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human usp10  (Santa Cruz Biotechnology)


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    Structured Review

    Santa Cruz Biotechnology human usp10
    (A) Schematic representation of the known domains in the SIRT6 protein. The green bar denotes the nuclear localization signal (NLS), orange lines indicate the positions of centenarian SIRT6 mutations, and the yellow bar marks the C-terminal region required for <t>USP10</t> binding. (B) SIRT6 protein levels in cytoplasmic and nuclear fractions of WT and CENT hMSCs. (C) Volcano plot showing differentially interacting proteins between WT SIRT6 and CentSIRT6 in hMSCs, identified by endogenous SIRT6 IP-MS. Protein abundances were normalized to SIRT6 levels in each pull-down sample. (D) Endogenous SIRT6 was immunoprecipitated from WT and CENT hMSC lysates using anti-SIRT6 antibody (D8D12). IP samples and input lysates were analyzed by western blotting with antibodies against SIRT6 (2G1H1) and Vimentin (VIM). Input represents whole-cell lysate prior to immunoprecipitation. (E) Protein levels of Vimentin and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting Vimentin. Protein levels were normalized to β-Actin. (F) Protein levels of Flag-VIM and SIRT6 in WT and CENT hMSCs transduced with lentiviruses expressing Flag or Flag-VIM. Protein levels were normalized to β-Actin. (G) Predicted interaction between the VIM IDR and the C-terminal IDR of SIRT6 using FINCHES. The right panel showing the effects of different SIRT6 mutations on these predicted interactions.
    Human Usp10, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Rare centenarian SIRT6 variants elevate SIRT6 protein levels and resist cellular senescence"

    Article Title: Rare centenarian SIRT6 variants elevate SIRT6 protein levels and resist cellular senescence

    Journal: bioRxiv

    doi: 10.1101/2025.09.29.679208

    (A) Schematic representation of the known domains in the SIRT6 protein. The green bar denotes the nuclear localization signal (NLS), orange lines indicate the positions of centenarian SIRT6 mutations, and the yellow bar marks the C-terminal region required for USP10 binding. (B) SIRT6 protein levels in cytoplasmic and nuclear fractions of WT and CENT hMSCs. (C) Volcano plot showing differentially interacting proteins between WT SIRT6 and CentSIRT6 in hMSCs, identified by endogenous SIRT6 IP-MS. Protein abundances were normalized to SIRT6 levels in each pull-down sample. (D) Endogenous SIRT6 was immunoprecipitated from WT and CENT hMSC lysates using anti-SIRT6 antibody (D8D12). IP samples and input lysates were analyzed by western blotting with antibodies against SIRT6 (2G1H1) and Vimentin (VIM). Input represents whole-cell lysate prior to immunoprecipitation. (E) Protein levels of Vimentin and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting Vimentin. Protein levels were normalized to β-Actin. (F) Protein levels of Flag-VIM and SIRT6 in WT and CENT hMSCs transduced with lentiviruses expressing Flag or Flag-VIM. Protein levels were normalized to β-Actin. (G) Predicted interaction between the VIM IDR and the C-terminal IDR of SIRT6 using FINCHES. The right panel showing the effects of different SIRT6 mutations on these predicted interactions.
    Figure Legend Snippet: (A) Schematic representation of the known domains in the SIRT6 protein. The green bar denotes the nuclear localization signal (NLS), orange lines indicate the positions of centenarian SIRT6 mutations, and the yellow bar marks the C-terminal region required for USP10 binding. (B) SIRT6 protein levels in cytoplasmic and nuclear fractions of WT and CENT hMSCs. (C) Volcano plot showing differentially interacting proteins between WT SIRT6 and CentSIRT6 in hMSCs, identified by endogenous SIRT6 IP-MS. Protein abundances were normalized to SIRT6 levels in each pull-down sample. (D) Endogenous SIRT6 was immunoprecipitated from WT and CENT hMSC lysates using anti-SIRT6 antibody (D8D12). IP samples and input lysates were analyzed by western blotting with antibodies against SIRT6 (2G1H1) and Vimentin (VIM). Input represents whole-cell lysate prior to immunoprecipitation. (E) Protein levels of Vimentin and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting Vimentin. Protein levels were normalized to β-Actin. (F) Protein levels of Flag-VIM and SIRT6 in WT and CENT hMSCs transduced with lentiviruses expressing Flag or Flag-VIM. Protein levels were normalized to β-Actin. (G) Predicted interaction between the VIM IDR and the C-terminal IDR of SIRT6 using FINCHES. The right panel showing the effects of different SIRT6 mutations on these predicted interactions.

