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n m ube1  (SignalChem)


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    SignalChem n m ube1
    N M Ube1, supplied by SignalChem, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/n+m+ube1/UBA1+(UBE1)%2C+Active/pmc05818180-537-72-99
    Average 90 stars, based on 2 article reviews
    n m ube1 - by Bioz Stars, 2026-09
    90/100 stars

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    Praja1 may interact and ubiquitinate tau as a substrate. (A) Top panels: VN155‐Praja1 and VC155‐tau were solely transfected and confirmed its distribution within SH‐SY5Y cells. Bottom panels: VN155‐Praja1 and VC155‐tau co‐expressed in the SH‐SY5Y cells and Venus‐based bimolecular fluorescence complementation (BiFC) fluorescence was observed by fluorescence microscopy ( n = 3). Scale bar: 10 μm. Fluorescence was only observed upon co‐transfection indicating two proteins are in proximity. (B) FLAG‐Praja1 and tau co‐expressed in the SH‐SY5Y cells treated with MG132 for 6 h. Immunoprecipitation was performed with tau‐C antibody, and multi‐ubiquitin was detected by Western blotting showing increased ubiquitination level in Praja1‐dependent manner. Vertical line shows potential ubiquitinated tau ( n = 3). (C) Immunoprecipitated fraction using anti‐tau (JM) was analyzed by HA antibody in Neuro2a cells, resulting in Praja1 dependent increase in ubiquitination ( n = 3). (D) In vitro ubiquitination assay was performed for 1 h, 37 °C using <t>E1,</t> E2, His‐Praja1, His‐tau, Ubiquitin, and Mg‐ATP ( n = 3). (E) Immunostaining for FLAG‐Praja and tau in SH‐SY5Y cells transfected with both FLAG‐Praja1 and tau, treated with MG132 for 6 h. DAPI was applied for nuclear staining ( n = 3). Scale bar: 10 μm. Fluorescence intensity profiles along the indicated lines are plotted at the bottom. For statistical analyses, mean values were subjected to Student's t ‐test (n.s. P ≥ 0.10). Error bars indicate standard deviation. Error bars in the quantified immunofluorescence images were calculated using standard error.
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    Praja1 may interact and ubiquitinate tau as a substrate. (A) Top panels: VN155‐Praja1 and VC155‐tau were solely transfected and confirmed its distribution within SH‐SY5Y cells. Bottom panels: VN155‐Praja1 and VC155‐tau co‐expressed in the SH‐SY5Y cells and Venus‐based bimolecular fluorescence complementation (BiFC) fluorescence was observed by fluorescence microscopy ( n = 3). Scale bar: 10 μm. Fluorescence was only observed upon co‐transfection indicating two proteins are in proximity. (B) FLAG‐Praja1 and tau co‐expressed in the SH‐SY5Y cells treated with MG132 for 6 h. Immunoprecipitation was performed with tau‐C antibody, and multi‐ubiquitin was detected by Western blotting showing increased ubiquitination level in Praja1‐dependent manner. Vertical line shows potential ubiquitinated tau ( n = 3). (C) Immunoprecipitated fraction using anti‐tau (JM) was analyzed by HA antibody in Neuro2a cells, resulting in Praja1 dependent increase in ubiquitination ( n = 3). (D) In vitro ubiquitination assay was performed for 1 h, 37 °C using <t>E1,</t> E2, His‐Praja1, His‐tau, Ubiquitin, and Mg‐ATP ( n = 3). (E) Immunostaining for FLAG‐Praja and tau in SH‐SY5Y cells transfected with both FLAG‐Praja1 and tau, treated with MG132 for 6 h. DAPI was applied for nuclear staining ( n = 3). Scale bar: 10 μm. Fluorescence intensity profiles along the indicated lines are plotted at the bottom. For statistical analyses, mean values were subjected to Student's t ‐test (n.s. P ≥ 0.10). Error bars indicate standard deviation. Error bars in the quantified immunofluorescence images were calculated using standard error.
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    Praja1 may interact and ubiquitinate tau as a substrate. (A) Top panels: VN155‐Praja1 and VC155‐tau were solely transfected and confirmed its distribution within SH‐SY5Y cells. Bottom panels: VN155‐Praja1 and VC155‐tau co‐expressed in the SH‐SY5Y cells and Venus‐based bimolecular fluorescence complementation (BiFC) fluorescence was observed by fluorescence microscopy ( n = 3). Scale bar: 10 μm. Fluorescence was only observed upon co‐transfection indicating two proteins are in proximity. (B) FLAG‐Praja1 and tau co‐expressed in the SH‐SY5Y cells treated with MG132 for 6 h. Immunoprecipitation was performed with tau‐C antibody, and multi‐ubiquitin was detected by Western blotting showing increased ubiquitination level in Praja1‐dependent manner. Vertical line shows potential ubiquitinated tau ( n = 3). (C) Immunoprecipitated fraction using anti‐tau (JM) was analyzed by HA antibody in Neuro2a cells, resulting in Praja1 dependent increase in ubiquitination ( n = 3). (D) In vitro ubiquitination assay was performed for 1 h, 37 °C using <t>E1,</t> E2, His‐Praja1, His‐tau, Ubiquitin, and Mg‐ATP ( n = 3). (E) Immunostaining for FLAG‐Praja and tau in SH‐SY5Y cells transfected with both FLAG‐Praja1 and tau, treated with MG132 for 6 h. DAPI was applied for nuclear staining ( n = 3). Scale bar: 10 μm. Fluorescence intensity profiles along the indicated lines are plotted at the bottom. For statistical analyses, mean values were subjected to Student's t ‐test (n.s. P ≥ 0.10). Error bars indicate standard deviation. Error bars in the quantified immunofluorescence images were calculated using standard error.
