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ief cathode buffer  (Bio-Rad)


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    Structured Review

    Bio-Rad ief cathode buffer
    Isoelectic focusing <t>(IEF)</t> of the bee venom fractions 1–7 in Ready Gel Precast Gels <t>with</t> <t>ampholytes</t> of pH gradient from 3.0 to 10.5. A multi-sample horizontal IEF gel was employed with 11 lanes containing the seven bee venom fractions and four unrelated samples. For presentation in , the lanes of the seven bee venom fractions were excised from the original IEF gel photograph and are arranged adjacently to facilitate comparative analysis. Lane 1 includes tube 3–6, lane 2 includes tubes 7–9, lane 3 includes tubes 10–11, lane 4 includes tubes 12–13, lane 5 includes tubes 14–16, lane 6 includes tubes 27–30, and lane 7 includes tubes 31–36, as shown in . The standard p I markers (FMC Corporation, Rockland, ME, USA) sample of a p I range from 4.65 to 10.6 is applied on the unmarked lane on the far left.
    Ief Cathode Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ief+buffer/10x+IEF+Cathode+Buffer/pmc12472953-150-92-95
    Average 93 stars, based on 7 article reviews
    ief cathode buffer - by Bioz Stars, 2026-10
    93/100 stars

    Images

    1) Product Images from "Bee Venom Proteins Enhance Proton Absorption by Membranes Composed of Phospholipids of the Myelin Sheath and Endoplasmic Reticulum: Pharmacological Relevance"

    Article Title: Bee Venom Proteins Enhance Proton Absorption by Membranes Composed of Phospholipids of the Myelin Sheath and Endoplasmic Reticulum: Pharmacological Relevance

    Journal: Pharmaceuticals

    doi: 10.3390/ph18091334

    Isoelectic focusing (IEF) of the bee venom fractions 1–7 in Ready Gel Precast Gels with ampholytes of pH gradient from 3.0 to 10.5. A multi-sample horizontal IEF gel was employed with 11 lanes containing the seven bee venom fractions and four unrelated samples. For presentation in , the lanes of the seven bee venom fractions were excised from the original IEF gel photograph and are arranged adjacently to facilitate comparative analysis. Lane 1 includes tube 3–6, lane 2 includes tubes 7–9, lane 3 includes tubes 10–11, lane 4 includes tubes 12–13, lane 5 includes tubes 14–16, lane 6 includes tubes 27–30, and lane 7 includes tubes 31–36, as shown in . The standard p I markers (FMC Corporation, Rockland, ME, USA) sample of a p I range from 4.65 to 10.6 is applied on the unmarked lane on the far left.
    Figure Legend Snippet: Isoelectic focusing (IEF) of the bee venom fractions 1–7 in Ready Gel Precast Gels with ampholytes of pH gradient from 3.0 to 10.5. A multi-sample horizontal IEF gel was employed with 11 lanes containing the seven bee venom fractions and four unrelated samples. For presentation in , the lanes of the seven bee venom fractions were excised from the original IEF gel photograph and are arranged adjacently to facilitate comparative analysis. Lane 1 includes tube 3–6, lane 2 includes tubes 7–9, lane 3 includes tubes 10–11, lane 4 includes tubes 12–13, lane 5 includes tubes 14–16, lane 6 includes tubes 27–30, and lane 7 includes tubes 31–36, as shown in . The standard p I markers (FMC Corporation, Rockland, ME, USA) sample of a p I range from 4.65 to 10.6 is applied on the unmarked lane on the far left.

    Techniques Used:

    Related Articles

    Electrofocusing:

    Article Title: Biochar Administration to San Marzano Tomato Plants Cultivated Under Low-Input Farming Increases Growth, Fruit Yield, and Affects Gene Expression
    Article Snippet: .. Protein pellets were washed once with ice-cold methanol and three times with ice-cold acetone, dried and solved in IEF buffer (9 M urea, 4% w/v CHAPS, 0.5% v/v Triton X-100, 20 mM DTT, and 1% w/v carrier ampholytes pH 3–10) (BioRad, Hercules, CA, USA). .. Protein concentration was quantified using the BioRad protein assay, using BSA as a standard.

