Ionic detergent compatibility reagent

Manufactured by Thermo Fisher Scientific

Sourced in United States, Germany

The Ionic Detergent Compatibility Reagent is a laboratory product designed to assess the compatibility of ionic detergents with various biological samples or experimental conditions. It provides a simple and efficient way to evaluate the suitability of ionic detergents for a specific application.

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Lab products found in correlation

Pierce 660 nm protein assay reagent, by Thermo Fisher Scientific (7 mentions) Pierce 660 nm protein assay, by Thermo Fisher Scientific (5 mentions) Glucose uptake glo assay, by Promega (3 mentions) Odyssey clx, by LI COR (2 mentions) α rabbit ir800 α mouse ir680 secondary antibodies, by LI COR (2 mentions) Bovine serum albumin (bsa), by Merck Group (2 mentions) Cytation 5 plate reader, by Agilent Technologies (2 mentions) Glucose uptake glo assay, by Thermo Fisher Scientific (2 mentions) Dialyzed fbs, by Merck Group (2 mentions) Western blotting substrate, by Thermo Fisher Scientific (2 mentions) Pierce bicinchoninic acid protein assay kit, by Thermo Fisher Scientific (2 mentions) 13c6 l lysine, by Merck Group (2 mentions) L arginine, by Merck Group (2 mentions) L lysine, by Merck Group (2 mentions) Dulbecco s phosphate buffered saline pbs, by Merck Group (2 mentions) Dot blot apparatus, by Bio-Rad (2 mentions) Benzonase, by Merck Group (2 mentions) Beclin 1, by Cell Signaling Technology (1 mentions) 5 and 6 chloromethyl 2 7 dichlorodihydrofluorescein diacetate cm h2dcfda, by Thermo Fisher Scientific (1 mentions) Antibody against human β actin, by Santa Cruz Biotechnology (1 mentions)

23 protocols using ionic detergent compatibility reagent

Protein Sample Preparation for Proteomics

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Samples used for proteomic analysis were precipitated in 20% trichloroacetic acid in acetone, as previously described^{34 (link)}, and finally resuspended in a SDS buffer (2% SDS, 500 mM Tris pH 7.6 and 0.05 M Dithiothreitol).
Protein quantitation was done with Pierce 660 nm Protein Assay mixed with Ionic Detergent Compatibility Reagent following the manufacturer´s instructions (Thermo Fisher Scientific, Asheville, NC, USA).

Hermida-Nogueira L., Barrachina M.N., Morán L.A., Bravo S., Diz P., García Á, & Blanco J. (2020). Deciphering the secretome of leukocyte-platelet rich fibrin: towards a better understanding of its wound healing properties. Scientific Reports, 10, 14571.

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Hippocampal Synaptosomal Fractionation for Immunoblotting

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The crude synaptosomal fractions from hippocampus were isolated for immunoblotting. First, freshly dissected whole hippocampi were mechanically homogenized using a Potter–Elvehjem homogenizer in an ice-cold homogenization buffer (0.32 M sucrose, 10 mM HEPES, 2 mM EDTA, and protease inhibitors cocktail; 400 µL/hippocampus). The homogenate was then centrifuged at 900× g for 15 min at 4 °C. The supernatant was centrifuged at 16,000× g for 15 min at 4 °C. The pellet was then washed and resuspended in fresh ice-cold homogenization buffer (300 µL/hippocampus) and centrifuged again at 16,000× g for 15 min at 4 °C. The resulting pellet containing synaptosomes was resuspended in a HEPES lysis buffer (50 mM HEPES, 2 mM EDTA, protease inhibitors cocktail; 150 µL/hippocampus). Samples were briefly sonicated to ensure membrane lysis and used for immunoblots. For normalization, the exact protein concentration of each sample was determined using an ionic detergent compatibility reagent (22663, Thermo Fisher). The purity and composition of our hippocampal synaptosomal fractions have been previously verified and reported [13 (link),19 (link),20 (link)].

Cheung G., Chever O., Rollenhagen A., Quenech’du N., Ezan P., Lübke J.H, & Rouach N. (2023). Astroglial Connexin 43 Regulates Synaptic Vesicle Release at Hippocampal Synapses. Cells, 12(8), 1133.

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Immunoblotting Analysis of Sporulation Proteins

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Sporulation was induced as indicated, and samples were harvested and processed for immunoblotting as previously⁸⁶. Total protein in each sample was quantified using the Pierce 660nm protein assay with the ionic detergent compatibility reagent (Thermo Fisher) and 5 μg of protein was loaded for each sample. σ^F, σ^E, and Spo0A were resolved on 15% SDS-PAGE gels while SpoIIQ and SpoIVA were resolved on 12% SDS-PAGE gels. Protein was transferred to PVDF membranes, which were subsequently probed with rabbit (σ^F, σ^E, SpoIIQ) and mouse (Spo0A, SpoIVA) polyclonal primary antibodies and α-rabbit IR800/α-mouse IR680 secondary antibodies (LI-COR). Blots were imaged on the LiCor Odyssey CLx. Results shown are representative of analyses of two biological replicates.

