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laemmli sample buffer  (Bio-Rad)


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    Bio-Rad laemmli sample buffer
    Laemmli Sample Buffer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 11874 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/4x+laemmli+sample+buffer/4x+Laemmli+Sample+Buffer/pmc13688550-69-32-35
    Average 99 stars, based on 11874 article reviews
    laemmli sample buffer - by Bioz Stars, 2026-11
    99/100 stars

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    other:

    Article Title: A systemic circadian nicotinic acid riboside (NaR) signal engages the unfolded protein response and adipogenesis via the prefoldin complex.
    Article Snippet: REAGENT or RESOURCES SOURCE IDENTIFIER Antibodies anti-CEBPA Cell Signaling Cat#8178; RRID: AB_11178517 anti-ATF4 Cell Signaling Cat#11815; RRID: AB_2616025 anti-XBP1s Cell Signaling Cat#40435; RRID: AB_2891025 anti-ATF6 Novus Biologicals Cat#40256; RRID: AB_2058774 anti-alpha-TUBULIN Cell Signaling Cat#9099; RRID: AB_10695471 anti-P84 Genetex Cat#GTX70220; RRID: AB_372637 Rabbit IgG-HRP Sigma-Aldrich Cat#A9169; RRID: AB_258434 Mouse IgG-HRP Sigma-Aldrich Cat#5278; RRID: AB_258232 Biological samples Mouse skeletal muscle, C57BL/6 This study N/A Mouse epididymal white adipose tissue (eWAT), C57BL/6 This study N/A Mouse brain tissue, C57BL/6 This study N/A Chemicals, peptides, and recombinant proteins DharmaFECT 1 Transfection Reagent Horizon Discovery Cat#T-2001-02 DMEM 1.0g/L Glucose w/o L-Gln Lonza Cat#12-707F SYBR-green Master Mix Bio-Rad Cat#1708884 Amersham ECL Prime Western Blotting Detection Reagent GE Healthcare Cat#RPN2232 Blotto Immunoanalytical Grade (Non-Fat Dry Milk) BioNordika Cat#B501-0500 DTT Sigma-Aldrich Cat#10197777001 2-Mercaptoethanol Sigma-Aldrich Cat#M3148-100ML RIPA buffer Thermo Fisher Scientific Cat#89901 FGF2 human Sigma-Aldrich Cat#F0291 Insulin (liquid, ready to use, 10mg/mL, 5mL) Sigma-Aldrich Cat#I9278 T3 Sigma-Aldrich Cat#T6397 Transferrin Sigma-Aldrich Cat#T8158 IBMX (3-Isobutyl-1-methylxanthin) - for human cell line Sigma-Aldrich Cat#I5879 Rosiglitazone (100 mg) Cayman Chemicals Cat#71740 Dexamethasone Sigma-Aldrich Cat#D1756 IBMX (3-Isobutyl-1-methylxanthin) - for murine cell lines Sigma-Aldrich Cat#7018 Bovine insulin Sigma-Aldrich Cat#I6634 0.5% Trypsin/EDTA (10x) Invitrogen (GIBCO) Cat#15400-054 Penicilline G 10000U/mL/Streptomycine 10000μg/mL Invitrogen (GIBCO) Cat#15140-122 HEPES 1M Invitrogen (GIBCO) Cat#15630-056 Ham’s F-12 Nutrient Mix Invitrogen (GIBCO) Cat#21765-037 DMEM, low glucose, pyruvate (+glutamine) Invitrogen (GIBCO) Cat#31885-023 4x Laemmli Sample Buffer Bio-Rad Cat#1610747 Bodipy 493/503 Thermo Fisher Scientific Cat#D3922 Hoechst Thermo Fisher Scientific Cat#34580 (Continued on next page) 18 Cell Reports 45, 118136, October 27, 2026

    Concentration Assay:

