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loading buffer  (Thermo Fisher)


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    Structured Review

    Thermo Fisher loading buffer
    Loading Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/loading+buffer+4x/LDS-sample+buffer+(4X)%2C+reducing/pm42048165-211-0-2
    Average 99 stars, based on 1 article reviews
    loading buffer - by Bioz Stars, 2026-09
    99/100 stars

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    Related Articles

    Polyacrylamide Gel Electrophoresis:

    Article Title: Chimeric switch scaffold protein augments CAR synapse formation and signaling networks.
    Article Snippet: Protein concentrations were measured using the BCA assay (Thermo Fisher Scientific). .. Samples were mixed with 4×lithium dodecyl sulfate (LDS) sample buffer (Thermo Fisher Scientific), boiled at 70°C for 10 min, and separated on 4–12% BisTris sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS- PAGE) gels (Thermo Fisher Scientific). .. Proteins were transferred to polyvinylidene difluoride (PVDF) membranes using an iBlot2 Dry blotting system (Thermo Fisher Scientific).

    SDS Page:

    Article Title: Chimeric switch scaffold protein augments CAR synapse formation and signaling networks.
    Article Snippet: Protein concentrations were measured using the BCA assay (Thermo Fisher Scientific). .. Samples were mixed with 4×lithium dodecyl sulfate (LDS) sample buffer (Thermo Fisher Scientific), boiled at 70°C for 10 min, and separated on 4–12% BisTris sodium dodecyl sulfate- polyacrylamide gel electrophoresis (SDS- PAGE) gels (Thermo Fisher Scientific). .. Proteins were transferred to polyvinylidene difluoride (PVDF) membranes using an iBlot2 Dry blotting system (Thermo Fisher Scientific).

    Article Title: NLRP3 haploinsufficiency unmasks a compensatory NLRP1-NLRP3 interaction that drives accelerated aging in mice.
    Article Snippet: .. For SDS- PAGE, proteins were extracted using radioimmunoprecipitation assay (RIPA) buffer (Thermo Fisher Scientific, Waltham, MA, USA, 89901), preserved in LDS NuPAGE buffer (Thermo Fisher Scientific, Waltham, MA, USA, NP0008), and heatshocked at 95°C for 2 min. Gel electrophoresis was performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Tris- Glycine- SDS buffer (Bio- Rad, Hercules, CA, USA, 1610772) for 45 min. For native PAGE, proteins were extracted using native cell lysis buffer (Abcam, Cambridge, UK, ab156035) and preserved in TrisGlycine sample buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC267). .. Gel electrophoresis were performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Novex Tris- Glycine buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC2672) for 4 hours in ice.

    Article Title: TREM2 restrains myeloid inflammasome activation to protect against photoreceptor degeneration.
    Article Snippet: Total protein concentration was determined using a BCA assay (Thermo Fisher Scientific, 23227). .. Equal amounts of protein lysates were denatured in 4X NuPAGETM LDS Sample Buffer containing 10% 2- mercaptoethanol at 70°C for 10 min. After SDS-PAGE (Thermo Fisher Scientific) separation and transfer to PVDF membranes, membranes were blocked with 5% nonfat dry milk in Tris-buffered saline containing 0.1% Tween 20 and incubated with primary and secondary antibodies (Table S2). .. Protein bands were visualized using ECL substrate (Thermo Fisher Scientific, 32106) and quantified by densitometry.

    Radio Immunoprecipitation:

    Article Title: NLRP3 haploinsufficiency unmasks a compensatory NLRP1-NLRP3 interaction that drives accelerated aging in mice.
    Article Snippet: .. For SDS- PAGE, proteins were extracted using radioimmunoprecipitation assay (RIPA) buffer (Thermo Fisher Scientific, Waltham, MA, USA, 89901), preserved in LDS NuPAGE buffer (Thermo Fisher Scientific, Waltham, MA, USA, NP0008), and heatshocked at 95°C for 2 min. Gel electrophoresis was performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Tris- Glycine- SDS buffer (Bio- Rad, Hercules, CA, USA, 1610772) for 45 min. For native PAGE, proteins were extracted using native cell lysis buffer (Abcam, Cambridge, UK, ab156035) and preserved in TrisGlycine sample buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC267). .. Gel electrophoresis were performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Novex Tris- Glycine buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC2672) for 4 hours in ice.