    Techniques Used: Binding Assay, Protein-Protein interactions, Immunoprecipitation, Western Blot, Transfection, Transduction, Expressing

    (A) Protein levels of USP10 and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting USP10. (B) AlphaFold-predicted structural confidence for SIRT6 and VIM. Low confidence scores correspond to predicted intrinsic disorder regions (IDRs).
    Figure Legend Snippet: (A) Protein levels of USP10 and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting USP10. (B) AlphaFold-predicted structural confidence for SIRT6 and VIM. Low confidence scores correspond to predicted intrinsic disorder regions (IDRs).

    Techniques Used: Transfection

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    Article Title: LPS promotes HBO1 stability via USP25 to modulate inflammatory gene transcription in THP-1 cells
    Article Snippet: USP10 , 1:250 , sc-365828 , G0616 , 67–95 (h) , Santa Cruz.



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    (A) Schematic representation of the known domains in the SIRT6 protein. The green bar denotes the nuclear localization signal (NLS), orange lines indicate the positions of centenarian SIRT6 mutations, and the yellow bar marks the C-terminal region required for <t>USP10</t> binding. (B) SIRT6 protein levels in cytoplasmic and nuclear fractions of WT and CENT hMSCs. (C) Volcano plot showing differentially interacting proteins between WT SIRT6 and CentSIRT6 in hMSCs, identified by endogenous SIRT6 IP-MS. Protein abundances were normalized to SIRT6 levels in each pull-down sample. (D) Endogenous SIRT6 was immunoprecipitated from WT and CENT hMSC lysates using anti-SIRT6 antibody (D8D12). IP samples and input lysates were analyzed by western blotting with antibodies against SIRT6 (2G1H1) and Vimentin (VIM). Input represents whole-cell lysate prior to immunoprecipitation. (E) Protein levels of Vimentin and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting Vimentin. Protein levels were normalized to β-Actin. (F) Protein levels of Flag-VIM and SIRT6 in WT and CENT hMSCs transduced with lentiviruses expressing Flag or Flag-VIM. Protein levels were normalized to β-Actin. (G) Predicted interaction between the VIM IDR and the C-terminal IDR of SIRT6 using FINCHES. The right panel showing the effects of different SIRT6 mutations on these predicted interactions.
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    (A) Schematic representation of the known domains in the SIRT6 protein. The green bar denotes the nuclear localization signal (NLS), orange lines indicate the positions of centenarian SIRT6 mutations, and the yellow bar marks the C-terminal region required for <t>USP10</t> binding. (B) SIRT6 protein levels in cytoplasmic and nuclear fractions of WT and CENT hMSCs. (C) Volcano plot showing differentially interacting proteins between WT SIRT6 and CentSIRT6 in hMSCs, identified by endogenous SIRT6 IP-MS. Protein abundances were normalized to SIRT6 levels in each pull-down sample. (D) Endogenous SIRT6 was immunoprecipitated from WT and CENT hMSC lysates using anti-SIRT6 antibody (D8D12). IP samples and input lysates were analyzed by western blotting with antibodies against SIRT6 (2G1H1) and Vimentin (VIM). Input represents whole-cell lysate prior to immunoprecipitation. (E) Protein levels of Vimentin and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting Vimentin. Protein levels were normalized to β-Actin. (F) Protein levels of Flag-VIM and SIRT6 in WT and CENT hMSCs transduced with lentiviruses expressing Flag or Flag-VIM. Protein levels were normalized to β-Actin. (G) Predicted interaction between the VIM IDR and the C-terminal IDR of SIRT6 using FINCHES. The right panel showing the effects of different SIRT6 mutations on these predicted interactions.
