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6x sds-page sample loading buffer (G Biosciences)

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G Biosciences 6x sds-page sample loading buffer
6x Sds Page Sample Loading Buffer, supplied by G Biosciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sample+loading+buffer/sds+page+sample+loading+buffer/pm40181610-59-20-22
Average 90 stars, based on 1 article reviews

6x sds-page sample loading buffer - by Bioz Stars, 2026-09

90/100 stars

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Article Title: Exploring protein structural adaptations and polyphenol interactions: Influences on digestibility in pigeon pea dal and whole grains under heat and germination conditions.
Article Snippet: Pigeon pea, a protein-rich legume with low protein digestibility (PD) due to its high polyphenol content and other antinutritional factors (ANFs).. Consequently, processing methods are crucial to improve PD.. We investigated the effects of thermal treatments (cooking, hydrothermal, autoclaving, infrared rays) treatments and germination on modulation of PD, its properties and association with ANFs in two distinct genotypes based on polyphenol content: high (Pusa Arhar 2018–4) and low (ICP-1452).

Article Title: Primate TRIM34 is a broadly-acting, TRIM5-dependent lentiviral restriction factor.
Article Snippet: Cells were then lysed on ice for 30 min in 20 mM HEPES (Fisher Scientific, Fair Lawn, NJ, #BP310-1) containing 8 M urea (Sigma-Aldrich #U-6504), 50 mM DL-Dithiothreitol (DTT) (Gold Biotechnology, St. Louis, MO, #DTT10), 0.1% w/v SDS (Fisher Scientific #BP166-500), 1.5 mM MgCl2 (Sigma-Aldrich #208337-100G), 0.5 mM CaCl2 (Sigma-Aldrich #C-3306), 50 μg/mL DNAse I (Roche Diagnostics, Mannheim, Germany, #10104159001), and 1X EDTA-free protease inhibitor cocktail (Roche Diagnostics #11836170001). .. 6X SDS-PAGE sample loading buffer (G Biosciences, St. Louis, MO #785 -701) containing 5% v/v 2-mercaptoethanol (Sigma-Aldrich #M3148100ML) was added to lysates. .. Lysates were acid treated with 50 mM HCl (Sigma-Aldrich #320331-300ML) and then boiled at 95 °C for 7 min. After cooling, lysates were neutralized with 50 mM NaOH (Sigma-Aldrich #72068-100ML).

Article Title: Role of TRDMT1/DNMT2 in stress adaptation and its influence on transcriptome and proteome dynamics under osmotic stress in Physcomitrium patens.
Article Snippet: .. For this, 2 SDS-PAGE sample loading buffer (G Biosciences) was added to the bead bound complex and heated to 70 C for 10 min. After electrophoresis the gel was silver stained following the protocol described in Singh et al., 2020. ..

Article Title: Improved nutritional and functional properties of plant protein isolate blends through steam infusion: A study on chickpea, brown rice and defatted peanut protein blends.
Article Snippet: This study examined the impact of steam-infusion on defatted peanut (Pn), chickpea (Cp), and rice (R) protein isolates (PI) and their blends.. Steam infusion significantly increased protein content (up to 83.13 % in PnPI, 75.25 % in CpPI, 76.13 % in RPI) and digestibility (98.92 % in peanut, 98.84 % in chickpea) and improved protein solubility.. Steam-infused protein blends (SIPB) showed higher protein content (84.44 %), digestibility (89.61 %), improved EAA scores, and enhanced functional properties compared to non-steam infused protein blends (NSIPB).

Article Title: β-Hairpin Alignment Alters Oligomer Formation in Aβ-Derived Peptides
Article Snippet: .. 1 μl of 6X SDS-PAGE sample loading buffer (G Biosciences) and 2 μl 18 MΩ deionized water was added per 3 μl of sample solution to create working solutions. .. 5 μl aliquots of each working solution were run on a 16.5% polyacrylamide Mini-PROTEAN® Tris/Tricine Precast Gel from Bio-Rad Laboratories.2 Reagents for Tricine SDS-PAGE were prepared and used according to recipes and procedures detailed in the MiniPROTEAN Precast Gels Instruction Manual and Application Guide (2011) from Bio-Rad Laboratories.2 The gel was run at a constant 100 V for approximately 2 hours.

