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5x native sample loading buffer 697  (Sangon Biotech)

 
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    Sangon Biotech 5x native sample loading buffer 697
    5x Native Sample Loading Buffer 697, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sample+loading+buffer/buffer+lysis+ripa/pm42298820-329-12-18
    Average 86 stars, based on 1 article reviews
    5x native sample loading buffer 697 - by Bioz Stars, 2026-09
    86/100 stars

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    Related Articles

    Lysis:

    Article Title: Mycobacterial HBHA drives mitochondrial damage-mediated apoptosis via inhibiting mitophagy in macrophages.
    Article Snippet: Heparin-binding hemagglutinin adhesin (HBHA), an important adhesion protein located on the surface of Mycobacterium tuberculosis (Mtb), plays a critical role in the pathogen infection process.. Macrophages serve as the primary effector cells that modulate the host immune response.. It has been established that HBHA can regulate macrophage autophagy and apoptosis; however, the precise mechanism underlying HBHA's effect on macrophage apoptosis remains to be fully elucidated.

    Article Title: Mechanism and Intervention of the <scp>NPY1R</scp> / <scp>CREB</scp> Signaling Axis in Regulating Inflammatory Response in Aged Ovarian Granulosa Cells and Ovarian Senescence
    Article Snippet: .. Cells were lysed on ice for 30 min with RIPA lysis buffer containing protease inhibitors (Sangon Biotech, Shanghai, China), and total protein was extracted by high- speed refrigerated centrifugation at 12000 rpm for 15 min at 4°C. ..

    Article Title: SGO1 and SGO2 are Associated With Disease Progression and an Immunosuppressive Microenvironment in Papillary Renal Cell Carcinoma.
    Article Snippet: .. Tissues and cells were lysed with RIPA Lysis Buffer (Sangon Biotech, Shanghai, China). ..

    Article Title: Targeting ZMIZ1 induces differentiation in acute myeloid leukemia via chromatin remodeling.
    Article Snippet: .. Co-immunoprecipitation (Co-IP) About 1 × 107 MOLM13 and OCI-AML3 cells were washed with PBS, lysed in lysis buffer (RIPA with 100 μM PMSF (A100754, Sangon Biotech) and 1 × protease inhibitor cocktail (C0001, TargetMol)) and clarified by centrifugation. .. Incubate the supernatant overnight at 4 °C with indicated antibodies (5 μg), followed by 2–4 h of capture with DynabeadsTM Protein G (1004D, Invitrogen).

    Article Title: RPL27 Promotes Gastric Cancer Progression by Enhancing Oxidative Phosphorylation Via FMC1.
    Article Snippet: Gastric cancer remains a leading cause of cancer‐related mortality worldwide, underscoring the urgent need for novel biomarkers and therapeutic targets.. Ribosomal proteins have recently emerged as critical regulators of tumorigenesis beyond their classical roles in protein synthesis.. Here, we investigated the expression, functional significance, and underlying mechanism of RPL27 in gastric cancer.

    Centrifugation:

    Article Title: Mycobacterial HBHA drives mitochondrial damage-mediated apoptosis via inhibiting mitophagy in macrophages.
    Article Snippet: Heparin-binding hemagglutinin adhesin (HBHA), an important adhesion protein located on the surface of Mycobacterium tuberculosis (Mtb), plays a critical role in the pathogen infection process.. Macrophages serve as the primary effector cells that modulate the host immune response.. It has been established that HBHA can regulate macrophage autophagy and apoptosis; however, the precise mechanism underlying HBHA's effect on macrophage apoptosis remains to be fully elucidated.

    Article Title: Mechanism and Intervention of the <scp>NPY1R</scp> / <scp>CREB</scp> Signaling Axis in Regulating Inflammatory Response in Aged Ovarian Granulosa Cells and Ovarian Senescence
    Article Snippet: .. Cells were lysed on ice for 30 min with RIPA lysis buffer containing protease inhibitors (Sangon Biotech, Shanghai, China), and total protein was extracted by high- speed refrigerated centrifugation at 12000 rpm for 15 min at 4°C. ..

    Article Title: Targeting ZMIZ1 induces differentiation in acute myeloid leukemia via chromatin remodeling.
    Article Snippet: .. Co-immunoprecipitation (Co-IP) About 1 × 107 MOLM13 and OCI-AML3 cells were washed with PBS, lysed in lysis buffer (RIPA with 100 μM PMSF (A100754, Sangon Biotech) and 1 × protease inhibitor cocktail (C0001, TargetMol)) and clarified by centrifugation. .. Incubate the supernatant overnight at 4 °C with indicated antibodies (5 μg), followed by 2–4 h of capture with DynabeadsTM Protein G (1004D, Invitrogen).

    Saline:

    Article Title: Dual-Site Cooperative Recognition Hybridization Chain Reaction for High-Sensitivity Imaging of lncRNA.
    Article Snippet: Developing highly sensitive and specific imaging strategies for long noncoding RNAs (lncRNAs) is crucial for disease diagnosis and therapeutic research.. However, lncRNAs are characterized by long sequence lengths (>200 nt), low abundance, and complex secondary structures, which make their sensitive and specific imaging challenging.. To address these challenges, we developed a hybridization chain reaction (HCR) strategy based on dual-site cooperative recognition for lncRNA imaging, termed dualsite cooperative recognition HCR (DCHCR).

