ubiquityl histone h2b lys120 d11 rabbit mab  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc ubiquityl histone h2b lys120 d11 rabbit mab
    a Model structure of the RINGA-RINGB-Rad6A-ubiquitin complex bound to the nucleosome in two views. b Close-up view of ubiquitin and <t>H2B.</t> Two lysine residues (H2BK120 and H2BK116) near G76 of ubiquitin are shown. H2BS112, whose GlcNAcylation stimulates H2BK120 ubiquitination, is also shown. c Proposed mechanistic model. The wild-type Bre1 complex can bind to the nucleosome in two orientations, but H2BK120 ubiquitination occurs only when Bre1A binds to the acidic patch, as RING A , but not RING B , can recruit Rad6A and ubiquitin. Bre1B with G974T B -A978T B double substitution can recruit Rad6A and ubiquitin; thus, H2BK120 ubiquitination occurs in both binding modes.
    Ubiquityl Histone H2b Lys120 D11 Rabbit Mab, supplied by Cell Signaling Technology Inc, 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/result/ubiquityl histone h2b lys120 d11 rabbit mab/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ubiquityl histone h2b lys120 d11 rabbit mab - by Bioz Stars, 2024-07
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    Images

    1) Product Images from "Structure of the human Bre1 complex bound to the nucleosome"

    Article Title: Structure of the human Bre1 complex bound to the nucleosome

    Journal: Nature Communications

    doi: 10.1038/s41467-024-46910-8

    a Model structure of the RINGA-RINGB-Rad6A-ubiquitin complex bound to the nucleosome in two views. b Close-up view of ubiquitin and H2B. Two lysine residues (H2BK120 and H2BK116) near G76 of ubiquitin are shown. H2BS112, whose GlcNAcylation stimulates H2BK120 ubiquitination, is also shown. c Proposed mechanistic model. The wild-type Bre1 complex can bind to the nucleosome in two orientations, but H2BK120 ubiquitination occurs only when Bre1A binds to the acidic patch, as RING A , but not RING B , can recruit Rad6A and ubiquitin. Bre1B with G974T B -A978T B double substitution can recruit Rad6A and ubiquitin; thus, H2BK120 ubiquitination occurs in both binding modes.
    Figure Legend Snippet: a Model structure of the RINGA-RINGB-Rad6A-ubiquitin complex bound to the nucleosome in two views. b Close-up view of ubiquitin and H2B. Two lysine residues (H2BK120 and H2BK116) near G76 of ubiquitin are shown. H2BS112, whose GlcNAcylation stimulates H2BK120 ubiquitination, is also shown. c Proposed mechanistic model. The wild-type Bre1 complex can bind to the nucleosome in two orientations, but H2BK120 ubiquitination occurs only when Bre1A binds to the acidic patch, as RING A , but not RING B , can recruit Rad6A and ubiquitin. Bre1B with G974T B -A978T B double substitution can recruit Rad6A and ubiquitin; thus, H2BK120 ubiquitination occurs in both binding modes.

    Techniques Used: Binding Assay

    anti ubiquityl histone h2b lys120 d11 xp  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc anti ubiquityl histone h2b lys120 d11 xp
    Anti Ubiquityl Histone H2b Lys120 D11 Xp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ubiquityl histone h2b lys120 d11 xp rabbit mab  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Structured Review

