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ief buffer concentrate  (Cytiva Europe)


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    Structured Review

    Cytiva Europe ief buffer concentrate
    Ief Buffer Concentrate, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 95/100, based on 3283 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/ief+buffer/IPG+buffer/pm41742785-135-59-64
    Average 95 stars, based on 3283 article reviews
    ief buffer concentrate - by Bioz Stars, 2026-09
    95/100 stars

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    Related Articles

    Recombinant:

    Article Title: AMH regulates ovary size by counteracting the positive influence of clustered ovarian follicle growth.
    Article Snippet: Immunofluorescence was imaged on an Odyssey infrared fluorescence scanner (Licor). .. Aliquots (625 ng) of recombinant human AMH (produced in HEK293 cells by PX Therapeutics under contract to University of Otago, �20% proAMH, 80% AMHN, C) were combined with 130 μl of an isoelectric focusing (IEF) rehydration buffer [containing 7 mol/l urea, 2 mol/l thiourea, 2% w/v CHAPS, 50 mM DTT, 5 mmol/l TCEP (triscarboxyethylphosphine), to which 25 μl of IEF buffer concentrate (IPG buffer, GE Healthcare, Cytiva) was added per 0.5 ml of rehydration buffer, just prior to use], and the solution used to rehydrate overnight Immobiline DryStrip pH 3–10, 7 cm, linear gradient IEF strips (GE Healthcare). .. The rehydrated IEF strips were then subjected to electrophoresis in an IEF flatbed electrophoresis system (IPGphor, Pharmacia Biotech) in a ceramic-welled plate with the IEF strips submerged under mineral oil, and using a voltage programme from 200 to 8000 V over 10 h, with a V/h target of 30 000 V/h.

    Produced:

    Article Title: AMH regulates ovary size by counteracting the positive influence of clustered ovarian follicle growth.
    Article Snippet: Immunofluorescence was imaged on an Odyssey infrared fluorescence scanner (Licor). .. Aliquots (625 ng) of recombinant human AMH (produced in HEK293 cells by PX Therapeutics under contract to University of Otago, �20% proAMH, 80% AMHN, C) were combined with 130 μl of an isoelectric focusing (IEF) rehydration buffer [containing 7 mol/l urea, 2 mol/l thiourea, 2% w/v CHAPS, 50 mM DTT, 5 mmol/l TCEP (triscarboxyethylphosphine), to which 25 μl of IEF buffer concentrate (IPG buffer, GE Healthcare, Cytiva) was added per 0.5 ml of rehydration buffer, just prior to use], and the solution used to rehydrate overnight Immobiline DryStrip pH 3–10, 7 cm, linear gradient IEF strips (GE Healthcare). .. The rehydrated IEF strips were then subjected to electrophoresis in an IEF flatbed electrophoresis system (IPGphor, Pharmacia Biotech) in a ceramic-welled plate with the IEF strips submerged under mineral oil, and using a voltage programme from 200 to 8000 V over 10 h, with a V/h target of 30 000 V/h.

    Electrofocusing:

    Article Title: AMH regulates ovary size by counteracting the positive influence of clustered ovarian follicle growth.
    Article Snippet: Immunofluorescence was imaged on an Odyssey infrared fluorescence scanner (Licor). .. Aliquots (625 ng) of recombinant human AMH (produced in HEK293 cells by PX Therapeutics under contract to University of Otago, �20% proAMH, 80% AMHN, C) were combined with 130 μl of an isoelectric focusing (IEF) rehydration buffer [containing 7 mol/l urea, 2 mol/l thiourea, 2% w/v CHAPS, 50 mM DTT, 5 mmol/l TCEP (triscarboxyethylphosphine), to which 25 μl of IEF buffer concentrate (IPG buffer, GE Healthcare, Cytiva) was added per 0.5 ml of rehydration buffer, just prior to use], and the solution used to rehydrate overnight Immobiline DryStrip pH 3–10, 7 cm, linear gradient IEF strips (GE Healthcare). .. The rehydrated IEF strips were then subjected to electrophoresis in an IEF flatbed electrophoresis system (IPGphor, Pharmacia Biotech) in a ceramic-welled plate with the IEF strips submerged under mineral oil, and using a voltage programme from 200 to 8000 V over 10 h, with a V/h target of 30 000 V/h.



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    ief cathode buffer  (Bio-Rad)
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    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.
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    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 <t>1X</t> <t>PBS</t> 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.
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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