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    (A) Schematic representation of the known domains in the SIRT6 protein. The green bar denotes the nuclear localization signal (NLS), orange lines indicate the positions of centenarian SIRT6 mutations, and the yellow bar marks the C-terminal region required for <t>USP10</t> binding. (B) SIRT6 protein levels in cytoplasmic and nuclear fractions of WT and CENT hMSCs. (C) Volcano plot showing differentially interacting proteins between WT SIRT6 and CentSIRT6 in hMSCs, identified by endogenous SIRT6 IP-MS. Protein abundances were normalized to SIRT6 levels in each pull-down sample. (D) Endogenous SIRT6 was immunoprecipitated from WT and CENT hMSC lysates using anti-SIRT6 antibody (D8D12). IP samples and input lysates were analyzed by western blotting with antibodies against SIRT6 (2G1H1) and Vimentin (VIM). Input represents whole-cell lysate prior to immunoprecipitation. (E) Protein levels of Vimentin and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting Vimentin. Protein levels were normalized to β-Actin. (F) Protein levels of Flag-VIM and SIRT6 in WT and CENT hMSCs transduced with lentiviruses expressing Flag or Flag-VIM. Protein levels were normalized to β-Actin. (G) Predicted interaction between the VIM IDR and the C-terminal IDR of SIRT6 using FINCHES. The right panel showing the effects of different SIRT6 mutations on these predicted interactions.
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    (A) Schematic representation of the known domains in the SIRT6 protein. The green bar denotes the nuclear localization signal (NLS), orange lines indicate the positions of centenarian SIRT6 mutations, and the yellow bar marks the C-terminal region required for <t>USP10</t> binding. (B) SIRT6 protein levels in cytoplasmic and nuclear fractions of WT and CENT hMSCs. (C) Volcano plot showing differentially interacting proteins between WT SIRT6 and CentSIRT6 in hMSCs, identified by endogenous SIRT6 IP-MS. Protein abundances were normalized to SIRT6 levels in each pull-down sample. (D) Endogenous SIRT6 was immunoprecipitated from WT and CENT hMSC lysates using anti-SIRT6 antibody (D8D12). IP samples and input lysates were analyzed by western blotting with antibodies against SIRT6 (2G1H1) and Vimentin (VIM). Input represents whole-cell lysate prior to immunoprecipitation. (E) Protein levels of Vimentin and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting Vimentin. Protein levels were normalized to β-Actin. (F) Protein levels of Flag-VIM and SIRT6 in WT and CENT hMSCs transduced with lentiviruses expressing Flag or Flag-VIM. Protein levels were normalized to β-Actin. (G) Predicted interaction between the VIM IDR and the C-terminal IDR of SIRT6 using FINCHES. The right panel showing the effects of different SIRT6 mutations on these predicted interactions.
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    (A) Schematic representation of the known domains in the SIRT6 protein. The green bar denotes the nuclear localization signal (NLS), orange lines indicate the positions of centenarian SIRT6 mutations, and the yellow bar marks the C-terminal region required for <t>USP10</t> binding. (B) SIRT6 protein levels in cytoplasmic and nuclear fractions of WT and CENT hMSCs. (C) Volcano plot showing differentially interacting proteins between WT SIRT6 and CentSIRT6 in hMSCs, identified by endogenous SIRT6 IP-MS. Protein abundances were normalized to SIRT6 levels in each pull-down sample. (D) Endogenous SIRT6 was immunoprecipitated from WT and CENT hMSC lysates using anti-SIRT6 antibody (D8D12). IP samples and input lysates were analyzed by western blotting with antibodies against SIRT6 (2G1H1) and Vimentin (VIM). Input represents whole-cell lysate prior to immunoprecipitation. (E) Protein levels of Vimentin and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting Vimentin. Protein levels were normalized to β-Actin. (F) Protein levels of Flag-VIM and SIRT6 in WT and CENT hMSCs transduced with lentiviruses expressing Flag or Flag-VIM. Protein levels were normalized to β-Actin. (G) Predicted interaction between the VIM IDR and the C-terminal IDR of SIRT6 using FINCHES. The right panel showing the effects of different SIRT6 mutations on these predicted interactions.
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    Image Search Results


