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buffer  (Thermo Fisher)


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    Structured Review

    Thermo Fisher buffer
    Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sample+buffer/TBE+urea+sample+buffer/pmc13118919-80-16-36
    Average 95 stars, based on 1 article reviews
    buffer - by Bioz Stars, 2026-10
    95/100 stars

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    Related Articles

    Staining:

    Article Title: Structural basis for protein-free catalysis by ribonuclease P ribozyme.
    Article Snippet: .. Samples were analyzed on an 8 M urea Tris-borate-EDTA (TBE) denaturing preparative 8% polyacrylamide (29:1 acrylamide: bis-acrylamide) gel and stained with SYBRTM Gold (Invitrogen Thermo Fisher Scientific). ..

    Article Title: The E. coli DEAD box ATPase CsdA, is a NAD + capped RNA binding protein
    Article Snippet: RNA was extracted post DNase treatment using acid phenol: chloroform: isoamyl alcohol, 25:24:1 (Sigma Aldrich) and recovered by ethanol precipitation. .. The RNAs were resuspended in RNase free water post recovery, and purity confirmed by TBE Urea PAGE gel electrophoresis on a 10% TBE Urea gel (Thermo fisher Scientific) and visualized by SYBR Gold staining (Thermo Fisher Scientific). .. In vitro synthesized single stranded probe RNA was subjected to 3′ biotinylation using pCp-Biotin (Jena Bioscience) in presence of T4 RNA ligase 1 (New England Biolabs).

    Polyacrylamide Gel Electrophoresis:

    Article Title: The E. coli DEAD box ATPase CsdA, is a NAD + capped RNA binding protein
    Article Snippet: RNA was extracted post DNase treatment using acid phenol: chloroform: isoamyl alcohol, 25:24:1 (Sigma Aldrich) and recovered by ethanol precipitation. .. The RNAs were resuspended in RNase free water post recovery, and purity confirmed by TBE Urea PAGE gel electrophoresis on a 10% TBE Urea gel (Thermo fisher Scientific) and visualized by SYBR Gold staining (Thermo Fisher Scientific). .. In vitro synthesized single stranded probe RNA was subjected to 3′ biotinylation using pCp-Biotin (Jena Bioscience) in presence of T4 RNA ligase 1 (New England Biolabs).

    Gel Electrophoresis:

    Article Title: The E. coli DEAD box ATPase CsdA, is a NAD + capped RNA binding protein
    Article Snippet: RNA was extracted post DNase treatment using acid phenol: chloroform: isoamyl alcohol, 25:24:1 (Sigma Aldrich) and recovered by ethanol precipitation. .. The RNAs were resuspended in RNase free water post recovery, and purity confirmed by TBE Urea PAGE gel electrophoresis on a 10% TBE Urea gel (Thermo fisher Scientific) and visualized by SYBR Gold staining (Thermo Fisher Scientific). .. In vitro synthesized single stranded probe RNA was subjected to 3′ biotinylation using pCp-Biotin (Jena Bioscience) in presence of T4 RNA ligase 1 (New England Biolabs).

    other:

    Article Title: Systematic identification of variant-specific RNA structure-small molecule interactions exemplified by RNA G-quadruplexes.
    Article Snippet: For the index PCR, a 25μL reaction containing amplicon PCR product, 0.5 μL of Platinum SuperFi II DNA Polymerase, 1× SuperFi II Buffer (Thermo Fisher Scientific), and 0.5μM each of Nextera XT Index Kit v2 index primers (Illumina) was prepared.

    Purification:

    Article Title: DMN-seq enriches DNA hypomethylated regions for biomarker discovery using 5-methylcytosine glycosylase.
    Article Snippet: The final gel filtration was performed on a HiLoad 16/600 Superdex 200-pg column (GE Healthcare). .. 100ng of 82bp dsDNA 5mC oligo and 82bp dsDNA 5hmC oligo (IDT, Additional file 1: Table S1), respectively, were treated in 1x DME reaction buffer (80 mM Tris-HCl, pH 8, 200 mM NaCl, 200 mM EDTA, 1 mM dithiothreitol (DTT), 400 μg/mL BSA) and a reaction volume of 30 μl with 0, 125, 250, 500, 750 and 1000 ng of DME, and the treatment reaction was carried out at 37 °C for 2 h. After purification with a DNA Clean & Concentrate kit (Zymo Research), the oligos were eluted in 20 μl of water and mixed with 20 μl of Novex 2x Tris-borate-EDTA (TBE)-Urea Sample Buffer (Invitrogen) to run on 10% Novex TBE-Urea Gel (Invitrogen) at constant 180 V for 80 min. .. The gel was stained with 2 μl of SYBR Gold Nucleic Acid Gel Stain (Invitrogen) in 25 ml of TBE buffer at room temperature for 15 min.