    Article Title: γ-Radiation induces long-term dose-related proteomic and phosphorylated-tau species changes in non-human primate hippocampus
    Article Snippet: .. Protein samples were mixed with dH2O and 10% by volume 10x NuPAGE Sample Reducing Agent (Life Technologies, cat#2353153, Carlsbad, CA, USA), 25% by volume 4x Laemmli Sample Buffer (Bio-Rad Laboratories, Inc., cat1610747, Hercules, CA, USA), and a calculated volume of protein to achieve 2 μg/μl concentration, denatured for 10 min at 70 °C. .. For all brain regions, 20 μg of protein per sample (Control n = 5, 4 Gy n = 5, 8 Gy n = 4) were loaded into Novex Nupage 4–12% Bis-Tris Gels (Life Technologies, cat#NP0329, Carlsbad, CA, USA) for 30 min electrophoresis at constant 200 V, with 2.5 μl Precision Plus Protein Dual Color Standards (Bio-Rad Laboratories, cat#1610374, Hercules, CA, USA) loaded into one well per gel.

    Centrifugation:

    Article Title: Mechanisms of transcription control by distal enhancers from single-gene nanoscopy.
    Article Snippet: mESCs were lysed in RIPA buffer (50 mM Tris–HCl pH 7.4, 150 mM NaCl, 1% Triton X-100, 0.5% sodium deoxycholate, and 0.1% SDS) supplemented with protease inhibitors (Thermo fisher, A32965) for 30 min at 4 ◦C. .. Lysates were clarified by centrifugation at 12,000 g for 5 min, and the supernatants were mixed with 4x Laemmli Sample Buffer (Bio-Rad, 1610747) and boiled at 95 ◦C for 5 min. Proteins were resolved on 4–20% SDS–PAGE gels (Bio-Rad) at 120 V for 1 hr and transferred to 0.2 μm PVDF membranes (Bio-Rad,1620177) at 300 mA for 80 min. Membranes were blocked with 3% non-fat milk (CST, 9999) in TBST for 1 hr at room temperature and incubated with primary antibodies overnight at 4 ◦C. ..

    Incubation:

    Article Title: Mechanisms of transcription control by distal enhancers from single-gene nanoscopy.
    Article Snippet: mESCs were lysed in RIPA buffer (50 mM Tris–HCl pH 7.4, 150 mM NaCl, 1% Triton X-100, 0.5% sodium deoxycholate, and 0.1% SDS) supplemented with protease inhibitors (Thermo fisher, A32965) for 30 min at 4 ◦C. .. Lysates were clarified by centrifugation at 12,000 g for 5 min, and the supernatants were mixed with 4x Laemmli Sample Buffer (Bio-Rad, 1610747) and boiled at 95 ◦C for 5 min. Proteins were resolved on 4–20% SDS–PAGE gels (Bio-Rad) at 120 V for 1 hr and transferred to 0.2 μm PVDF membranes (Bio-Rad,1620177) at 300 mA for 80 min. Membranes were blocked with 3% non-fat milk (CST, 9999) in TBST for 1 hr at room temperature and incubated with primary antibodies overnight at 4 ◦C. ..

    Western Blot:

    Article Title: Lycopene inhibits proliferation, induces apoptosis, and suppresses migration in cervical cancer cells: involvement of PI3K/Akt signaling.
    Article Snippet: 1 Laboratorio de Ciencias de la Naturaleza, Departamento de Ciencias de la Naturaleza, Centro Universitario del Sur (CUSur), Universidad de Guadalajara, Ciudad Guzmán, Jalisco, México 2 Departamento de Fisiología, Instituto Nacional de Cardiología Ignacio Chávez, Juan Badiano 1, Sección XVI, Tlalpan, 14080 Ciudad de Mexico, México 3 Centro de Investigación, Facultad de Medicina, Facultad de Medicina y Cirugía, UNAM-UABJO, Universidad Autónoma “Benito Juárez” de Oaxaca, 68020 Ciudad Oaxaca de Juárez, México Abstract Cervical cancer remains a major cause of mortality worldwide, highlighting the need for alternative therapeutic strategies.. Lycopene, a dietary carotenoid with known antioxidant properties, has demonstrated anticancer activity in several malignancies; however, its mechanistic effects in cervical cancer remain poorly understood.. We hypothesize that lycopene inhibits the growth of cervical cancer cell lines and certain cancer-related processes.