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Nucleic Acid Electrophoresis:

Article Title: An iPSC model of fragile X syndrome reflects clinical phenotypes and reveals m 6 A-mediated epi-transcriptomic dysregulation underlying synaptic dysfunction
Article Snippet: Protein concentrations were determined using the PierceTM BCA Protein Assay Kit (ThermoFisher). .. Equal amounts of protein lysates were denatured in SDS-polyacrylamide gel electrophoresis (PAGE) Sample Loading Buffer (G-Biosciences), separated on 4-12% Bolt Bis-Tris Plus Protein Gels (ThermoFisher), and transferred to polyvinylidene fluoride (PVDF) membranes (Millipore) using the XCell SureLockTM Mini-Cell system (ThermoFisher). .. The membranes were blocked for 1 hour at room temperature (RT) with 5% non-fat milk in Tris-buffered saline containing Tween-20 (TBST) (blocking buffer), followed by overnight incubation at 4°C with the following primary antibodies diluted in blocking buffer: rabbit polyclonal anti-FMRP (1:1000; Abcam), rabbit monoclonal Synapsin II (1:1000; Abcam), mouse monoclonal SV2 (1:1000; DSHB), rabbit monoclonal METTL3 (1:500; MedChemExpress), rabbit polyclonal METTL14 (1:1000; Sigma), rabbit monoclonal WTAP (1:500; Cell Signaling Technology), and mouse monoclonal GAPDH (1:5000; Santa Cruz Biotechnology).

Polyacrylamide Gel Electrophoresis:

Western Blot:

Article Title: Individual differences in behavioral responses to predator odor predict subsequent stress reactivity in female rats.
Article Snippet: .. Western blot techniques were completed in the manner previously described (smiley et al., 2023). a solution containing 6X sDs-PaGe sample loading buffer (G-Biosciences) + β-mercaptoethanol was added to each sample at a 1:6 ratio prior to heating for 5 minutes at 75 °c and loading onto gels (mini-protean gels, Bio-Rad, hercules, ca). .. Gels were run at 135 volts for 1 hour submerged in 1X running buffer (Bio-Rad) for electrophoresis.

other:

Article Title: Nuclease-induced stepwise photodropping (NISP) to precisely investigate single-stranded DNA degradation behaviors of exonucleases and endonucleases
Article Snippet: After the desired incubation time, reactions were stopped by adding 10 L of 2× TBE/urea sample buffer (G-Biosciences) and heating at 65°C for 20 minutes.

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$a , Domain architecture of RAP80 and ARISC constructs. FL, full-length; SIM, small ubiquitin-like modifier (SUMO)-interacting motif; UIM, ubiquitin-interacting motif; AIR, Abraxas1-interacting region; ZnF, zinc finger; MPN, Mpr1, Pad1 N-terminal; CC, coiled coil; UEV, ubiquitin E2 variant; vWFA, von Willebrand factor type A ( left ). Schematics of indicated complexes ( right ). b , SDS-PAGE analysis of ARISC, ARISC–RAP80, and ARISC–RAP80 AIR. c , K63-linked ubiquitin chains (1 µM) were incubated with ARISC or ARISC–RAP80 (5 nM) for the indicated time points. Cleavage activity was analysed by SDS-PAGE and silver staining. Data are representative of two independent experiments. d , K63-Ub2, -Ub4, and - Ub7 chains (1 µM) were incubated with ARISC, ARISC–RAP80, or ARISC–RAP80 AIR (5 nM) for the indicated time points. Cleavage activity was analysed as in c . Data are representative of three independent experiments. e , Schematics ( left ) and SDS-PAGE analysis ( right ) of indicated complexes. dStrepII, double StrepII tag. * indicates Abraxas1 degradation product. f , Alexa-Fluor 488 (AF488) labelled distally (AF488- Cys Ub4 K63R ) blocked K63-Ub4 chains (1.5 µM) were incubated with ARISC–RAP80, ARISC–RAP80 ΔUIMs, or ARISC–RAP80 ΔZnF (10 nM) for the indicated time points. Cleavage activity was analysed by SDS-PAGE and fluorescence scanning ( left ; see Methods ). The disappearance of the K63-Ub4 parent band was quantified using densitometry, and plotted as fraction of substrate consumed (%). Data points are mean ± SEM of two independent experiments ( right ). g , Cyclical and linear K63-Ub5 chains (2 µM) were incubated with ARISC or ARISC–RAP80 (10 nM) for the indicated time points. Cleavage activity was analysed by SDS-PAGE and Oriole staining. Data are representative of two independent experiments. Ub, ubiquitin; DUB, deubiquitylating enzyme. * indicates lower molecular weight ubiquitin species.$