    Luciferase:

    Article Title: Historical Pandemic and Contemporary Influenza A Viruses Reveal PB2 M631L as a Convergent Adaptation to Human ANP32
    Article Snippet: .. Equal amounts of cell lysates from luciferase assay replicates were pooled; denatured in reducing SDS-PAGE sample buffer for 5 min at 95 °C; separated on 8% SDS gels; subjected to immunoblotting with antibodies against PB2 (rabbit, ThermoFisher/Pierce, Dreieich, Germany, #PAS-32221, used at 1:2000 dilution), PB1 (rabbit, ThermoFisher/Pierce, Dreieich, Germany, # PAS34914 , 1:1000), PA (rabbit, GeneTex, Freising, Germany, #125932, 1:1000), NP (mouse, Acris, Herford, Germany, #AM00929PU-N, 1:2000) and actin (mouse, Sigma-Aldrich, St. Louis, MO, USA, #A2228, 1:5000), respectively and detected with HRP-labeled anti-mouse (DAKO, Glostrup, Denmark, #P0260) or anti-rabbit antibodies (DAKO, Glostrup, Denmark, #P0217), respectively. ..

    SDS Page:

    Article Title: Historical Pandemic and Contemporary Influenza A Viruses Reveal PB2 M631L as a Convergent Adaptation to Human ANP32
    Article Snippet: .. Equal amounts of cell lysates from luciferase assay replicates were pooled; denatured in reducing SDS-PAGE sample buffer for 5 min at 95 °C; separated on 8% SDS gels; subjected to immunoblotting with antibodies against PB2 (rabbit, ThermoFisher/Pierce, Dreieich, Germany, #PAS-32221, used at 1:2000 dilution), PB1 (rabbit, ThermoFisher/Pierce, Dreieich, Germany, # PAS34914 , 1:1000), PA (rabbit, GeneTex, Freising, Germany, #125932, 1:1000), NP (mouse, Acris, Herford, Germany, #AM00929PU-N, 1:2000) and actin (mouse, Sigma-Aldrich, St. Louis, MO, USA, #A2228, 1:5000), respectively and detected with HRP-labeled anti-mouse (DAKO, Glostrup, Denmark, #P0260) or anti-rabbit antibodies (DAKO, Glostrup, Denmark, #P0217), respectively. ..

    Western Blot:

    Article Title: Historical Pandemic and Contemporary Influenza A Viruses Reveal PB2 M631L as a Convergent Adaptation to Human ANP32
    Article Snippet: .. Equal amounts of cell lysates from luciferase assay replicates were pooled; denatured in reducing SDS-PAGE sample buffer for 5 min at 95 °C; separated on 8% SDS gels; subjected to immunoblotting with antibodies against PB2 (rabbit, ThermoFisher/Pierce, Dreieich, Germany, #PAS-32221, used at 1:2000 dilution), PB1 (rabbit, ThermoFisher/Pierce, Dreieich, Germany, # PAS34914 , 1:1000), PA (rabbit, GeneTex, Freising, Germany, #125932, 1:1000), NP (mouse, Acris, Herford, Germany, #AM00929PU-N, 1:2000) and actin (mouse, Sigma-Aldrich, St. Louis, MO, USA, #A2228, 1:5000), respectively and detected with HRP-labeled anti-mouse (DAKO, Glostrup, Denmark, #P0260) or anti-rabbit antibodies (DAKO, Glostrup, Denmark, #P0217), respectively. ..