    Nucleic Acid Electrophoresis:

    Article Title: NLRP3 haploinsufficiency unmasks a compensatory NLRP1-NLRP3 interaction that drives accelerated aging in mice.
    Article Snippet: .. For SDS- PAGE, proteins were extracted using radioimmunoprecipitation assay (RIPA) buffer (Thermo Fisher Scientific, Waltham, MA, USA, 89901), preserved in LDS NuPAGE buffer (Thermo Fisher Scientific, Waltham, MA, USA, NP0008), and heatshocked at 95°C for 2 min. Gel electrophoresis was performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Tris- Glycine- SDS buffer (Bio- Rad, Hercules, CA, USA, 1610772) for 45 min. For native PAGE, proteins were extracted using native cell lysis buffer (Abcam, Cambridge, UK, ab156035) and preserved in TrisGlycine sample buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC267). .. Gel electrophoresis were performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Novex Tris- Glycine buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC2672) for 4 hours in ice.

    Article Title: Metabolic engineering of Saccharomyces cerevisiae for co-production of ergothioneine, salidroside and gadusol.
    Article Snippet: .. These crude extracts were then mixed with LDS Sample Buffer (ThermoFisher Scientific, Shanghai, China) and heated at 95 ◦C for 10 min. For protein separation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was conducted on 10% Bis-Tris gels using MES running buffer at a constant voltage of 150 V. The gel was stained with Coomassie Brilliant Blue dye and the image was captured using a Gel Doc imaging system (Bio-Rad, Hercules, USA). ..

    Staining:

    Article Title: NLRP3 haploinsufficiency unmasks a compensatory NLRP1-NLRP3 interaction that drives accelerated aging in mice.
    Article Snippet: .. For SDS- PAGE, proteins were extracted using radioimmunoprecipitation assay (RIPA) buffer (Thermo Fisher Scientific, Waltham, MA, USA, 89901), preserved in LDS NuPAGE buffer (Thermo Fisher Scientific, Waltham, MA, USA, NP0008), and heatshocked at 95°C for 2 min. Gel electrophoresis was performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Tris- Glycine- SDS buffer (Bio- Rad, Hercules, CA, USA, 1610772) for 45 min. For native PAGE, proteins were extracted using native cell lysis buffer (Abcam, Cambridge, UK, ab156035) and preserved in TrisGlycine sample buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC267). .. Gel electrophoresis were performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Novex Tris- Glycine buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC2672) for 4 hours in ice.

    Article Title: Metabolic engineering of Saccharomyces cerevisiae for co-production of ergothioneine, salidroside and gadusol.
    Article Snippet: .. These crude extracts were then mixed with LDS Sample Buffer (ThermoFisher Scientific, Shanghai, China) and heated at 95 ◦C for 10 min. For protein separation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was conducted on 10% Bis-Tris gels using MES running buffer at a constant voltage of 150 V. The gel was stained with Coomassie Brilliant Blue dye and the image was captured using a Gel Doc imaging system (Bio-Rad, Hercules, USA). ..

    Clear Native PAGE:

    Article Title: NLRP3 haploinsufficiency unmasks a compensatory NLRP1-NLRP3 interaction that drives accelerated aging in mice.
    Article Snippet: .. For SDS- PAGE, proteins were extracted using radioimmunoprecipitation assay (RIPA) buffer (Thermo Fisher Scientific, Waltham, MA, USA, 89901), preserved in LDS NuPAGE buffer (Thermo Fisher Scientific, Waltham, MA, USA, NP0008), and heatshocked at 95°C for 2 min. Gel electrophoresis was performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Tris- Glycine- SDS buffer (Bio- Rad, Hercules, CA, USA, 1610772) for 45 min. For native PAGE, proteins were extracted using native cell lysis buffer (Abcam, Cambridge, UK, ab156035) and preserved in TrisGlycine sample buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC267). .. Gel electrophoresis were performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Novex Tris- Glycine buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC2672) for 4 hours in ice.