    Cell Signaling Technology Inc ubiquityl histone h2b lys120 d11 xp rabbit mab
    RAD6 promotes expression of CSC proteins and acquisition of stemness phenotype and is important for efficient DDR. Control and siRAD6 transfected OV90 cells were treated with 20 μM carboplatin and DDR and CSC proteins were assessed by Western blot. RAD6 knockdown impairs carboplatin induced DDR (A & B) and decreases pro-transcription histone modifications <t>H2B-Ub</t> and H3K79me3 and expression of CSC signaling proteins (B & C). The results presented are representative blots and the average values obtained from three independent experiments with each band adjusted to the corresponding GAPDH control. (D) Consistent with the expression studies, knocking down RAD6 impaired the ability of OV90 cells to form stem cell spheres by anchorage-independent growth, as both number and size of number of spheroids decreased. Left panel shows 1 view field of a representative stem cell sphere culture and the right panel is total spheroid count from multiple experiments. (E) Multiple siRNAs targeting either RAD6A or RAD6B were used to ensure the impact was not siRNA specific and to confirm that regulation occurs through both RAD6 isoforms. Left panel is a representative blot and the right is a compilation of 3 experiments. *p<0.05 and **p<0.01.
    Ubiquityl Histone H2b Lys120 D11 Xp Rabbit Mab, supplied by Cell Signaling Technology Inc, 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/result/ubiquityl histone h2b lys120 d11 xp rabbit mab/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ubiquityl histone h2b lys120 d11 xp rabbit mab - by Bioz Stars, 2024-07
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    Images

    1) Product Images from "RAD6 promotes DNA repair and stem cell signaling in ovarian cancer and is a promising therapeutic target to prevent and treat acquired chemoresistance"

    Article Title: RAD6 promotes DNA repair and stem cell signaling in ovarian cancer and is a promising therapeutic target to prevent and treat acquired chemoresistance

    Journal: Oncogene

    doi: 10.1038/onc.2017.279

    RAD6 promotes expression of CSC proteins and acquisition of stemness phenotype and is important for efficient DDR. Control and siRAD6 transfected OV90 cells were treated with 20 μM carboplatin and DDR and CSC proteins were assessed by Western blot. RAD6 knockdown impairs carboplatin induced DDR (A & B) and decreases pro-transcription histone modifications H2B-Ub and H3K79me3 and expression of CSC signaling proteins (B & C). The results presented are representative blots and the average values obtained from three independent experiments with each band adjusted to the corresponding GAPDH control. (D) Consistent with the expression studies, knocking down RAD6 impaired the ability of OV90 cells to form stem cell spheres by anchorage-independent growth, as both number and size of number of spheroids decreased. Left panel shows 1 view field of a representative stem cell sphere culture and the right panel is total spheroid count from multiple experiments. (E) Multiple siRNAs targeting either RAD6A or RAD6B were used to ensure the impact was not siRNA specific and to confirm that regulation occurs through both RAD6 isoforms. Left panel is a representative blot and the right is a compilation of 3 experiments. *p<0.05 and **p<0.01.
    Figure Legend Snippet: RAD6 promotes expression of CSC proteins and acquisition of stemness phenotype and is important for efficient DDR. Control and siRAD6 transfected OV90 cells were treated with 20 μM carboplatin and DDR and CSC proteins were assessed by Western blot. RAD6 knockdown impairs carboplatin induced DDR (A & B) and decreases pro-transcription histone modifications H2B-Ub and H3K79me3 and expression of CSC signaling proteins (B & C). The results presented are representative blots and the average values obtained from three independent experiments with each band adjusted to the corresponding GAPDH control. (D) Consistent with the expression studies, knocking down RAD6 impaired the ability of OV90 cells to form stem cell spheres by anchorage-independent growth, as both number and size of number of spheroids decreased. Left panel shows 1 view field of a representative stem cell sphere culture and the right panel is total spheroid count from multiple experiments. (E) Multiple siRNAs targeting either RAD6A or RAD6B were used to ensure the impact was not siRNA specific and to confirm that regulation occurs through both RAD6 isoforms. Left panel is a representative blot and the right is a compilation of 3 experiments. *p<0.05 and **p<0.01.