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    Image Search Results


    Targeted activation of endogenous mitochondrial ClpP. (A) Western blots of mitochondrial lysates (30 μg) from wild‐type and ClpP‐KO HEK293T cells were probed with antibodies against ClpP and α‐tubulin, the latter being used as a loading control. (B) Analysis of ClpP and ClpX assembly was carried out in wild‐type HEK293T mitochondria through isokinetic sucrose gradient centrifugation. Mitochondrial lysate (0.65 mg) was centrifuged on a 10%–30% gradient using the SW 60Ti rotor at 40 000 rpm for 2 h and 15 min at 4°C. Small and large mitoribosomal subunits were used as a reference of migration and were immunodecorated by antibodies against marker proteins of the mt‐SSU (mS29; HUGO protein name: DAP3) and the mt‐LSU (uL13m; HUGO protein name: MRPL13). (C) Effect of ONC201‐mediated ClpP activation on casein hydrolysis in the PAGE‐based fluorescent assay. Mitochondrial lysates (50 μg) from wild‐type and KO cells were used as a source of ClpP activity, and incubated with ONC201 at a final concentration of 100 μM. Upper panels: Milk casein isoforms (α, β and k) are depicted to the left; molecular weight markers (M; Precision Plus Protein Dual Color Standards, Bio‐Rad) are indicated to the right. Middle panels: Total densitometric profile of fluorescent substrate was determined for each lane. Lower panels: Coomassie blue staining (CBS) of mitochondrial proteins was used as a loading control. (D) Chemical structure of DA29 (ClpP activator) and DA28 (negative control). (E) Effect of ClpP chemoactivation by DA29 on casein hydrolysis in the PAGE‐based fluorescent assay; DA28 was used as a negative control. For description, see panel C.

    Journal: The FASEB Journal

    Article Title: Elucidating the Molecular Impact of DA29‐Induced ClpP Chemoactivation on Mitochondrial Function

    doi: 10.1096/fj.202603398RR

    Figure Lengend Snippet: Targeted activation of endogenous mitochondrial ClpP. (A) Western blots of mitochondrial lysates (30 μg) from wild‐type and ClpP‐KO HEK293T cells were probed with antibodies against ClpP and α‐tubulin, the latter being used as a loading control. (B) Analysis of ClpP and ClpX assembly was carried out in wild‐type HEK293T mitochondria through isokinetic sucrose gradient centrifugation. Mitochondrial lysate (0.65 mg) was centrifuged on a 10%–30% gradient using the SW 60Ti rotor at 40 000 rpm for 2 h and 15 min at 4°C. Small and large mitoribosomal subunits were used as a reference of migration and were immunodecorated by antibodies against marker proteins of the mt‐SSU (mS29; HUGO protein name: DAP3) and the mt‐LSU (uL13m; HUGO protein name: MRPL13). (C) Effect of ONC201‐mediated ClpP activation on casein hydrolysis in the PAGE‐based fluorescent assay. Mitochondrial lysates (50 μg) from wild‐type and KO cells were used as a source of ClpP activity, and incubated with ONC201 at a final concentration of 100 μM. Upper panels: Milk casein isoforms (α, β and k) are depicted to the left; molecular weight markers (M; Precision Plus Protein Dual Color Standards, Bio‐Rad) are indicated to the right. Middle panels: Total densitometric profile of fluorescent substrate was determined for each lane. Lower panels: Coomassie blue staining (CBS) of mitochondrial proteins was used as a loading control. (D) Chemical structure of DA29 (ClpP activator) and DA28 (negative control). (E) Effect of ClpP chemoactivation by DA29 on casein hydrolysis in the PAGE‐based fluorescent assay; DA28 was used as a negative control. For description, see panel C.

    Article Snippet: Whole‐cell proteins (20‐30 μg), mitochondrial lysates (30 μg) or sucrose gradient fractions (10 μL) were denatured in 4X Laemmli sample buffer (Bio‐Rad) complemented with 10% 2‐mercaptoethanol, separated by SDS‐PAGE and subjected to immunoblotting as described in [ ], using the following primary antibodies: ClpP (#A306224, Antibodies.com), ClpX (#ab168338, Abcam), total OXPHOS cocktail (#ab110413, Abcam), HA‐tag (#3724, Cell Signaling Technology), uL13m (#16241–1‐AP, Proteintech), VDAC1 (#ab186321, Abcam), mS29 (# MA141279 , Thermo Fisher Scientific), α‐tubulin (#T6074, Sigma‐Aldrich) and β‐actin (#A2066, Sigma‐Aldrich).

    Techniques: Activation Assay, Western Blot, Control, Analysis, Gradient Centrifugation, Migration, Marker, Fluorescence, Activity Assay, Incubation, Concentration Assay, Molecular Weight, Staining, Negative Control