Oliveira P.H., Ribis J.W., Garrett E.M., Trzilova D., Kim A., Sekulovic O., Mead E.A., Pak T., Zhu S., Deikus G., Touchon M., Lewis-Sandari M., Beckford C., Zeitouni N.E., Altman D.R., Webster E., Oussenko I., Bunyavanich S., Aggarwal A.K., Bashir A., Patel G., Wallach F., Hamula C., Huprikar S., Schadt E.E., Sebra R., van Bakel H., Kasarskis A., Tamayo R., Shen A, & Fang G. (2019). Epigenomic characterization of Clostridioides difficile finds a conserved DNA methyltransferase that mediates sporulation and pathogenesis. Nature microbiology, 5(1), 166-180.

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Quantitative Proteomic Analysis of Apoptosis

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DMXAA (purity ≥ 98%), ¹³C₆-L-lysine, L-lysine, ¹³C 15 (link)6 N4-L-arginine, L-arginine, RNase A, propidium iodide, Dulbecco’s phosphate-buffered saline (PBS), heat-inactivated fetal bovine serum (FBS), dialyzed FBS, and Roswell Park Memorial Institute (RPMI)-1640 medium for SILAC were purchased from Sigma-Aldrich Co. (St Louis, MO, USA). The 5-(and 6)-chloromethyl-2′,7′-dichlorodihydrofluorescein diacetate (CM-H₂DCFDA) was sourced from Invitrogen Inc. (Carlsbad, CA, USA). A FASP™ protein digestion kit was purchased from Protein Discovery Inc. (Knoxville, TN, USA). RPMI-1640 medium for general cultural use was obtained from Corning Cellgro Inc. (Herndon, VA, USA). The polyvinylidene difluoride membrane was purchased from EMD Millipore Inc. (Bedford, MA, USA). Proteomic quantitation kits for acidification, desalting, and digestion, ionic detergent compatibility reagent, a Pierce bicinchoninic acid protein assay kit, and Western blotting substrate were obtained from Thermo Fisher Scientific Inc. (Waltham, MA, USA). Primary antibodies against human cytochrome c, cleaved caspase 3, microtubule-associated protein 1A/1B-light chain 3-I (LC3-I), LC3-II, and beclin 1 were all purchased from Cell Signaling Technology Inc. (Beverly, MA, USA). The antibody against human β-actin was obtained from Santa Cruz Biotechnology Inc. (Dallas, TX, USA).

Pan S.T., Zhou Z.W., He Z.X., Zhang X., Yang T., Yang Y.X., Wang D., Qiu J.X, & Zhou S.F. (2015). Proteomic response to 5,6-dimethylxanthenone 4-acetic acid (DMXAA, vadimezan) in human non-small cell lung cancer A549 cells determined by the stable-isotope labeling by amino acids in cell culture (SILAC) approach. Drug Design, Development and Therapy, 9, 937-968.

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Total Cell Extract Proteome Analysis

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The total cell extract was collected using 2× sample buffer and sonicated, or syringe sampled 15 times using a 1 ml syringe fitted with a 24 G needle to ensure lysate homogenization and genomic DNA shearing. Afterward, the protein concentration was analyzed using Ionic Detergent Compatibility Reagent (Thermo Fisher Scientific) and Pierce 660 nm Protein Assay Reagent (Thermo Fisher Scientific) according to the manufacturer’s instructions. The total cell lysate was analyzed by western blotting using the indicated antibodies.

Ueda N., Maekawa M., Matsui T.S., Deguchi S., Takata T., Katahira J., Higashiyama S, & Hieda M. (2022). Inner Nuclear Membrane Protein, SUN1, is Required for Cytoskeletal Force Generation and Focal Adhesion Maturation. Frontiers in Cell and Developmental Biology, 10, 885859.

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Sperm Protein Extraction for Analysis

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Isolated sperm were washed once with PBS containing protease inhibitors and pelleted by centrifugation (800 g, 7 min, RT). Next, sperm were dissolved in H₂O supplemented with protease inhibitors to induce lysis of contaminating non-sperm cells (e.g., blood cells) by hypotonic shock. Sperm pellets were dissolved in RIPA buffer (Cell Signaling Technology, 10 µL per 1 × 10⁶ sperm) supplemented with protease inhibitor cocktail and 100 mM DTT. Following incubation on ice for 30 min, samples were sonified for 5 min in 30 s intervals using a Bioruptor sonication device (Diagenode, Seraing, Belgium). Samples were diluted in Roti^®-Load 1 and boiled at 95°C for 5 min. Cell debris was removed by centrifugation (20,800× g, 4 °C). Protein concentrations were quantified using the Pierce 660 nm Protein Assay Reagent supplemented with Ionic Detergent Compatibility Reagent according to the 96-well microplate procedure of the manufacturer’s protocol assay (Thermo Fisher Scientific).

Schneider S., Shakeri F., Trötschel C., Arévalo L., Kruse A., Buness A., Poetsch A., Steger K, & Schorle H. (2020). Protamine-2 Deficiency Initiates a Reactive Oxygen Species (ROS)-Mediated Destruction Cascade during Epididymal Sperm Maturation in Mice. Cells, 9(8), 1789.