    Techniques Used: Expressing, Transfection, Western Blot

    Carboplatin treatment induces expression of RAD6 and RAD6 subsequently regulates ALDH1A1 and SOX2 through pro-transcription histone modifications. (A) To determine if RAD6 regulates CSC gene expression, OV90 cells transfected with control siRNA or siRAD6B-1 and treated with carboplatin or vehicle (DMSO) were used for qRT-PCR. Knockdown of RAD6B decreased both basal and carboplatin-induced expression of (A) SOX2 and (B) ALDH1A1. (C) ChIP was used in SKOV3 cells to determine if depletion of RAD6 (siRAD6B-1) altered the level of pro-transcription H2B-Ub in the promoters of ALDH1A1 (243 to 418 bp upstream of ATG) and SOX2 (542 TO 778 bp before ATG) genes. The β-actin is not regulated by RAD6 and was used as a negative control. (D) ChIP for β-catenin binding to putative binding sites ([CTTTG(A/T)(A/T)] located in same regions analyzed for H2B-Ub in C). RAD6B depletion (siRNA) reduces β-catenin interaction at a putative β-catenin/TCF binding site located at 284–290 bp upstream of the ALDH1A1 ATG. There are no putative β-catenin binding sites in the β-actin promoter thus it was used as a negative control. (E) Systematic exposure of SKOV3 cells to sub-lethal carboplatin (2.5μM) caused progressive increase in RAD6 and associated H2B-Ub levels as well as expression of RAD18 and CSC proteins. (F) Ability to grow as stem cell spheres increased with acquired carboplatin resistance indicating correlation between stemness and chemoresistance. *p<0.05, **p<0.01 and ***p<0.001.
    Figure Legend Snippet: Carboplatin treatment induces expression of RAD6 and RAD6 subsequently regulates ALDH1A1 and SOX2 through pro-transcription histone modifications. (A) To determine if RAD6 regulates CSC gene expression, OV90 cells transfected with control siRNA or siRAD6B-1 and treated with carboplatin or vehicle (DMSO) were used for qRT-PCR. Knockdown of RAD6B decreased both basal and carboplatin-induced expression of (A) SOX2 and (B) ALDH1A1. (C) ChIP was used in SKOV3 cells to determine if depletion of RAD6 (siRAD6B-1) altered the level of pro-transcription H2B-Ub in the promoters of ALDH1A1 (243 to 418 bp upstream of ATG) and SOX2 (542 TO 778 bp before ATG) genes. The β-actin is not regulated by RAD6 and was used as a negative control. (D) ChIP for β-catenin binding to putative binding sites ([CTTTG(A/T)(A/T)] located in same regions analyzed for H2B-Ub in C). RAD6B depletion (siRNA) reduces β-catenin interaction at a putative β-catenin/TCF binding site located at 284–290 bp upstream of the ALDH1A1 ATG. There are no putative β-catenin binding sites in the β-actin promoter thus it was used as a negative control. (E) Systematic exposure of SKOV3 cells to sub-lethal carboplatin (2.5μM) caused progressive increase in RAD6 and associated H2B-Ub levels as well as expression of RAD18 and CSC proteins. (F) Ability to grow as stem cell spheres increased with acquired carboplatin resistance indicating correlation between stemness and chemoresistance. *p<0.05, **p<0.01 and ***p<0.001.

    Techniques Used: Expressing, Transfection, Quantitative RT-PCR, Negative Control, Binding Assay