    Transfection:

    Article Title: Dual-Site Cooperative Recognition Hybridization Chain Reaction for High-Sensitivity Imaging of lncRNA.
    Article Snippet: Developing highly sensitive and specific imaging strategies for long noncoding RNAs (lncRNAs) is crucial for disease diagnosis and therapeutic research.. However, lncRNAs are characterized by long sequence lengths (>200 nt), low abundance, and complex secondary structures, which make their sensitive and specific imaging challenging.. To address these challenges, we developed a hybridization chain reaction (HCR) strategy based on dual-site cooperative recognition for lncRNA imaging, termed dualsite cooperative recognition HCR (DCHCR).

    Protease Inhibitor:

    Article Title: Targeting ZMIZ1 induces differentiation in acute myeloid leukemia via chromatin remodeling.
    Article Snippet: .. Co-immunoprecipitation (Co-IP) About 1 × 107 MOLM13 and OCI-AML3 cells were washed with PBS, lysed in lysis buffer (RIPA with 100 μM PMSF (A100754, Sangon Biotech) and 1 × protease inhibitor cocktail (C0001, TargetMol)) and clarified by centrifugation. .. Incubate the supernatant overnight at 4 °C with indicated antibodies (5 μg), followed by 2–4 h of capture with DynabeadsTM Protein G (1004D, Invitrogen).

    Nucleic Acid Electrophoresis:

    Article Title: A wheat lncRNA-encoded peptide promotes autophagy and targets viral NIb for degradation to confer antiviral resistance.
    Article Snippet: .. 695 Native gel electrophoresis analysis 696 Purified His-TaLEP1 proteins were mixed with 5X Native Sample Loading Buffer 697 (Sangon Biotech, Shanghai, China) and incubated at room temperature for 10 min. 698 Protein samples were separated using 4-20% Hepes Native-PAGE Gel in native running 699 buffer (250 mM Tris, 50 mM HEPES, 2 mM EDTA) at 80 V for 2 h on ice. .. After 700 separation, the gel was transferred to a PVDF membrane using a semi-dry transfer 701 system (Bio-Rad) at 15 V for 45 min. Membranes were blocked with 5% non-fat milk 702 in TBST (Tris-buffered saline with 0.1% Tween-20) for 1 h at room temperature, 703 followed by immunoblotting using anti-TaLEP1 antibodies.

    Purification:

    Article Title: A wheat lncRNA-encoded peptide promotes autophagy and targets viral NIb for degradation to confer antiviral resistance.
    Article Snippet: .. 695 Native gel electrophoresis analysis 696 Purified His-TaLEP1 proteins were mixed with 5X Native Sample Loading Buffer 697 (Sangon Biotech, Shanghai, China) and incubated at room temperature for 10 min. 698 Protein samples were separated using 4-20% Hepes Native-PAGE Gel in native running 699 buffer (250 mM Tris, 50 mM HEPES, 2 mM EDTA) at 80 V for 2 h on ice. .. After 700 separation, the gel was transferred to a PVDF membrane using a semi-dry transfer 701 system (Bio-Rad) at 15 V for 45 min. Membranes were blocked with 5% non-fat milk 702 in TBST (Tris-buffered saline with 0.1% Tween-20) for 1 h at room temperature, 703 followed by immunoblotting using anti-TaLEP1 antibodies.

    Incubation:

    Article Title: A wheat lncRNA-encoded peptide promotes autophagy and targets viral NIb for degradation to confer antiviral resistance.
    Article Snippet: .. 695 Native gel electrophoresis analysis 696 Purified His-TaLEP1 proteins were mixed with 5X Native Sample Loading Buffer 697 (Sangon Biotech, Shanghai, China) and incubated at room temperature for 10 min. 698 Protein samples were separated using 4-20% Hepes Native-PAGE Gel in native running 699 buffer (250 mM Tris, 50 mM HEPES, 2 mM EDTA) at 80 V for 2 h on ice. .. After 700 separation, the gel was transferred to a PVDF membrane using a semi-dry transfer 701 system (Bio-Rad) at 15 V for 45 min. Membranes were blocked with 5% non-fat milk 702 in TBST (Tris-buffered saline with 0.1% Tween-20) for 1 h at room temperature, 703 followed by immunoblotting using anti-TaLEP1 antibodies.

    Clear Native PAGE:

    Article Title: A wheat lncRNA-encoded peptide promotes autophagy and targets viral NIb for degradation to confer antiviral resistance.
    Article Snippet: .. 695 Native gel electrophoresis analysis 696 Purified His-TaLEP1 proteins were mixed with 5X Native Sample Loading Buffer 697 (Sangon Biotech, Shanghai, China) and incubated at room temperature for 10 min. 698 Protein samples were separated using 4-20% Hepes Native-PAGE Gel in native running 699 buffer (250 mM Tris, 50 mM HEPES, 2 mM EDTA) at 80 V for 2 h on ice. .. After 700 separation, the gel was transferred to a PVDF membrane using a semi-dry transfer 701 system (Bio-Rad) at 15 V for 45 min. Membranes were blocked with 5% non-fat milk 702 in TBST (Tris-buffered saline with 0.1% Tween-20) for 1 h at room temperature, 703 followed by immunoblotting using anti-TaLEP1 antibodies.



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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