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Protein Purification and Digestion Protocol

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The protein concentrations of the co‐IP samples were estimated using the Pierce 660 nm assay supplemented with the ionic detergent compatibility reagent (Thermo Fisher Scientific, USA). A protein amount of 20 μg was subjected to proteolytic digestion using the filter‐aided sample preparation (FASP) protocol with 30 kDa Vivacon filters (Sartorius, Germany) as previously described (Wisniewski et al, 2009). Peptides were purified with self‐packed C18 stop and go extraction (STAGE) tips as previously described (Rappsilber et al, 2003).

Pigoni M., Hsia H., Hartmann J., Rudan Njavro J., Shmueli M.D., Müller S.A., Güner G., Tüshaus J., Kuhn P., Kumar R., Gao P., Tran M.L., Ramazanov B., Blank B., Hipgrave Ederveen A.L., Von Blume J., Mulle C., Gunnersen J.M., Wuhrer M., Rammes G., Busche M.A., Koeglsperger T, & Lichtenthaler S.F. (2020). Seizure protein 6 controls glycosylation and trafficking of kainate receptor subunits GluK2 and GluK3. The EMBO Journal, 39(15), e103457.

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Protein Quantification by Pierce 660 nm Assay

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The Protein concentration was quantified by Pierce^TM 660 nm Protein Assay Reagent (Thermo Scientific, Germany) following the manufacturer’s instructions. Ionic Detergent Compatibility Reagent (Thermo Scientific, Germany) was added to the assay reagent to measure samples containing SDS. A standard calibration curve was prepared with bovine serum albumin (Sigma-Aldrich, Germany). Absorption was measured with an Infinite M1000 plate reader (Tecan, Switzerland) at 660 nm.

Han S., da Costa Marques R., Simon J., Kaltbeitzel A., Koynov K., Landfester K., Mailänder V, & Lieberwirth I. (2023). Endosomal sorting results in a selective separation of the protein corona from nanoparticles. Nature Communications, 14, 295.

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Glucose Uptake Assay in Rat Neurons

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Primary rat neurons were plated in standard plastic 96-well plates at a density of 40,000 cells/well, then transduced with codon-optimized lentiviruses as described in the previous section. Four days after transduction, the Glucose Uptake-Glo assay (Promega) was performed according to the manufacturer’s instructions. The reactions were then transferred to opaque white 96-well plates, and the luminescence was measured using standard luminometer settings on the Cytation 5 plate reader (BioTek). An aliquot of Glucose Uptake Glo assay lysates was analyzed for total protein content using the Pierce 660 nm protein assay according to the manufacturer’s instructions and with Ionic Detergent Compatibility Reagent (Thermo Scientific). Luminescence values were then normalized to total protein.

Nelson A.T., Cicardi M.E., Markandaiah S.S., Han J.Y., Philp N.J., Welebob E., Haeusler A.R., Pasinelli P., Manfredi G., Kawamata H, & Trotti D. (2024). Glucose hypometabolism prompts RAN translation and exacerbates C9orf72-related ALS/FTD phenotypes. EMBO Reports, 25(5), 2479-2510.

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Protein Quantification and Immunoblotting

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Cells were collected and directly lysed in Laemmli buffer. Proteins were quantified using Pierce solution supplemented with Ionic Detergent Compatibility Reagent (Thermo Scientific), following manufacturer’s instructions. Equal amounts of cells were loaded for immunoblotting, and sample loading was assessed by Ponceau staining after membrane transfer. Antibodies against SUMO2 (MBL, M114-3), SUMO1 (Abcam, ab32058), Ubc9 (Abcam, ab75854), Dppa2 (Millipore, MAB4356), Dppa4 (R&D Systems, AF3730), Hnrnpc (Abcam, ab133607), Histone H3 (Abcam, ab24834), Smchd1 (Abcam, ab31865), HA-probe (Santa Cruz, SC805), Sae1 (Abcam, ab185949), Uba2 (Abcam, ab185955), Pias1 (Cell Signaling, 3550), Pias2 (Novus Biologicals, NBP2-19819), Pias3 (Santa Cruz, SC46682), Pias4 (Cell Signaling, 4392), Znf451 (Sigma, SAB2108741), Ranbp2 (Santa Cruz, SC74518), Senp1 (Santa Cruz, SC271360), Senp2 (Santa Cruz, SC67075), Senp3 (Cell Signaling, 5591), Senp5 (Abcam, ab47631), Senp6 (Thermo Fisher Scientific, PA5-69704), and Senp7 (Thermo Fisher Scientific, PA5-36089), were used between 1/1000 and 1/500 concentration according to standard protocols and supplier’s recommendations.

Theurillat I., Hendriks I.A., Cossec J.C., Andrieux A., Nielsen M.L, & Dejean A. (2020). Extensive SUMO Modification of Repressive Chromatin Factors Distinguishes Pluripotent from Somatic Cells. Cell Reports, 32(11), 108146.

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