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ubiquitin antibody no. 3933  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc ubiquitin antibody no. 3933
    ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and <t>ubiquitin</t> (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.
    Ubiquitin Antibody No. 3933, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ubiquitin antibody no. 3933/product/Cell Signaling Technology Inc
    Average 90 stars, based on 1 article reviews
    ubiquitin antibody no. 3933 - by Bioz Stars, 2026-03
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    Images

    1) Product Images from "A haploinsufficiency restoration strategy corrects neurobehavioral deficits in Nf1 +/– mice"

    Article Title: A haploinsufficiency restoration strategy corrects neurobehavioral deficits in Nf1 +/– mice

    Journal: The Journal of Clinical Investigation

    doi: 10.1172/JCI188932

    ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and ubiquitin (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.
    Figure Legend Snippet: ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and ubiquitin (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.

    Techniques Used: Expressing, Transfection, Western Blot, Co-Immunoprecipitation Assay, Binding Assay, Activity Assay, Cotransfection, Negative Control, Purification, Isolation, Incubation, Ubiquitin Proteomics, Molecular Weight, Control



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    ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and <t>ubiquitin</t> (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.
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    ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and <t>ubiquitin</t> (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.
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    ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and <t>ubiquitin</t> (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.
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    ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and <t>ubiquitin</t> (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.
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    ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and <t>ubiquitin</t> (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.
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    ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and <t>ubiquitin</t> (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.
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    Cell Signaling Technology Inc antibody against ubiquitin cell signaling 3933
    ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and <t>ubiquitin</t> (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.
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    ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and ubiquitin (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.

    Journal: The Journal of Clinical Investigation

    Article Title: A haploinsufficiency restoration strategy corrects neurobehavioral deficits in Nf1 +/– mice

    doi: 10.1172/JCI188932

    Figure Lengend Snippet: ( A ) Schematic map of the neurofibromin (NF1) interaction domains used to test interactions with FBXW11. Full-length NF1 was divided into the 6 indicated domains and subcloned into GFP-expressing plasmids. Flag-tagged FBXW11 and the various GFP-tagged NF1 subdomains were transfected into HEK293T cells. Six hours prior to harvesting, the cells were treated with 15 μM MG-132. Anti-Flag IP followed by immunoblotting was used to detect GFP-tagged NF1 co-IP with FBXW11. Relative binding activity as determined by immunoblotting is indicated. Image created in BioRender. Angus, S. (2025) https://BioRender.com/n28p603 ( B ) HEK293T cells were treated as in A to confirm the specific interaction of FBXW11 with the domain 3 (D3) fragment of the NF1 peptide, which encompasses the GRD of NF1 isoform 1 (GRD1), but not GRD2. ( C ) A NanoBiT complementation assay was performed after cotransfection of HEK293T cells with LgBiT-FBXW11 and SmBiT-GRD1 or GRD2 fusion proteins. Forty-five hours after transfection, the interaction was detected by luminescence. The negative control (neg. cont.) refers to luminescence values obtained from wells containing cells with LgbiT-FBXW11 and SmBiT-empty. Vehicle or the proteasome inhibitor bortezomib (1 mM) was included to enhance the interaction due to GRD1 accumulation. * P < 0.05 and *** P < 0.001, by unpaired 2-tailed t test. Data indicate the mean ± SEM. Image created in BioRender. Angus, S. (2025) https://BioRender.com/e61l197 ( D ) The SCF complex (SKP1, CUL1, RBX1, and Flag-FBXW11) was purified after cotransfection and subsequent Flag-IP (and Flag-peptide elution) from HEK293T cell lysates. Isolated GFP-GRD1 was incubated at 37°C for 60 minutes in the presence of E1 (100 nM), E2 (2 mM), Mg-ATP (5 mM), and ubiquitin (Ub) in the presence (+) or absence (–) of SCF FBXW11 . Samples were then subjected to immunoblotting, and GRD1 ubiquitination was detected by GFP antibody and the smearing due to higher-molecular-weight species. ( E ) HEK293T cells were transfected with control or FBXW11 -targeting siRNAs for 72 hours. A TUBEs assay was performed using agarose-TUBE2 to pull down total ubiquitinated protein. Immunoblotting was used to detect ubiquitin and NF1.

    Article Snippet: The relative levels of ubiquitylated neurofibromin were determined by immunoblotting with neurofibromin antibody (ab238142, Abcam) or ubiquitin antibody (no. 3933, Cell Signaling Technology).

    Techniques: Expressing, Transfection, Western Blot, Co-Immunoprecipitation Assay, Binding Assay, Activity Assay, Cotransfection, Negative Control, Purification, Isolation, Incubation, Ubiquitin Proteomics, Molecular Weight, Control