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    Cell Signaling Technology Inc ubiquityl histone h2b lys120 d11 rabbit mab
    a Model structure of the RINGA-RINGB-Rad6A-ubiquitin complex bound to the nucleosome in two views. b Close-up view of ubiquitin and <t>H2B.</t> Two lysine residues (H2BK120 and H2BK116) near G76 of ubiquitin are shown. H2BS112, whose GlcNAcylation stimulates H2BK120 ubiquitination, is also shown. c Proposed mechanistic model. The wild-type Bre1 complex can bind to the nucleosome in two orientations, but H2BK120 ubiquitination occurs only when Bre1A binds to the acidic patch, as RING A , but not RING B , can recruit Rad6A and ubiquitin. Bre1B with G974T B -A978T B double substitution can recruit Rad6A and ubiquitin; thus, H2BK120 ubiquitination occurs in both binding modes.
    Ubiquityl Histone H2b Lys120 D11 Rabbit Mab, supplied by Cell Signaling Technology Inc, 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/result/ubiquityl histone h2b lys120 d11 rabbit mab/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ubiquityl histone h2b lys120 d11 rabbit mab - by Bioz Stars, 2024-07
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    95
    Cell Signaling Technology Inc anti ubiquityl histone h2b lys120 d11 xp
    a Model structure of the RINGA-RINGB-Rad6A-ubiquitin complex bound to the nucleosome in two views. b Close-up view of ubiquitin and <t>H2B.</t> Two lysine residues (H2BK120 and H2BK116) near G76 of ubiquitin are shown. H2BS112, whose GlcNAcylation stimulates H2BK120 ubiquitination, is also shown. c Proposed mechanistic model. The wild-type Bre1 complex can bind to the nucleosome in two orientations, but H2BK120 ubiquitination occurs only when Bre1A binds to the acidic patch, as RING A , but not RING B , can recruit Rad6A and ubiquitin. Bre1B with G974T B -A978T B double substitution can recruit Rad6A and ubiquitin; thus, H2BK120 ubiquitination occurs in both binding modes.
    Anti Ubiquityl Histone H2b Lys120 D11 Xp, supplied by Cell Signaling Technology Inc, 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/result/anti ubiquityl histone h2b lys120 d11 xp/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti ubiquityl histone h2b lys120 d11 xp - by Bioz Stars, 2024-07
    95/100 stars
      Buy from Supplier

    86
    Cell Signaling Technology Inc ubiquityl histone h2b lys120 d11 xp rabbit mab
    RAD6 promotes expression of CSC proteins and acquisition of stemness phenotype and is important for efficient DDR. Control and siRAD6 transfected OV90 cells were treated with 20 μM carboplatin and DDR and CSC proteins were assessed by Western blot. RAD6 knockdown impairs carboplatin induced DDR (A & B) and decreases pro-transcription histone modifications <t>H2B-Ub</t> and H3K79me3 and expression of CSC signaling proteins (B & C). The results presented are representative blots and the average values obtained from three independent experiments with each band adjusted to the corresponding GAPDH control. (D) Consistent with the expression studies, knocking down RAD6 impaired the ability of OV90 cells to form stem cell spheres by anchorage-independent growth, as both number and size of number of spheroids decreased. Left panel shows 1 view field of a representative stem cell sphere culture and the right panel is total spheroid count from multiple experiments. (E) Multiple siRNAs targeting either RAD6A or RAD6B were used to ensure the impact was not siRNA specific and to confirm that regulation occurs through both RAD6 isoforms. Left panel is a representative blot and the right is a compilation of 3 experiments. *p<0.05 and **p<0.01.
    Ubiquityl Histone H2b Lys120 D11 Xp Rabbit Mab, supplied by Cell Signaling Technology Inc, 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/result/ubiquityl histone h2b lys120 d11 xp rabbit mab/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ubiquityl histone h2b lys120 d11 xp rabbit mab - by Bioz Stars, 2024-07
    86/100 stars
      Buy from Supplier

    Image Search Results


    a Model structure of the RINGA-RINGB-Rad6A-ubiquitin complex bound to the nucleosome in two views. b Close-up view of ubiquitin and H2B. Two lysine residues (H2BK120 and H2BK116) near G76 of ubiquitin are shown. H2BS112, whose GlcNAcylation stimulates H2BK120 ubiquitination, is also shown. c Proposed mechanistic model. The wild-type Bre1 complex can bind to the nucleosome in two orientations, but H2BK120 ubiquitination occurs only when Bre1A binds to the acidic patch, as RING A , but not RING B , can recruit Rad6A and ubiquitin. Bre1B with G974T B -A978T B double substitution can recruit Rad6A and ubiquitin; thus, H2BK120 ubiquitination occurs in both binding modes.