    Article Title: Unraveling the Protein Network of Tomato Fruit in Response to Necrotrophic Phytopathogenic Rhizopus nigricans
    Article Snippet: .. IPG strips (13 cm pH 4–7, Bio-Rad ReadyStrip, Bio-Rad) were rehydrated overnight with 200 μL of IEF buffer containing 500 μg of total proteins. .. Isoelectric focusing (IEF) was performed on an Ettan IPGphor unit (GE Healthcare Bio-Sciences AB, Uppsala, Sweden) at 20°C, applying the following program: a linear increase from 0–500 V over 1 h, 500 V to 1000 V over 1 h, 1000 V to 8000 V over 2∶30 h and then held at 8000 V for 0∶55 h. After focusing, the proteins were reduced and alkylated followed by equiliberation in a buffer containing 6 M urea, 30% w/v glycerol, 2% SDS, and 50 mM Tris-HCl, pH 8.8.

    Article Title: An efficient protein extraction method applied to mangrove plant Kandelia obovata leaves for proteomic analysis
    Article Snippet: .. IPG strips (17 cm pH 4-7, Bio-Rad ReadyStrip; Bio-Rad) were passively rehydrated at 17 °C for 14 h with 330 μL IEF buffer (7 M urea, 2 M thiourea, 4 % (v/v) 3-[(3-Cholanidopropyl) dimethylammonio]-1-propanesulfonate (CHAPS), 2 % (v/v) pharmalyte 4-7, 50 mM DTT, 2 mM TBP, 0.1 mM PMSF, and 0.002% bromophenol blue) containing 2.0 mg of protein. .. Isoelectric focusing was performed with a Protean i12 IEF Cell (Bio-Rad) apparatus under the following program: 250 V for 30 min, 500 V for 30 min, 1000 V for 30 min, 8000 V for 5 h and 8000 V for a total of 40,000 Vh.

    Article Title: Biochar Administration to San Marzano Tomato Plants Cultivated Under Low-Input Farming Increases Growth, Fruit Yield, and Affects Gene Expression
    Article Snippet: Protein concentration was quantified using the BioRad protein assay, using BSA as a standard. .. IPG strips (17 cm, pH 4–7, BioRad ReadyStrip, BioRad) were rehydrated with 300 μl of IEF buffer containing 400 μg of total proteins, overnight. .. Proteins were focused using a Protean IEF Cell (BioRad, Segrate MI, Italy) at 12°C, applying 250 V (90 min), 500 V (90 min), 1,000 V (180 min), and 8,000 V, for a total of 53 KVh.

    Article Title: A metabolomics and proteomics study of the Lactobacillus plantarum in the grass carp fermentation.
    Article Snippet: Eventually, proteins were purified using the 2-D Clean-Up kit (GE healthcare, USA), and the protein concentration was measured by using the Bradford assay [51]. .. 2-DE analysis After determining the protein concentration from the control and experimental groups, the proteins were diluted with IEF buffer (8M Urea, 4% (w/v) CHAPS, 2M thiourea, 65 mM DTT, 0.2% (v/v) Bio-lyte (3/10, Bio-Rad, USA)). .. After centrifugation at 12,000 rpm and 4 °C for 10 min, isoelectric focusing (IEF) was performed on PROTEAN IEF cell (Bio-Rad, USA) by rehydrating Ready Strip IPG Strips (pH 4–7, 7 cm) with 150 μL protein solution (300 μg) for 14 h with a maximum current setting of 50 mA/strip at 20 °C.

    Article Title: Comparative proteomic analysis of durum wheat shoots from modern and ancient cultivars.
    Article Snippet: Accepted Manuscript Comparative proteomic analysis of durum wheat shoots from modern and ancient cultivars Mariapina Rocco, Maria Tartaglia, Francesco Paolo Izzo, Ettore Varricchio, Simona Arena, Andrea Scaloni, Mauro Marra PII: S0981-9428(18)30557-6 DOI: https://doi.org/10.1016/j.plaphy.2018.12.010 Reference: PLAPHY 5530 To appear in: Plant Physiology and Biochemistry Received Date: 6 July 2018 Revised Date: 10 December 2018 Accepted Date: 16 December 2018 Please cite this article as: M. Rocco, M. Tartaglia, F.P.. Izzo, E. Varricchio, S. Arena, A. Scaloni, M. Marra, Comparative proteomic analysis of durum wheat shoots from modern and ancient cultivars, Plant Physiology et Biochemistry (2019), doi: https://doi.org/10.1016/j.plaphy.2018.12.010.. This is a PDF file of an unedited manuscript that has been accepted for publication.