    (A) Schematic representation of the known domains in the SIRT6 protein. The green bar denotes the nuclear localization signal (NLS), orange lines indicate the positions of centenarian SIRT6 mutations, and the yellow bar marks the C-terminal region required for USP10 binding. (B) SIRT6 protein levels in cytoplasmic and nuclear fractions of WT and CENT hMSCs. (C) Volcano plot showing differentially interacting proteins between WT SIRT6 and CentSIRT6 in hMSCs, identified by endogenous SIRT6 IP-MS. Protein abundances were normalized to SIRT6 levels in each pull-down sample. (D) Endogenous SIRT6 was immunoprecipitated from WT and CENT hMSC lysates using anti-SIRT6 antibody (D8D12). IP samples and input lysates were analyzed by western blotting with antibodies against SIRT6 (2G1H1) and Vimentin (VIM). Input represents whole-cell lysate prior to immunoprecipitation. (E) Protein levels of Vimentin and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting Vimentin. Protein levels were normalized to β-Actin. (F) Protein levels of Flag-VIM and SIRT6 in WT and CENT hMSCs transduced with lentiviruses expressing Flag or Flag-VIM. Protein levels were normalized to β-Actin. (G) Predicted interaction between the VIM IDR and the C-terminal IDR of SIRT6 using FINCHES. The right panel showing the effects of different SIRT6 mutations on these predicted interactions.

    Journal: bioRxiv

    Article Title: Rare centenarian SIRT6 variants elevate SIRT6 protein levels and resist cellular senescence

    doi: 10.1101/2025.09.29.679208

    Figure Lengend Snippet: (A) Schematic representation of the known domains in the SIRT6 protein. The green bar denotes the nuclear localization signal (NLS), orange lines indicate the positions of centenarian SIRT6 mutations, and the yellow bar marks the C-terminal region required for USP10 binding. (B) SIRT6 protein levels in cytoplasmic and nuclear fractions of WT and CENT hMSCs. (C) Volcano plot showing differentially interacting proteins between WT SIRT6 and CentSIRT6 in hMSCs, identified by endogenous SIRT6 IP-MS. Protein abundances were normalized to SIRT6 levels in each pull-down sample. (D) Endogenous SIRT6 was immunoprecipitated from WT and CENT hMSC lysates using anti-SIRT6 antibody (D8D12). IP samples and input lysates were analyzed by western blotting with antibodies against SIRT6 (2G1H1) and Vimentin (VIM). Input represents whole-cell lysate prior to immunoprecipitation. (E) Protein levels of Vimentin and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting Vimentin. Protein levels were normalized to β-Actin. (F) Protein levels of Flag-VIM and SIRT6 in WT and CENT hMSCs transduced with lentiviruses expressing Flag or Flag-VIM. Protein levels were normalized to β-Actin. (G) Predicted interaction between the VIM IDR and the C-terminal IDR of SIRT6 using FINCHES. The right panel showing the effects of different SIRT6 mutations on these predicted interactions.

    Article Snippet: siRNAs targeting human USP10 (sc-365828) and Vimentin (sc-373717) were purchased from Santa Cruz Biotechnology. siRNAs were transfected into MSCs using Lipofectamine RNAiMAX Reagent (Thermo Fisher) according to the manufacturer’s instructions.

    Techniques: Binding Assay, Protein-Protein interactions, Immunoprecipitation, Western Blot, Transfection, Transduction, Expressing

    (A) Protein levels of USP10 and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting USP10. (B) AlphaFold-predicted structural confidence for SIRT6 and VIM. Low confidence scores correspond to predicted intrinsic disorder regions (IDRs).

    Journal: bioRxiv

    Article Title: Rare centenarian SIRT6 variants elevate SIRT6 protein levels and resist cellular senescence

    doi: 10.1101/2025.09.29.679208

    Figure Lengend Snippet: (A) Protein levels of USP10 and SIRT6 in WT and CENT hMSCs transfected with siRNAs targeting USP10. (B) AlphaFold-predicted structural confidence for SIRT6 and VIM. Low confidence scores correspond to predicted intrinsic disorder regions (IDRs).

    Article Snippet: siRNAs targeting human USP10 (sc-365828) and Vimentin (sc-373717) were purchased from Santa Cruz Biotechnology. siRNAs were transfected into MSCs using Lipofectamine RNAiMAX Reagent (Thermo Fisher) according to the manufacturer’s instructions.

    Techniques: Transfection