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Hippr detergent removal column

Manufactured by Thermo Fisher Scientific
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The HiPPR detergent removal columns are designed to effectively remove detergents from protein samples. The columns utilize proprietary resin technology to enable efficient separation of proteins from detergents, allowing for the purification and recovery of high-quality protein samples.

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Lab products found in correlation

30 kda molecular weight cutoff spin filter, by Merck Group (2 mentions) Dithiothreitol (dtt), by Thermo Fisher Scientific (1 mentions) Iodacetamide, by Merck Group (1 mentions) Glycine, by Avantor (1 mentions) Methanol, by Avantor (1 mentions) Ammonium bicarbonate abc, by Merck Group (1 mentions) Branched polyethylenimine, by Merck Group (1 mentions) Poly acrylic acid solution, by Merck Group (1 mentions) Ultrapure tris, by Avantor (1 mentions) Pierce c18 spin column, by Thermo Fisher Scientific (1 mentions) Trypsin, by Merck Group (1 mentions) Acetonitrile, by Merck Group (1 mentions) Hydrochloric acid (hcl), by Merck Group (1 mentions) Poly sodium 4 styrenesulfonate, by Merck Group (1 mentions) Loprodyne lp, by Pall Corporation (1 mentions) Sequencing grade modified trypsin, by Promega (1 mentions)

5 protocols using hippr detergent removal column

1

Native GELFrEE Purification and Exchange

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Fractions from native GELFrEE were first treated to remove detergent with 1–2 applications of a HiPPR detergent removal column (Thermo Fisher). Native GELFrEE and ion exchange fractions were exchanged into 100–200 mM ammonium acetate and concentrated using a 30 kDa molecular weight cutoff spin filter (Millipore).
Skinner O.S., Haverland N.A., Fornelli L., Melani R.D., Do Vale L.H., Seckler H.S., Doubleday P.F., Schachner L.F., Srzentić K., Kelleher N.L, & Compton P.D. (2017). Top-down characterization of endogenous protein complexes with native proteomics. Nature chemical biology, 14(1), 36-41.
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2

Native GELFrEE Purification and Exchange

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Fractions from native GELFrEE were first treated to remove detergent with 1–2 applications of a HiPPR detergent removal column (Thermo Fisher). Native GELFrEE and ion exchange fractions were exchanged into 100–200 mM ammonium acetate and concentrated using a 30 kDa molecular weight cutoff spin filter (Millipore).
Skinner O.S., Haverland N.A., Fornelli L., Melani R.D., Do Vale L.H., Seckler H.S., Doubleday P.F., Schachner L.F., Srzentić K., Kelleher N.L, & Compton P.D. (2017). Top-down characterization of endogenous protein complexes with native proteomics. Nature chemical biology, 14(1), 36-41.
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3

Membrane Protein Purification and Analysis

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Nylon membranes (LoProdyne LP, pore size 1.2 μm, 110 μm thickness) were acquired from Pall Corporation (Port Washington, New York). Poly(sodium 4-styrenesulfonate) (Mw ~ 70,000) (PSS), sodium chloride, trypsin (from porcine pancreas type IX-S, lypholized powder), hydrochloric acid, poly(acrylic acid) solution (Mw ~ 100,000), branched polyethylenimine (Mw ~ 25,000) , iodacetamide, acetonitrile, ammonium bicarbonate (ABC), and sodium dodecyl sulphate (BioReagent, suitable for electrophoresis) were purchased from Sigma Aldrich (St. Louis, Missouri). Sequencing grade modified trypsin was obtained from Promega (Madison, Wisconsin), and Mini-Protean 4-20% TGX precast gels were purchased from Bio Rad (Hercules, California). HiPPR Detergent Removal columns (0.1 mL), dithiothreitol (DTT, molecular biology grade), unstained protein molecular weight marker, extra thick western blotting filter paper, and Pierce C-18 Spin Columns, were acquired from Thermo Scientific (Waltham, Massachusetts). Methanol, glycine, and ultra-pure Tris were purchased from VWR (Radnor, Pennsylvania), and low fluorescence PVDF (0.45 μm) was obtained from Azure Biosystems (Dublin, California). Zwittergent 3-16 detergent was purchased from EMD Millipore (Burlington, Massachusetts).
Bickner A.N., Champion M.M., Hummon A.B, & Bruening M.L. (2020). Electroblotting through a tryptic membrane for LC-MS/MS analysis of proteins separated in electrophoretic gels. The Analyst, 145(23), 7724-7735.
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4

RAP-MS Protein Purification and Digestion

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Proteins from RAP-MS captures were resuspended in fresh 8 M urea dissolved in 40 µL of 100 mM Tris-HCl pH 8.5. Disulfide bonds were reduced by incubation with 3 mM TCEP for 20 minutes at room temperature, followed by alkylation with 11 mM iodoacetamide for 15 minutes at room temperature in the dark. Samples were then digested with 0.1 µg endoproteinase Lys-C for 4 hours at room temperature. After Lys-C digestion the samples were diluted to a final concentration of 2M urea by the addition of 100 mM Tris-HCl pH 8.5, and CaCl2 was added to a final concentration of 1 mM. Tryptic peptides were generated by treatment with 0.1 to 0.5 µg of trypsin overnight at room temperature. Contaminating detergents were removed from peptides using HiPPR detergent removal columns (Thermo), and peptides were protonated by the addition of 5% formic acid before desalting on a Microm Bioresources C8 peptide MicroTrap column. Peptide fractions were collected and lyophilized, and dried peptides were resuspended in 0.2% formic acid with 5% acetonitrile.
McHugh C.A., Chen C.K., Chow A., Surka C.F., Tran C., McDonel P., Pandya-Jones A., Blanco M., Burghard C., Moradian A., Sweredoski M.J., Shishkin A.A., Su J., Lander E.S., Hess S., Plath K, & Guttman M. (2015). The Xist lncRNA directly interacts with SHARP to silence transcription through HDAC3. Nature, 521(7551), 232-236.
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5

RAP-MS Protein Purification and Digestion

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Proteins from RAP-MS captures were resuspended in fresh 8 M urea dissolved in 40 µL of 100 mM Tris-HCl pH 8.5. Disulfide bonds were reduced by incubation with 3 mM TCEP for 20 minutes at room temperature, followed by alkylation with 11 mM iodoacetamide for 15 minutes at room temperature in the dark. Samples were then digested with 0.1 µg endoproteinase Lys-C for 4 hours at room temperature. After Lys-C digestion the samples were diluted to a final concentration of 2M urea by the addition of 100 mM Tris-HCl pH 8.5, and CaCl2 was added to a final concentration of 1 mM. Tryptic peptides were generated by treatment with 0.1 to 0.5 µg of trypsin overnight at room temperature. Contaminating detergents were removed from peptides using HiPPR detergent removal columns (Thermo), and peptides were protonated by the addition of 5% formic acid before desalting on a Microm Bioresources C8 peptide MicroTrap column. Peptide fractions were collected and lyophilized, and dried peptides were resuspended in 0.2% formic acid with 5% acetonitrile.
McHugh C.A., Chen C.K., Chow A., Surka C.F., Tran C., McDonel P., Pandya-Jones A., Blanco M., Burghard C., Moradian A., Sweredoski M.J., Shishkin A.A., Su J., Lander E.S., Hess S., Plath K, & Guttman M. (2015). The Xist lncRNA directly interacts with SHARP to silence transcription through HDAC3. Nature, 521(7551), 232-236.
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