nonidet-p40 Roche Search Results


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  • 95
    Millipore lacz wash buffer
    Lacz Wash Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche nonidet p40
    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
    Nonidet P40, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 4070 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Roche nonidet p40 substitute
    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
    Nonidet P40 Substitute, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Roche nonidet p40 detergent
    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
    Nonidet P40 Detergent, supplied by Roche, used in various techniques. Bioz Stars score: 89/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Roche nonidet p40 buffer
    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
    Nonidet P40 Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 82/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Roche nonidet p40 np40
    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
    Nonidet P40 Np40, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Roche nonidet p40 plus protease inhibitor cocktails
    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
    Nonidet P40 Plus Protease Inhibitor Cocktails, supplied by Roche, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Roche detergent nonidet p40 np40
    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
    Detergent Nonidet P40 Np40, supplied by Roche, used in various techniques. Bioz Stars score: 78/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Roche nonidet p40 lysis buffer
    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
    Nonidet P40 Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Roche nonidet p40 np 40
    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
    Nonidet P40 Np 40, supplied by Roche, used in various techniques. Bioz Stars score: 90/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Roche enzyme compatible solvent system isopropanol nonidat p40
    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
    Enzyme Compatible Solvent System Isopropanol Nonidat P40, supplied by Roche, used in various techniques. Bioz Stars score: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    np40  (Roche)
    99
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    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
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    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.
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    A. <t>AEGFR-immunoprecipitation</t> from MDA-MB-231 cell extracts followed by western blotting shows that B6H12 treatment for 15 min disrupts the association between EGFR and CD47 and inhibits EGFR-Y 1068 phosphorylation. B . CD47-immunoprecipitation showed that a fraction of EGFR co-immunoprecipitates with EGFR. B6H12 treatment for 15 min reduced interaction between CD47 and EGFR in MDA-MB-231 cells. ( C .- D .) MDA-MB-231 cells were pretreated with B6H12 for 15 minutes followed by EGF for 5 minutes, and IP-western blotting was performed using phospho-EGFR antibody. D . Quantification of three experiments was analyzed using the t-test (*P
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    A. <t>AEGFR-immunoprecipitation</t> from MDA-MB-231 cell extracts followed by western blotting shows that B6H12 treatment for 15 min disrupts the association between EGFR and CD47 and inhibits EGFR-Y 1068 phosphorylation. B . CD47-immunoprecipitation showed that a fraction of EGFR co-immunoprecipitates with EGFR. B6H12 treatment for 15 min reduced interaction between CD47 and EGFR in MDA-MB-231 cells. ( C .- D .) MDA-MB-231 cells were pretreated with B6H12 for 15 minutes followed by EGF for 5 minutes, and IP-western blotting was performed using phospho-EGFR antibody. D . Quantification of three experiments was analyzed using the t-test (*P
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    A. <t>AEGFR-immunoprecipitation</t> from MDA-MB-231 cell extracts followed by western blotting shows that B6H12 treatment for 15 min disrupts the association between EGFR and CD47 and inhibits EGFR-Y 1068 phosphorylation. B . CD47-immunoprecipitation showed that a fraction of EGFR co-immunoprecipitates with EGFR. B6H12 treatment for 15 min reduced interaction between CD47 and EGFR in MDA-MB-231 cells. ( C .- D .) MDA-MB-231 cells were pretreated with B6H12 for 15 minutes followed by EGF for 5 minutes, and IP-western blotting was performed using phospho-EGFR antibody. D . Quantification of three experiments was analyzed using the t-test (*P
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    A. <t>AEGFR-immunoprecipitation</t> from MDA-MB-231 cell extracts followed by western blotting shows that B6H12 treatment for 15 min disrupts the association between EGFR and CD47 and inhibits EGFR-Y 1068 phosphorylation. B . CD47-immunoprecipitation showed that a fraction of EGFR co-immunoprecipitates with EGFR. B6H12 treatment for 15 min reduced interaction between CD47 and EGFR in MDA-MB-231 cells. ( C .- D .) MDA-MB-231 cells were pretreated with B6H12 for 15 minutes followed by EGF for 5 minutes, and IP-western blotting was performed using phospho-EGFR antibody. D . Quantification of three experiments was analyzed using the t-test (*P
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    Image Search Results


    IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ).  B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third  and  fourth panels ). β-Actin was used as a loading control ( bottom panel ).  C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control.  D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.