    Lysis:

    Article Title: NLRP3 haploinsufficiency unmasks a compensatory NLRP1-NLRP3 interaction that drives accelerated aging in mice.
    Article Snippet: .. For SDS- PAGE, proteins were extracted using radioimmunoprecipitation assay (RIPA) buffer (Thermo Fisher Scientific, Waltham, MA, USA, 89901), preserved in LDS NuPAGE buffer (Thermo Fisher Scientific, Waltham, MA, USA, NP0008), and heatshocked at 95°C for 2 min. Gel electrophoresis was performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Tris- Glycine- SDS buffer (Bio- Rad, Hercules, CA, USA, 1610772) for 45 min. For native PAGE, proteins were extracted using native cell lysis buffer (Abcam, Cambridge, UK, ab156035) and preserved in TrisGlycine sample buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC267). .. Gel electrophoresis were performed using 4 to 20% MiniPROTEAN TGX Stain- Free Protein Gels (Bio- Rad, Hercules, CA, USA) at 200 V in Novex Tris- Glycine buffer (Thermo Fisher Scientific, Waltham, MA, USA, LC2672) for 4 hours in ice.

    Article Title: Bioinstructive Orthogonally-crosslinked Ovoprotein Microgels for Modular Bioprinting
    Article Snippet: The fluorescence signal was detected using Power SYBR PCR master mix (Applied Biosystems, Invitrogen, USA) in a real-time PCR machine (QuantStudioTM 5, Thermo Fisher Scientific). .. Western Blot Analysis: At given time points of cultivation, spheroid-laden constructs were collected, and total protein from them were lysed using RIPA Lysis buffer (Thermo-Scientific) supplemented with 1× Protease/Phosphatase Inhibitor Cocktail (Cell Signaling Technologies, USA) and 1× LDS sample buffer (Invitrogen, USA). ..

    Saline:

    Article Title: TREM2 restrains myeloid inflammasome activation to protect against photoreceptor degeneration.
    Article Snippet: Total protein concentration was determined using a BCA assay (Thermo Fisher Scientific, 23227). .. Equal amounts of protein lysates were denatured in 4X NuPAGETM LDS Sample Buffer containing 10% 2- mercaptoethanol at 70°C for 10 min. After SDS-PAGE (Thermo Fisher Scientific) separation and transfer to PVDF membranes, membranes were blocked with 5% nonfat dry milk in Tris-buffered saline containing 0.1% Tween 20 and incubated with primary and secondary antibodies (Table S2). .. Protein bands were visualized using ECL substrate (Thermo Fisher Scientific, 32106) and quantified by densitometry.

    Incubation:

    Article Title: TREM2 restrains myeloid inflammasome activation to protect against photoreceptor degeneration.
    Article Snippet: Total protein concentration was determined using a BCA assay (Thermo Fisher Scientific, 23227). .. Equal amounts of protein lysates were denatured in 4X NuPAGETM LDS Sample Buffer containing 10% 2- mercaptoethanol at 70°C for 10 min. After SDS-PAGE (Thermo Fisher Scientific) separation and transfer to PVDF membranes, membranes were blocked with 5% nonfat dry milk in Tris-buffered saline containing 0.1% Tween 20 and incubated with primary and secondary antibodies (Table S2). .. Protein bands were visualized using ECL substrate (Thermo Fisher Scientific, 32106) and quantified by densitometry.

    Imaging:

    Article Title: Metabolic engineering of Saccharomyces cerevisiae for co-production of ergothioneine, salidroside and gadusol.
    Article Snippet: .. These crude extracts were then mixed with LDS Sample Buffer (ThermoFisher Scientific, Shanghai, China) and heated at 95 ◦C for 10 min. For protein separation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was conducted on 10% Bis-Tris gels using MES running buffer at a constant voltage of 150 V. The gel was stained with Coomassie Brilliant Blue dye and the image was captured using a Gel Doc imaging system (Bio-Rad, Hercules, USA). ..