Journal: bioRxiv

Article Title: Mechanism of K63-linked polyubiquitin recognition and cleavage by the BRCA1-A complex

doi: 10.64898/2026.06.05.730395

Figure Lengend Snippet: a , Domain architecture of RAP80 and ARISC constructs. FL, full-length; SIM, small ubiquitin-like modifier (SUMO)-interacting motif; UIM, ubiquitin-interacting motif; AIR, Abraxas1-interacting region; ZnF, zinc finger; MPN, Mpr1, Pad1 N-terminal; CC, coiled coil; UEV, ubiquitin E2 variant; vWFA, von Willebrand factor type A ( left ). Schematics of indicated complexes ( right ). b , SDS-PAGE analysis of ARISC, ARISC–RAP80, and ARISC–RAP80 AIR. c , K63-linked ubiquitin chains (1 µM) were incubated with ARISC or ARISC–RAP80 (5 nM) for the indicated time points. Cleavage activity was analysed by SDS-PAGE and silver staining. Data are representative of two independent experiments. d , K63-Ub2, -Ub4, and - Ub7 chains (1 µM) were incubated with ARISC, ARISC–RAP80, or ARISC–RAP80 AIR (5 nM) for the indicated time points. Cleavage activity was analysed as in c . Data are representative of three independent experiments. e , Schematics ( left ) and SDS-PAGE analysis ( right ) of indicated complexes. dStrepII, double StrepII tag. * indicates Abraxas1 degradation product. f , Alexa-Fluor 488 (AF488) labelled distally (AF488- Cys Ub4 K63R ) blocked K63-Ub4 chains (1.5 µM) were incubated with ARISC–RAP80, ARISC–RAP80 ΔUIMs, or ARISC–RAP80 ΔZnF (10 nM) for the indicated time points. Cleavage activity was analysed by SDS-PAGE and fluorescence scanning ( left ; see Methods ). The disappearance of the K63-Ub4 parent band was quantified using densitometry, and plotted as fraction of substrate consumed (%). Data points are mean ± SEM of two independent experiments ( right ). g , Cyclical and linear K63-Ub5 chains (2 µM) were incubated with ARISC or ARISC–RAP80 (10 nM) for the indicated time points. Cleavage activity was analysed by SDS-PAGE and Oriole staining. Data are representative of two independent experiments. Ub, ubiquitin; DUB, deubiquitylating enzyme. * indicates lower molecular weight ubiquitin species.

Article Snippet: Reactions were stopped with the addition of 3 μL 4x SDS-PAGE loading dye [240 mM Tris-HCl pH 6.8, 40% (v/v) glycerol, 8% (w/v) SDS, 0.04% (w/v) bromophenol blue, and 5% (v/v) β-Mercaptoethanol], and products were separated on 4-12% or 12% Nu-PAGE Bis-Tris gels (Invitrogen).