    Journal: The Journal of Biological Chemistry

    Article Title: Host Protein Ku70 Binds and Protects HIV-1 Integrase from Proteasomal Degradation and Is Required for HIV Replication *

    doi: 10.1074/jbc.M110.184739

    Figure Lengend Snippet: IN is degraded through the Lys 48 -linked polyubiquitination proteasomal pathway, and Ku70 protects IN by reducing the overall ubiquitination level in the cells and partially blocking ubiquitination of IN and its bound cellular proteins. A , IN is degraded through Lys 48 -linked polyubiquitination. 293T cells were mock-transfected or cotransfected with GFP-IN and HA-Ubwt, HA-UbK48R, or HA-UbK63R for 48 h, as indicated. The ubiquitination levels of IN and IN-associated proteins were checked by IP with anti-GFP antibody and anti-HA antibody in a WB ( middle panel ). The same membrane was reprobed with anti-GFP antibody to detect GFP-IN expression in each sample ( top panel ). About 5% of the cells prior to co-IP were lysed in 0.5% Nonidet P-40, and the protein contents were subjected to WB to detect total HA-Ub levels in the cells using anti-HA antibody ( bottom panel ). B , Ku70 protects IN from degradation by targeting the cellular ubiquitin-proteasome pathway and reducing ubiquitin binding to IN. 293T cells were mock-transfected ( lane 1 ) or cotransfected with GFP-IN, HA-Ubwt and T7 vector, or T7-Ku70wt and T7-Ku70(1–430) ( lanes 2–4 ). The co-IP assay was done at 48 h post-transfection using anti-GFP antibody to pull down IN and its associated proteins and using immunoblotting with anti-HA antibody to determine the ubiquitination level of IN and its associated proteins ( second panel ). The same membrane was reprobed with anti-GFP antibody to examine GFP-IN expression ( first panel ). Simultaneously, equal amounts of total cellular proteins (about 5% of the total cell lysates) were resolved on a SDS-PAGE gel and immunoblotted with anti-HA and anti-T7 antibodies to determine the expression levels of the transfected protein expressors ( third and fourth panels ). β-Actin was used as a loading control ( bottom panel ). C , reduction of ubiquitin level by Ku70 is independent of the Lys 48 - and Lys 63 -linked polyubiquitination proteasomal pathway. 293T cells were transfected with HA-Ubwt/mut with T7-Ku70 or T7 vector for 48 h. Cells were lysed and analyzed for HA-Ub expression using anti-HA antibody in a WB. On the same membrane, β-actin was used as a protein-loading control. D , endogenous ubiquitin levels were increased in Ku70-down-regulated cells. C8166 T cells were transduced with empty vector or lentiviral vector expressing an shRNA against human Ku70 and selected with 1 μg/ml puromycin. After 1 week of selection, equal amounts of control or stable Ku70-KD cell lines were collected and lysed. The expression levels of ubiquitin, Ku70, and β-actin were assessed by WB using specific antibodies.

    Article Snippet: To examine the IN/Ku70 interaction in HIV-1-infected cells, HIV-1 (HxBru or HxBru-IN-HA)-infected C8166 T cells were lysed with 0.25% Nonidet P-40 and immunoprecipitated with anti-HA antibody followed by WB with anti-Ku70 antibody to detect IN-bound Ku70.

    Techniques: Blocking Assay, Transfection, Western Blot, Expressing, Co-Immunoprecipitation Assay, Binding Assay, Plasmid Preparation, SDS Page, Transduction, shRNA, Selection