    other:

    Article Title: Activity-based protein profiling of the hepatitis C virus replication in Huh-7 hepatoma cells using a non-directed active site probe
    Article Snippet: Precipitated protein pellets (200 μg) were resuspended in 125 μl of isoelectric focusing (IEF) buffer (7 M Urea, 2 M thiourea, 4% CHAPS, 1% DTT) containing 0.2% Ampholytes pH 3-10 (biolytes, Bio-Rad, Hercules, CA).

    Article Title: Proteome Analysis of Nicotiana tabacum Cells following Isonitrosoacetophenone Treatment Reveals Defence-Related Responses Associated with Priming
    Article Snippet: In short, 140 μL samples were prepared using 100 μg of protein in 2 μL of 50% dithiothreitol (DTT) ( w / v ), 1.25 μL of ampholyte solution pH 3–10 (BioRad, Hercules, CA, USA) and the necessary amount of isoelectric focusing (IEF) buffer (containing 0.1% bromophenol blue) to make up the volume.

    Protein Concentration:

    Article Title: A metabolomics and proteomics study of the Lactobacillus plantarum in the grass carp fermentation.
    Article Snippet: Eventually, proteins were purified using the 2-D Clean-Up kit (GE healthcare, USA), and the protein concentration was measured by using the Bradford assay [51]. .. 2-DE analysis After determining the protein concentration from the control and experimental groups, the proteins were diluted with IEF buffer (8M Urea, 4% (w/v) CHAPS, 2M thiourea, 65 mM DTT, 0.2% (v/v) Bio-lyte (3/10, Bio-Rad, USA)). .. After centrifugation at 12,000 rpm and 4 °C for 10 min, isoelectric focusing (IEF) was performed on PROTEAN IEF cell (Bio-Rad, USA) by rehydrating Ready Strip IPG Strips (pH 4–7, 7 cm) with 150 μL protein solution (300 μg) for 14 h with a maximum current setting of 50 mA/strip at 20 °C.

    Control:

    Article Title: A metabolomics and proteomics study of the Lactobacillus plantarum in the grass carp fermentation.
    Article Snippet: Eventually, proteins were purified using the 2-D Clean-Up kit (GE healthcare, USA), and the protein concentration was measured by using the Bradford assay [51]. .. 2-DE analysis After determining the protein concentration from the control and experimental groups, the proteins were diluted with IEF buffer (8M Urea, 4% (w/v) CHAPS, 2M thiourea, 65 mM DTT, 0.2% (v/v) Bio-lyte (3/10, Bio-Rad, USA)). .. After centrifugation at 12,000 rpm and 4 °C for 10 min, isoelectric focusing (IEF) was performed on PROTEAN IEF cell (Bio-Rad, USA) by rehydrating Ready Strip IPG Strips (pH 4–7, 7 cm) with 150 μL protein solution (300 μg) for 14 h with a maximum current setting of 50 mA/strip at 20 °C.



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    Image Search Results


    Isoelectic focusing (IEF) of the bee venom fractions 1–7 in Ready Gel Precast Gels with ampholytes of pH gradient from 3.0 to 10.5. A multi-sample horizontal IEF gel was employed with 11 lanes containing the seven bee venom fractions and four unrelated samples. For presentation in , the lanes of the seven bee venom fractions were excised from the original IEF gel photograph and are arranged adjacently to facilitate comparative analysis. Lane 1 includes tube 3–6, lane 2 includes tubes 7–9, lane 3 includes tubes 10–11, lane 4 includes tubes 12–13, lane 5 includes tubes 14–16, lane 6 includes tubes 27–30, and lane 7 includes tubes 31–36, as shown in . The standard p I markers (FMC Corporation, Rockland, ME, USA) sample of a p I range from 4.65 to 10.6 is applied on the unmarked lane on the far left.