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    Praja1 may interact and ubiquitinate tau as a substrate. (A) Top panels: VN155‐Praja1 and VC155‐tau were solely transfected and confirmed its distribution within SH‐SY5Y cells. Bottom panels: VN155‐Praja1 and VC155‐tau co‐expressed in the SH‐SY5Y cells and Venus‐based bimolecular fluorescence complementation (BiFC) fluorescence was observed by fluorescence microscopy ( n = 3). Scale bar: 10 μm. Fluorescence was only observed upon co‐transfection indicating two proteins are in proximity. (B) FLAG‐Praja1 and tau co‐expressed in the SH‐SY5Y cells treated with MG132 for 6 h. Immunoprecipitation was performed with tau‐C antibody, and multi‐ubiquitin was detected by Western blotting showing increased ubiquitination level in Praja1‐dependent manner. Vertical line shows potential ubiquitinated tau ( n = 3). (C) Immunoprecipitated fraction using anti‐tau (JM) was analyzed by HA antibody in Neuro2a cells, resulting in Praja1 dependent increase in ubiquitination ( n = 3). (D) In vitro ubiquitination assay was performed for 1 h, 37 °C using <t>E1,</t> E2, His‐Praja1, His‐tau, Ubiquitin, and Mg‐ATP ( n = 3). (E) Immunostaining for FLAG‐Praja and tau in SH‐SY5Y cells transfected with both FLAG‐Praja1 and tau, treated with MG132 for 6 h. DAPI was applied for nuclear staining ( n = 3). Scale bar: 10 μm. Fluorescence intensity profiles along the indicated lines are plotted at the bottom. For statistical analyses, mean values were subjected to Student's t ‐test (n.s. P ≥ 0.10). Error bars indicate standard deviation. Error bars in the quantified immunofluorescence images were calculated using standard error.
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    Praja1 may interact and ubiquitinate tau as a substrate. (A) Top panels: VN155‐Praja1 and VC155‐tau were solely transfected and confirmed its distribution within SH‐SY5Y cells. Bottom panels: VN155‐Praja1 and VC155‐tau co‐expressed in the SH‐SY5Y cells and Venus‐based bimolecular fluorescence complementation (BiFC) fluorescence was observed by fluorescence microscopy ( n = 3). Scale bar: 10 μm. Fluorescence was only observed upon co‐transfection indicating two proteins are in proximity. (B) FLAG‐Praja1 and tau co‐expressed in the SH‐SY5Y cells treated with MG132 for 6 h. Immunoprecipitation was performed with tau‐C antibody, and multi‐ubiquitin was detected by Western blotting showing increased ubiquitination level in Praja1‐dependent manner. Vertical line shows potential ubiquitinated tau ( n = 3). (C) Immunoprecipitated fraction using anti‐tau (JM) was analyzed by HA antibody in Neuro2a cells, resulting in Praja1 dependent increase in ubiquitination ( n = 3). (D) In vitro ubiquitination assay was performed for 1 h, 37 °C using <t>E1,</t> E2, His‐Praja1, His‐tau, Ubiquitin, and Mg‐ATP ( n = 3). (E) Immunostaining for FLAG‐Praja and tau in SH‐SY5Y cells transfected with both FLAG‐Praja1 and tau, treated with MG132 for 6 h. DAPI was applied for nuclear staining ( n = 3). Scale bar: 10 μm. Fluorescence intensity profiles along the indicated lines are plotted at the bottom. For statistical analyses, mean values were subjected to Student's t ‐test (n.s. P ≥ 0.10). Error bars indicate standard deviation. Error bars in the quantified immunofluorescence images were calculated using standard error.
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    Praja1 may interact and ubiquitinate tau as a substrate. (A) Top panels: VN155‐Praja1 and VC155‐tau were solely transfected and confirmed its distribution within SH‐SY5Y cells. Bottom panels: VN155‐Praja1 and VC155‐tau co‐expressed in the SH‐SY5Y cells and Venus‐based bimolecular fluorescence complementation (BiFC) fluorescence was observed by fluorescence microscopy ( n = 3). Scale bar: 10 μm. Fluorescence was only observed upon co‐transfection indicating two proteins are in proximity. (B) FLAG‐Praja1 and tau co‐expressed in the SH‐SY5Y cells treated with MG132 for 6 h. Immunoprecipitation was performed with tau‐C antibody, and multi‐ubiquitin was detected by Western blotting showing increased ubiquitination level in Praja1‐dependent manner. Vertical line shows potential ubiquitinated tau ( n = 3). (C) Immunoprecipitated fraction using anti‐tau (JM) was analyzed by HA antibody in Neuro2a cells, resulting in Praja1 dependent increase in ubiquitination ( n = 3). (D) In vitro ubiquitination assay was performed for 1 h, 37 °C using <t>E1,</t> E2, His‐Praja1, His‐tau, Ubiquitin, and Mg‐ATP ( n = 3). (E) Immunostaining for FLAG‐Praja and tau in SH‐SY5Y cells transfected with both FLAG‐Praja1 and tau, treated with MG132 for 6 h. DAPI was applied for nuclear staining ( n = 3). Scale bar: 10 μm. Fluorescence intensity profiles along the indicated lines are plotted at the bottom. For statistical analyses, mean values were subjected to Student's t ‐test (n.s. P ≥ 0.10). Error bars indicate standard deviation. Error bars in the quantified immunofluorescence images were calculated using standard error.
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    Image Search Results