    Journal: Nature Communications

    Article Title: Structure of the human Bre1 complex bound to the nucleosome

    doi: 10.1038/s41467-024-46910-8

    Figure Lengend Snippet: a Model structure of the RINGA-RINGB-Rad6A-ubiquitin complex bound to the nucleosome in two views. b Close-up view of ubiquitin and H2B. Two lysine residues (H2BK120 and H2BK116) near G76 of ubiquitin are shown. H2BS112, whose GlcNAcylation stimulates H2BK120 ubiquitination, is also shown. c Proposed mechanistic model. The wild-type Bre1 complex can bind to the nucleosome in two orientations, but H2BK120 ubiquitination occurs only when Bre1A binds to the acidic patch, as RING A , but not RING B , can recruit Rad6A and ubiquitin. Bre1B with G974T B -A978T B double substitution can recruit Rad6A and ubiquitin; thus, H2BK120 ubiquitination occurs in both binding modes.

    Article Snippet: For Western blotting, Ubiquityl-Histone H2B (Lys120) (D11) Rabbit mAb (No. 5546; Cell Signaling) was used as the primary antibody (1:1000 dilution), goat anti-rabbit IgG-HRP (sc-2004; Santa Cruz Biotechnology) as the secondary antibody (1:2000 dilution), and ECL Prime (Cytiva) as the chemiluminescent reagent.

    Techniques: Binding Assay

    RAD6 promotes expression of CSC proteins and acquisition of stemness phenotype and is important for efficient DDR. Control and siRAD6 transfected OV90 cells were treated with 20 μM carboplatin and DDR and CSC proteins were assessed by Western blot. RAD6 knockdown impairs carboplatin induced DDR (A & B) and decreases pro-transcription histone modifications H2B-Ub and H3K79me3 and expression of CSC signaling proteins (B & C). The results presented are representative blots and the average values obtained from three independent experiments with each band adjusted to the corresponding GAPDH control. (D) Consistent with the expression studies, knocking down RAD6 impaired the ability of OV90 cells to form stem cell spheres by anchorage-independent growth, as both number and size of number of spheroids decreased. Left panel shows 1 view field of a representative stem cell sphere culture and the right panel is total spheroid count from multiple experiments. (E) Multiple siRNAs targeting either RAD6A or RAD6B were used to ensure the impact was not siRNA specific and to confirm that regulation occurs through both RAD6 isoforms. Left panel is a representative blot and the right is a compilation of 3 experiments. *p<0.05 and **p<0.01.

    Journal: Oncogene

    Article Title: RAD6 promotes DNA repair and stem cell signaling in ovarian cancer and is a promising therapeutic target to prevent and treat acquired chemoresistance

    doi: 10.1038/onc.2017.279

    Figure Lengend Snippet: RAD6 promotes expression of CSC proteins and acquisition of stemness phenotype and is important for efficient DDR. Control and siRAD6 transfected OV90 cells were treated with 20 μM carboplatin and DDR and CSC proteins were assessed by Western blot. RAD6 knockdown impairs carboplatin induced DDR (A & B) and decreases pro-transcription histone modifications H2B-Ub and H3K79me3 and expression of CSC signaling proteins (B & C). The results presented are representative blots and the average values obtained from three independent experiments with each band adjusted to the corresponding GAPDH control. (D) Consistent with the expression studies, knocking down RAD6 impaired the ability of OV90 cells to form stem cell spheres by anchorage-independent growth, as both number and size of number of spheroids decreased. Left panel shows 1 view field of a representative stem cell sphere culture and the right panel is total spheroid count from multiple experiments. (E) Multiple siRNAs targeting either RAD6A or RAD6B were used to ensure the impact was not siRNA specific and to confirm that regulation occurs through both RAD6 isoforms. Left panel is a representative blot and the right is a compilation of 3 experiments. *p<0.05 and **p<0.01.

    Article Snippet: Rabbit IgG supplied with the kit was utilized as a negative control and chromatin containing monoubiquitinated H2B was immunoprecipitated using Ubiquityl-Histone H2B (Lys120) (D11) XP Rabbit mAb (Cell Signaling #5546) and chromatin bound to β-Catenin was immunoprecipitated with anti-β-Catenin antibody (Bethyl #A302-010A).