Techniques: Construct, Ubiquitin Proteomics, Variant Assay, SDS Page, Incubation, Activity Assay, Silver Staining, Fluorescence, Staining, Molecular Weight

a , K63-Ub2, -Ub4, and -Ub7 chains (1 µM) were incubated with ARISC WT or the indicated ARISC variants (5 nM) for 60 minutes. Cleavage activity was analysed by SDS-PAGE and silver staining. Data are representative of two independent experiments. b, SDS-PAGE analysis of ARISC(E33A)–RAP80, ARISC(E33A) BRCC36(S98K) –RAP80, ARISC(E33A) Abraxas1(Δ42-55) –RAP80, and ARISC(E33A) BRCC45(ΔLoop) –RAP80. dStrepII, double StrepII tag. * indicates Abraxas1 degradation product. c, Spectral shift assays measuring binding of labelled ARISC(E33A)–RAP80 or the indicated mutant complexes (40 nM) to cyclical K63-Ub6 chains (20 µM-0 µM). Data points are mean ± SEM of two independent experiments carried out in technical duplicates. Dissociation constants (K d ) are indicated; CI, confidence interval. d, Representative images of WT or mutants BRCC36 IRIF in HT-29 cells 4 h post irradiation (10 Gy). Scale bar is 10 µm. e, Western blots showing BRCC36 protein levels in HT-29 cells reconstituted with WT or mutants BRCC36 as indicated (l eft ). Scatter plot showing quantification of the BRCC36 IRIF described in d . Data represent mean ± SEM derived from n ≥ 300 nuclei examined over two independent experiments; p values are indicated, unpaired two-tailed t test ( right ). f, K63-Ub2, -Ub4, and -Ub7 chains (1 µM) were incubated with ARISC WT or ARISC Δ42-55 (Abraxas1 Δ42-55) (5 nM) for up to 60 minutes. Cleavage activity was analysed as in a . Data are representative of two independent experiments. DUB, deubiquitylating enzyme; WT, wild type; Ub, ubiquitin.

Journal: bioRxiv

Article Title: Mechanism of K63-linked polyubiquitin recognition and cleavage by the BRCA1-A complex

doi: 10.64898/2026.06.05.730395

Figure Lengend Snippet: a , K63-Ub2, -Ub4, and -Ub7 chains (1 µM) were incubated with ARISC WT or the indicated ARISC variants (5 nM) for 60 minutes. Cleavage activity was analysed by SDS-PAGE and silver staining. Data are representative of two independent experiments. b, SDS-PAGE analysis of ARISC(E33A)–RAP80, ARISC(E33A) BRCC36(S98K) –RAP80, ARISC(E33A) Abraxas1(Δ42-55) –RAP80, and ARISC(E33A) BRCC45(ΔLoop) –RAP80. dStrepII, double StrepII tag. * indicates Abraxas1 degradation product. c, Spectral shift assays measuring binding of labelled ARISC(E33A)–RAP80 or the indicated mutant complexes (40 nM) to cyclical K63-Ub6 chains (20 µM-0 µM). Data points are mean ± SEM of two independent experiments carried out in technical duplicates. Dissociation constants (K d ) are indicated; CI, confidence interval. d, Representative images of WT or mutants BRCC36 IRIF in HT-29 cells 4 h post irradiation (10 Gy). Scale bar is 10 µm. e, Western blots showing BRCC36 protein levels in HT-29 cells reconstituted with WT or mutants BRCC36 as indicated (l eft ). Scatter plot showing quantification of the BRCC36 IRIF described in d . Data represent mean ± SEM derived from n ≥ 300 nuclei examined over two independent experiments; p values are indicated, unpaired two-tailed t test ( right ). f, K63-Ub2, -Ub4, and -Ub7 chains (1 µM) were incubated with ARISC WT or ARISC Δ42-55 (Abraxas1 Δ42-55) (5 nM) for up to 60 minutes. Cleavage activity was analysed as in a . Data are representative of two independent experiments. DUB, deubiquitylating enzyme; WT, wild type; Ub, ubiquitin.

Techniques: Incubation, Activity Assay, SDS Page, Silver Staining, Binding Assay, Mutagenesis, Irradiation, Western Blot, Derivative Assay, Two Tailed Test, Ubiquitin Proteomics

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