Igepal lysis buffer

Manufactured by Merck Group

Sourced in United States

IGEPAL lysis buffer is a non-ionic detergent solution used for cell lysis and protein extraction in various laboratory applications. It effectively disrupts cell membranes and solubilizes proteins, allowing for the extraction and purification of target molecules from biological samples.

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Lab products found in correlation

Gel documentation system, by Bio-Techne (2 mentions) β actin, by Merck Group (2 mentions) Mmp 1, by Merck Group (1 mentions) Mmp 12, by Santa Cruz Biotechnology (1 mentions) Nitrocellulose membrane, by Cytiva (1 mentions) Ecl method, by Thermo Fisher Scientific (1 mentions) Phospho p53 ser15, by Cell Signaling Technology (1 mentions) Protein assay, by Bio-Rad (1 mentions) X ray film, by Kodak (1 mentions) Igepal, by Merck Group (1 mentions) Dithiothreitol (dtt), by Merck Group (1 mentions) Ethylene diamine tetraacetic acid (edta), by Merck Group (1 mentions) Il 17a, by Santa Cruz Biotechnology (1 mentions)

4 protocols using igepal lysis buffer

Airway MMP Regulation in Asthma and CRS

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Nasal tissues from 21 participants with adequate specimens, including seven smokers with asthma and CRS, nine non-smokers with asthma and CRS, and five asthmatic non-smokers without CRS were processed for western blot analyses of MMPs. Total protein was prepared using a 1% IGEPAL lysis buffer (Sigma-Aldrich. St. Louis, MO, USA). Cellular proteins (10 μg) were fractionated by SDS-PAGE and electroblotted onto polyvinylidene difluoride membranes. Primary antibodies including MMP-1 (1:200; Millipore, Billerica, MA, USA), MMP-9 (1:1000; CST, MA, USA), MMP-12 (1:100; Santa Cruz Biotechnology, Dallas, TX, USA), and β-actin (1:20,000; Millipore, Billerica, MA, USA) were used to assess differences in protein levels by enhanced chemiluminescence. Protein bands were visualized using a gel documentation system (Alpha Innotech, San Leandro, CA. USA). Relevant band intensities were quantified via densitometric analyses and normalized to β-actin.

Huang C.C., Wang C.H., Wu P.W., He J.R., Huang C.C., Chang P.H., Fu C.H, & Lee T.J. (2019). Increased nasal matrix metalloproteinase-1 and -9 expression in smokers with chronic rhinosinusitis and asthma. Scientific Reports, 9, 15357.

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Protein Expression Analysis in Mouse Limbs

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Mice limbs were collected and lysed in IGEPAL lysis buffer (Sigma Aldrich), quantified using Bio-Rad protein assay (Bio-Rad Laboratories). Sixty μg protein samples were then resolved on 10% SDS PAGE gels, transferred to nitrocellulose membrane (Whatman), blocked with 5% milk in TBS-tween or 1% BSA- and 10% Sodium Azide in TBS-tween, and incubated in primary antibody diluted in blocking solution at 4°C overnight. The antibodies that used were: Actin (Clone C4 (MAB1501, Millipore) and phospho-p53 (Ser15) (9284, Cell Signaling Technology), with the corresponding HRP-conjugated secondary antibodies. Detection was performed using the ECL method (Thermo scientific) and developed using X-ray film (Kodak). Band intensities were quantified using Image-J while relative expression levels were normalized to the expression of Actin.

Mor E., He L., Torchinsky A, & Shomron N. (2014). MicroRNA-34a is dispensable for p53 function as teratogenesis inducer. Archives of toxicology, 88(9), 1749-1763.

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Cell Lysis and Protein Extraction

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Cells were lysed as described previously [16 (link)]. Pellets were suspended in Igepal lysis buffer (20 mM Tris-HCl pH 7.4, Sigma; 150 mM NaCl, Fisher Scientific; 1 mM EDTA, Sigma; 1 mM DTT, Sigma; 40 mM GlcNAc, Sigma; and 1% Igepal, Sigma) and lysed on ice for 20 min with occasional vortexing.

Flax J., Wilkins H.M., Miller R., Griffith S., Cork G.K., Qiang A., Thompson J., Swerdlow R.H, & Slawson C. (2020). OGA Inhibition Alters Energetics and Nutrient Sensing in Alzheimer’s Disease Cytoplasmic Hybrids. Journal of Alzheimer's disease : JAD, 78(4), 1743-1753.

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Quantifying Cellular Protein Levels

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Total protein was prepared using 1% IGEPAL lysis buffer (Sigma-Aldrich. St. Louis, MO, USA). Cellular proteins (10 μg) were fractionated by SDS-PAGE, electroblotted onto polyvinylidene difluoride membranes, and antibodies against IL-17A (1:500; Santa Cruz Biotechnology, Dallas, TX, USA) and β-actin (1:20,000; Millipore, Billerica, MA, USA) were used to assess differences in protein levels by enhanced chemiluminescence. Protein bands were visualized using a gel documentation system (Alpha Innotech, San Leandro, CA. USA). Relevant band intensities were quantified by densitometric analysis and normalized to β-actin.

Huang C.C., Wu P.W., Chen C.L., Wang C.H., Lee T.J., Tsai C.N, & Chiu C.H. (2018). IL-17A expression in the adenoid tissue from children with sleep disordered breathing and its association with pneumococcal carriage. Scientific Reports, 8, 16770.

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