark).
4
MTT Assay for Cell Viability
Cells were exposed to sols of different concentrations (0.1–5.0 mM). 2 h before the end of the exposure period, the culture medium was removed from the plates with confluent cell monolayer, and MTT solution (3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H tetrazolium bromide, Sigma-Aldrich) in PBS (0.1 mg ml−1, 100 μl per well) was added to the cells. At the end of the exposure period, the supernatant liquid was removed, and a lysis solution containing 0.1% SDS (Sigma-Aldrich) solution in DMSO (Sigma-Aldrich) was added. The plates were shaken for 5 min and placed on a Thermo/LabSystems Multiskan MS Microplate Reader, and the absorbance was read colorimetrically at 492 nm. Each experiment was repeated three times with four replicates.
The index of metabolic activity (IMA) was calculated using the formula CMTT/CCV, where CMTT (%) is the calculated percentage of metabolically active cells relative to control cells taken as 100%; CCV (%) is the calculated percentage of adherent viable cells relative to control cells taken as 100%. Since the values of the control cells are taken as 100% in both the MTT and SV assays, their metabolic activity index is 1.
The index of metabolic activity (IMA) was calculated using the formula CMTT/CCV, where CMTT (%) is the calculated percentage of metabolically active cells relative to control cells taken as 100%; CCV (%) is the calculated percentage of adherent viable cells relative to control cells taken as 100%. Since the values of the control cells are taken as 100% in both the MTT and SV assays, their metabolic activity index is 1.
5
Adsorption of Proteins on Biomaterial Surfaces
To examine
protein adsorption on biomaterial surfaces, both 2D and 3D samples
were immersed in DMEM supplemented with 10% fetal bovine serum (HyClone,
GE Healthcare, Utah, U.S.A.) and incubated at 37 °C for 24 h.
Tissue culture plates were used as controls. After incubation, the
samples were washed with DPBS and then incubated in 2% sodium dodecyl
sulfate (Sigma-Aldrich) for 20 h. Total protein content was quantified
using a commercially available protein assay kit (Pierce BCA Protein
Assay, Rockford, IL, U.S.A.) according to the manufacturer’s
instructions. Label-free mass spectrometry was then used to determine
the relative abundance of proteins adsorbed on the nanocellulose surfaces,
as previously described.37 (link) Protein solutions
were lyophilized and mixed with urea solution for unfolding. After
trypsin digestion, the samples were purified, lyophilized and subjected
to mass spectrometric analysis using a Dionex Ultimate NCS-3500RS
liquid chromatography system (Sunnyvale, CA, USA). After protein identification,
filtering, and mapping, the raw data were processed using Perseus
(version 2.0.9.0). We performed a log2 transformation without additional
normalization, as the relative label-free quantification (LFQ) intensity
column already includes normalized abundance values. The processed
data underwent differential expression analysis (DE) using ANOVA.
A list of differentially expressed proteins was generated and subjected
to Post hoc Tukey’s Honestly Significant Difference (HSD) test,
with a False Discovery Rate threshold of 0.05. These proteins were
then grouped into clusters based on the Euclidean distance metric
and Average Linkage method. The data table was exported to a .txt
file for further analysis in Python, enabling additional analyses
beyond those available in Perseus. Python was used to identify the
unique and overlapping adsorbed proteins in all groups.
For
each protein, it was considered adsorbed in each treatment if at least
one biological replicate had a value greater than 0. This data was
then used to generate Venn diagrams and heatmaps.
protein adsorption on biomaterial surfaces, both 2D and 3D samples
were immersed in DMEM supplemented with 10% fetal bovine serum (HyClone,
GE Healthcare, Utah, U.S.A.) and incubated at 37 °C for 24 h.
Tissue culture plates were used as controls. After incubation, the
samples were washed with DPBS and then incubated in 2% sodium dodecyl
sulfate (Sigma-Aldrich) for 20 h. Total protein content was quantified
using a commercially available protein assay kit (Pierce BCA Protein
Assay, Rockford, IL, U.S.A.) according to the manufacturer’s
instructions. Label-free mass spectrometry was then used to determine
the relative abundance of proteins adsorbed on the nanocellulose surfaces,
as previously described.37 (link) Protein solutions
were lyophilized and mixed with urea solution for unfolding. After
trypsin digestion, the samples were purified, lyophilized and subjected
to mass spectrometric analysis using a Dionex Ultimate NCS-3500RS
liquid chromatography system (Sunnyvale, CA, USA). After protein identification,
filtering, and mapping, the raw data were processed using Perseus
(version 2.0.9.0). We performed a log2 transformation without additional
normalization, as the relative label-free quantification (LFQ) intensity
column already includes normalized abundance values. The processed
data underwent differential expression analysis (DE) using ANOVA.
A list of differentially expressed proteins was generated and subjected
to Post hoc Tukey’s Honestly Significant Difference (HSD) test,
with a False Discovery Rate threshold of 0.05. These proteins were
then grouped into clusters based on the Euclidean distance metric
and Average Linkage method. The data table was exported to a .txt
file for further analysis in Python, enabling additional analyses
beyond those available in Perseus. Python was used to identify the
unique and overlapping adsorbed proteins in all groups.
For
each protein, it was considered adsorbed in each treatment if at least
one biological replicate had a value greater than 0. This data was
then used to generate Venn diagrams and heatmaps.
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