    Nuclease and salt resistance of particles assembled in vitro and of authentic, immature particles. Particles assembled in buffer B ( A ), buffer B plus 5% rabbit reticulocyte lysate ( B ), or buffer B plus 2 μM IP5 ( C ), were treated with RNase A (lanes 2) or NaCl (lanes 3). Gag proteins in particles pelleted after treatment were examined by SDS/PAGE and Coomassie blue staining. We estimate that > 90% of the Gag protein was solubilized in A (lanes 2 and 3), whereas > 90% remained pelletable in B and C (lanes 2 and 3). ( D ) Immature MoMuLV and HIV-1 virions produced in mammalian cells were analyzed separately (lanes 1 and 2, respectively) or were mixed together (lanes 3–9) and treated with RNase A (lanes 6 and 7) or NaCl (lanes 8 and 9). They were also digested with HIV-1 PR to confirm that the lipid envelope was removed by the detergent (lane 3), or sedimented without RNase or NaCl treatment to confirm that the particles are stable in buffer B (lanes 4 and 5). Gag proteins in the samples in D were detected by immunoblotting with antibodies against the CA proteins of both HIV-1 and MoMuLV. We estimate that > 90% of the HIV-1 Gag protein was still pelletable after NaCl or RNase treatment. P, pellet; S, supernatant.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Modulation of HIV-like particle assembly in vitro by inositol phosphates

    doi: 10.1073/pnas.191224698

    Figure Lengend Snippet: Nuclease and salt resistance of particles assembled in vitro and of authentic, immature particles. Particles assembled in buffer B ( A ), buffer B plus 5% rabbit reticulocyte lysate ( B ), or buffer B plus 2 μM IP5 ( C ), were treated with RNase A (lanes 2) or NaCl (lanes 3). Gag proteins in particles pelleted after treatment were examined by SDS/PAGE and Coomassie blue staining. We estimate that > 90% of the Gag protein was solubilized in A (lanes 2 and 3), whereas > 90% remained pelletable in B and C (lanes 2 and 3). ( D ) Immature MoMuLV and HIV-1 virions produced in mammalian cells were analyzed separately (lanes 1 and 2, respectively) or were mixed together (lanes 3–9) and treated with RNase A (lanes 6 and 7) or NaCl (lanes 8 and 9). They were also digested with HIV-1 PR to confirm that the lipid envelope was removed by the detergent (lane 3), or sedimented without RNase or NaCl treatment to confirm that the particles are stable in buffer B (lanes 4 and 5). Gag proteins in the samples in D were detected by immunoblotting with antibodies against the CA proteins of both HIV-1 and MoMuLV. We estimate that > 90% of the HIV-1 Gag protein was still pelletable after NaCl or RNase treatment. P, pellet; S, supernatant.

    Article Snippet: Particles were assembled in 100 μl of buffer B (buffer A + 1% Nonidet P-40; Roche Molecular Biochemicals).

    Techniques: In Vitro, SDS Page, Staining, Produced

    A. AEGFR-immunoprecipitation from MDA-MB-231 cell extracts followed by western blotting shows that B6H12 treatment for 15 min disrupts the association between EGFR and CD47 and inhibits EGFR-Y 1068 phosphorylation. B . CD47-immunoprecipitation showed that a fraction of EGFR co-immunoprecipitates with EGFR. B6H12 treatment for 15 min reduced interaction between CD47 and EGFR in MDA-MB-231 cells. ( C .- D .) MDA-MB-231 cells were pretreated with B6H12 for 15 minutes followed by EGF for 5 minutes, and IP-western blotting was performed using phospho-EGFR antibody. D . Quantification of three experiments was analyzed using the t-test (*P

    Journal: Oncotarget

    Article Title: A function-blocking CD47 antibody suppresses stem cell and EGF signaling in triple-negative breast cancer

    doi: 10.18632/oncotarget.7100

    Figure Lengend Snippet: A. AEGFR-immunoprecipitation from MDA-MB-231 cell extracts followed by western blotting shows that B6H12 treatment for 15 min disrupts the association between EGFR and CD47 and inhibits EGFR-Y 1068 phosphorylation. B . CD47-immunoprecipitation showed that a fraction of EGFR co-immunoprecipitates with EGFR. B6H12 treatment for 15 min reduced interaction between CD47 and EGFR in MDA-MB-231 cells. ( C .- D .) MDA-MB-231 cells were pretreated with B6H12 for 15 minutes followed by EGF for 5 minutes, and IP-western blotting was performed using phospho-EGFR antibody. D . Quantification of three experiments was analyzed using the t-test (*P

    Article Snippet: Cell lysates were made using immunoprecipitation buffer (50 mM Tris-HCl, 150 mM NaCl, and 1% Nonidet P-40) along with 1× Complete Mini-protease inhibitor mixture (Roche Applied Science).

    Techniques: Immunoprecipitation, Multiple Displacement Amplification, Western Blot