    Journal: Pharmaceuticals

    Article Title: Bee Venom Proteins Enhance Proton Absorption by Membranes Composed of Phospholipids of the Myelin Sheath and Endoplasmic Reticulum: Pharmacological Relevance

    doi: 10.3390/ph18091334

    Figure Lengend Snippet: Isoelectic focusing (IEF) of the bee venom fractions 1–7 in Ready Gel Precast Gels with ampholytes of pH gradient from 3.0 to 10.5. A multi-sample horizontal IEF gel was employed with 11 lanes containing the seven bee venom fractions and four unrelated samples. For presentation in , the lanes of the seven bee venom fractions were excised from the original IEF gel photograph and are arranged adjacently to facilitate comparative analysis. Lane 1 includes tube 3–6, lane 2 includes tubes 7–9, lane 3 includes tubes 10–11, lane 4 includes tubes 12–13, lane 5 includes tubes 14–16, lane 6 includes tubes 27–30, and lane 7 includes tubes 31–36, as shown in . The standard p I markers (FMC Corporation, Rockland, ME, USA) sample of a p I range from 4.65 to 10.6 is applied on the unmarked lane on the far left.

    Article Snippet: The following materials and chemicals were used in this study: Phospholipids—phosphatidylserine, sphingomyelin, phosphatidylinositol, phosphatidylcholine, and phosphatidylethanolamine—were purified from the rat liver (see the Preparations section below), Dichloro-diphenyl-trichloroethane (DDT), Sephadex G-25 and CM Sephadex C-50 (Nanjing Duly Biotech Co., Ltd., Nanjing, China), Tris(hydroxymethyl)aminomethane (Tris) 10 M pH 8.5 buffer, 1.0 M Tris-HCl pH 6.8 with 0.4% SDS buffer, Bromo-phenol Blue (Thomas Scientific, Swedesboro, NJ, USA); Mini-PROTEAN TGX precast gels (8% density), Isoelectric Focusing Gel Sample Buffer (IEF Gel), Ready Gel Precast Gels with ampholytes making pH gradient 3–10.5, 10× IEF Anode Buffer, 10× IEF Cathode Buffer (Bio-Rad Laboratories Co., Ltd., Shanghai, China), IEF p I 4.65–10.6 range protein markers for IEF (Shanghai Yeyuan Biotechnology Co., Ltd., Shanghai, China), Sodium Dodecyl Sulfate (SDS), 50× TAE (Tris-acetate-EDTA, pH 8.3) buffer, Coomassie Brilliant Blue-R-250, low-molecular-weight markers for SDS-PAGE (Thermo Fisher Scientific Inc., Shanghai, China), lyophilized bee venom (Sigma Aldrich, Saint Louis, MO, USA), 3.5 kDa cutoff dialysis tubing (Sigma Aldrich, Saint Louis, MO, USA), research grade Glycine (Asiamerica Group, Inc., Westwood, NJ, USA); Deionized-Distilled water (dd-H 2 O) (XiZhiMeng Co., Ltd., Shanghai, China).

    Techniques:

    Dot blot of B. papyrifera pollen-protein extract. Samples of 1 µL of pure pollen-protein extracts and 1/10 diluted pollen-protein extracts in 1X PBS blotted on a nitrocellulose paper against 1:1000 diluted anti-IgE monoclonal HRP Southern Biotech antibodies. The dark spots show IgE binding with the respective serum ID given above the spot.

    Journal: Metabolites

    Article Title: Broussonetia papyrifera Pollen Metabolome Insights, Allergenicity, and Dispersal in Response to Climate Change Variables

    doi: 10.3390/metabo15020137

    Figure Lengend Snippet: Dot blot of B. papyrifera pollen-protein extract. Samples of 1 µL of pure pollen-protein extracts and 1/10 diluted pollen-protein extracts in 1X PBS blotted on a nitrocellulose paper against 1:1000 diluted anti-IgE monoclonal HRP Southern Biotech antibodies. The dark spots show IgE binding with the respective serum ID given above the spot.

    Article Snippet: Water-soluble pollen proteins were extracted in Bio-Rad TM 1X PBS buffer Cat # 1610763.

    Techniques: Dot Blot, Binding Assay