    Membrane:

    Article Title: Extended poly(A) tails are a shared feature of herpesvirus mRNAs.
    Article Snippet: In all cases, cells at 90% confluence were harvested by adding TRIzol and RNA extracted according to manufacturer’s protocol with addition of GlycoBlue (ThermoFisher) during the first precipitation step. .. Protein lysates were prepared in LDS Sample Buffer (Invitrogen) and separated on 4–12% bis-Tris NuPAGE gels (Invitrogen) before transfer to nitrocellulose membrane. .. Primary antibodies used were PABPC1 (Santa Cruz, SC-32318), CNOT1 (Proteintech, 14276–1-AP), GAPDH (Cell Signaling, 2118), and α-tubulin (Proteintech, 66031–1-Ig).

    Article Title: Methods of delivering anionic agents in vivo using non-viral nanoparticle-based delivery systems
    Article Snippet: MTS cytotoxicity assay kit was obtained from Promega (Madison, WI, USA). .. Subcloning DH5-alpha competent cells and Lipofectamine 2000, Tracklt 10-bp DNA ladder (0.5 μg/μl), Pre-cast Nupage 4-12% Bis-Tris gels, Nupage MES running buffer, Nupage transfer buffer, Nupage LDS sample buffer (4×), nitrocellulose membrane 0.45 μm, blotting filter paper and magic mark (1 Kb) protein ladder were obtained from Invitrogen (Burlington, ON, Canada). .. Orange dye solution (6×) was obtained from Fermentas (Burlington, ON, Canada). pEGFPataxin1 (E3-82Q) plasmid was obtained from Dr. Zoghbi Huda from Baylor College of Medicine, Houston, USA.

    Subcloning:

    Article Title: Methods of delivering anionic agents in vivo using non-viral nanoparticle-based delivery systems
    Article Snippet: MTS cytotoxicity assay kit was obtained from Promega (Madison, WI, USA). .. Subcloning DH5-alpha competent cells and Lipofectamine 2000, Tracklt 10-bp DNA ladder (0.5 μg/μl), Pre-cast Nupage 4-12% Bis-Tris gels, Nupage MES running buffer, Nupage transfer buffer, Nupage LDS sample buffer (4×), nitrocellulose membrane 0.45 μm, blotting filter paper and magic mark (1 Kb) protein ladder were obtained from Invitrogen (Burlington, ON, Canada). .. Orange dye solution (6×) was obtained from Fermentas (Burlington, ON, Canada). pEGFPataxin1 (E3-82Q) plasmid was obtained from Dr. Zoghbi Huda from Baylor College of Medicine, Houston, USA.

    Western Blot:

    Article Title: Bioinstructive Orthogonally-crosslinked Ovoprotein Microgels for Modular Bioprinting
    Article Snippet: The fluorescence signal was detected using Power SYBR PCR master mix (Applied Biosystems, Invitrogen, USA) in a real-time PCR machine (QuantStudioTM 5, Thermo Fisher Scientific). .. Western Blot Analysis: At given time points of cultivation, spheroid-laden constructs were collected, and total protein from them were lysed using RIPA Lysis buffer (Thermo-Scientific) supplemented with 1× Protease/Phosphatase Inhibitor Cocktail (Cell Signaling Technologies, USA) and 1× LDS sample buffer (Invitrogen, USA). ..

    Construct:

    Article Title: Bioinstructive Orthogonally-crosslinked Ovoprotein Microgels for Modular Bioprinting
    Article Snippet: The fluorescence signal was detected using Power SYBR PCR master mix (Applied Biosystems, Invitrogen, USA) in a real-time PCR machine (QuantStudioTM 5, Thermo Fisher Scientific). .. Western Blot Analysis: At given time points of cultivation, spheroid-laden constructs were collected, and total protein from them were lysed using RIPA Lysis buffer (Thermo-Scientific) supplemented with 1× Protease/Phosphatase Inhibitor Cocktail (Cell Signaling Technologies, USA) and 1× LDS sample buffer (Invitrogen, USA). ..



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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 <t>,</t> <t>SDS-PAGE</t> 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.
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    lds loading buffer  (Thermo Fisher)
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    97
    Thermo Fisher western blot analysis lds loading buffer
    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 <t>,</t> <t>SDS-PAGE</t> 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.
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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 <t>,</t> <t>SDS-PAGE</t> 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.
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    Image Search Results


    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.

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