    Techniques: Expressing, Transfection, Western Blot

    Carboplatin treatment induces expression of RAD6 and RAD6 subsequently regulates ALDH1A1 and SOX2 through pro-transcription histone modifications. (A) To determine if RAD6 regulates CSC gene expression, OV90 cells transfected with control siRNA or siRAD6B-1 and treated with carboplatin or vehicle (DMSO) were used for qRT-PCR. Knockdown of RAD6B decreased both basal and carboplatin-induced expression of (A) SOX2 and (B) ALDH1A1. (C) ChIP was used in SKOV3 cells to determine if depletion of RAD6 (siRAD6B-1) altered the level of pro-transcription H2B-Ub in the promoters of ALDH1A1 (243 to 418 bp upstream of ATG) and SOX2 (542 TO 778 bp before ATG) genes. The β-actin is not regulated by RAD6 and was used as a negative control. (D) ChIP for β-catenin binding to putative binding sites ([CTTTG(A/T)(A/T)] located in same regions analyzed for H2B-Ub in C). RAD6B depletion (siRNA) reduces β-catenin interaction at a putative β-catenin/TCF binding site located at 284–290 bp upstream of the ALDH1A1 ATG. There are no putative β-catenin binding sites in the β-actin promoter thus it was used as a negative control. (E) Systematic exposure of SKOV3 cells to sub-lethal carboplatin (2.5μM) caused progressive increase in RAD6 and associated H2B-Ub levels as well as expression of RAD18 and CSC proteins. (F) Ability to grow as stem cell spheres increased with acquired carboplatin resistance indicating correlation between stemness and chemoresistance. *p<0.05, **p<0.01 and ***p<0.001.

    Journal: Oncogene

    Article Title: RAD6 promotes DNA repair and stem cell signaling in ovarian cancer and is a promising therapeutic target to prevent and treat acquired chemoresistance

    doi: 10.1038/onc.2017.279

    Figure Lengend Snippet: Carboplatin treatment induces expression of RAD6 and RAD6 subsequently regulates ALDH1A1 and SOX2 through pro-transcription histone modifications. (A) To determine if RAD6 regulates CSC gene expression, OV90 cells transfected with control siRNA or siRAD6B-1 and treated with carboplatin or vehicle (DMSO) were used for qRT-PCR. Knockdown of RAD6B decreased both basal and carboplatin-induced expression of (A) SOX2 and (B) ALDH1A1. (C) ChIP was used in SKOV3 cells to determine if depletion of RAD6 (siRAD6B-1) altered the level of pro-transcription H2B-Ub in the promoters of ALDH1A1 (243 to 418 bp upstream of ATG) and SOX2 (542 TO 778 bp before ATG) genes. The β-actin is not regulated by RAD6 and was used as a negative control. (D) ChIP for β-catenin binding to putative binding sites ([CTTTG(A/T)(A/T)] located in same regions analyzed for H2B-Ub in C). RAD6B depletion (siRNA) reduces β-catenin interaction at a putative β-catenin/TCF binding site located at 284–290 bp upstream of the ALDH1A1 ATG. There are no putative β-catenin binding sites in the β-actin promoter thus it was used as a negative control. (E) Systematic exposure of SKOV3 cells to sub-lethal carboplatin (2.5μM) caused progressive increase in RAD6 and associated H2B-Ub levels as well as expression of RAD18 and CSC proteins. (F) Ability to grow as stem cell spheres increased with acquired carboplatin resistance indicating correlation between stemness and chemoresistance. *p<0.05, **p<0.01 and ***p<0.001.

    Article Snippet: Rabbit IgG supplied with the kit was utilized as a negative control and chromatin containing monoubiquitinated H2B was immunoprecipitated using Ubiquityl-Histone H2B (Lys120) (D11) XP Rabbit mAb (Cell Signaling #5546) and chromatin bound to β-Catenin was immunoprecipitated with anti-β-Catenin antibody (Bethyl #A302-010A).

    Techniques: Expressing, Transfection, Quantitative RT-PCR, Negative Control, Binding Assay