    Electrophoresis:

    Article Title: Lycopene inhibits proliferation, induces apoptosis, and suppresses migration in cervical cancer cells: involvement of PI3K/Akt signaling.
    Article Snippet: 1 Laboratorio de Ciencias de la Naturaleza, Departamento de Ciencias de la Naturaleza, Centro Universitario del Sur (CUSur), Universidad de Guadalajara, Ciudad Guzmán, Jalisco, México 2 Departamento de Fisiología, Instituto Nacional de Cardiología Ignacio Chávez, Juan Badiano 1, Sección XVI, Tlalpan, 14080 Ciudad de Mexico, México 3 Centro de Investigación, Facultad de Medicina, Facultad de Medicina y Cirugía, UNAM-UABJO, Universidad Autónoma “Benito Juárez” de Oaxaca, 68020 Ciudad Oaxaca de Juárez, México Abstract Cervical cancer remains a major cause of mortality worldwide, highlighting the need for alternative therapeutic strategies.. Lycopene, a dietary carotenoid with known antioxidant properties, has demonstrated anticancer activity in several malignancies; however, its mechanistic effects in cervical cancer remain poorly understood.. We hypothesize that lycopene inhibits the growth of cervical cancer cell lines and certain cancer-related processes.

    Blocking Assay:

    Article Title: Lycopene inhibits proliferation, induces apoptosis, and suppresses migration in cervical cancer cells: involvement of PI3K/Akt signaling.
    Article Snippet: 1 Laboratorio de Ciencias de la Naturaleza, Departamento de Ciencias de la Naturaleza, Centro Universitario del Sur (CUSur), Universidad de Guadalajara, Ciudad Guzmán, Jalisco, México 2 Departamento de Fisiología, Instituto Nacional de Cardiología Ignacio Chávez, Juan Badiano 1, Sección XVI, Tlalpan, 14080 Ciudad de Mexico, México 3 Centro de Investigación, Facultad de Medicina, Facultad de Medicina y Cirugía, UNAM-UABJO, Universidad Autónoma “Benito Juárez” de Oaxaca, 68020 Ciudad Oaxaca de Juárez, México Abstract Cervical cancer remains a major cause of mortality worldwide, highlighting the need for alternative therapeutic strategies.. Lycopene, a dietary carotenoid with known antioxidant properties, has demonstrated anticancer activity in several malignancies; however, its mechanistic effects in cervical cancer remain poorly understood.. We hypothesize that lycopene inhibits the growth of cervical cancer cell lines and certain cancer-related processes.

    SDS Page:

    Article Title: Small extracellular vesicles as mediators of paracrine senescence in cellular models of aging.
    Article Snippet: sEV were lysed using the following lysis buffer [(TrisHCl 20 mM pH 7.6; DTT 1 mM; EDTA 1 mM; PMSF 1 mM; benzamidine 1 mM; sodium molybdate 2 mM; β-sodium glycerophosphate 2 mM; sodium orthovanadate 0.2 mM; KCl 120 mM; 1 mg/ml (each) leupeptin, pepstatin A and antipain; Nonidet P-40 0.5% (v/v); Triton X-100 0.1% (v/v)] (all from Sigma- Aldrich)]. .. Lysates were diluted with 4X Laemmli Sample Buffer (Bio-Rad, UK) and an equal number of particles (3x109) were separated in SDS-PAGE gels at 80V. ..



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    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, <t>Bio‐Rad)</t> 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.
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    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