    Praja1 may interact and ubiquitinate tau as a substrate. (A) Top panels: VN155‐Praja1 and VC155‐tau were solely transfected and confirmed its distribution within SH‐SY5Y cells. Bottom panels: VN155‐Praja1 and VC155‐tau co‐expressed in the SH‐SY5Y cells and Venus‐based bimolecular fluorescence complementation (BiFC) fluorescence was observed by fluorescence microscopy ( n = 3). Scale bar: 10 μm. Fluorescence was only observed upon co‐transfection indicating two proteins are in proximity. (B) FLAG‐Praja1 and tau co‐expressed in the SH‐SY5Y cells treated with MG132 for 6 h. Immunoprecipitation was performed with tau‐C antibody, and multi‐ubiquitin was detected by Western blotting showing increased ubiquitination level in Praja1‐dependent manner. Vertical line shows potential ubiquitinated tau ( n = 3). (C) Immunoprecipitated fraction using anti‐tau (JM) was analyzed by HA antibody in Neuro2a cells, resulting in Praja1 dependent increase in ubiquitination ( n = 3). (D) In vitro ubiquitination assay was performed for 1 h, 37 °C using E1, E2, His‐Praja1, His‐tau, Ubiquitin, and Mg‐ATP ( n = 3). (E) Immunostaining for FLAG‐Praja and tau in SH‐SY5Y cells transfected with both FLAG‐Praja1 and tau, treated with MG132 for 6 h. DAPI was applied for nuclear staining ( n = 3). Scale bar: 10 μm. Fluorescence intensity profiles along the indicated lines are plotted at the bottom. For statistical analyses, mean values were subjected to Student's t ‐test (n.s. P ≥ 0.10). Error bars indicate standard deviation. Error bars in the quantified immunofluorescence images were calculated using standard error.

    Journal: The Febs Journal

    Article Title: E3 ligase Praja1 mediates ubiquitination and degradation of microtubule‐associated protein tau

    doi: 10.1111/febs.70303

    Figure Lengend Snippet: Praja1 may interact and ubiquitinate tau as a substrate. (A) Top panels: VN155‐Praja1 and VC155‐tau were solely transfected and confirmed its distribution within SH‐SY5Y cells. Bottom panels: VN155‐Praja1 and VC155‐tau co‐expressed in the SH‐SY5Y cells and Venus‐based bimolecular fluorescence complementation (BiFC) fluorescence was observed by fluorescence microscopy ( n = 3). Scale bar: 10 μm. Fluorescence was only observed upon co‐transfection indicating two proteins are in proximity. (B) FLAG‐Praja1 and tau co‐expressed in the SH‐SY5Y cells treated with MG132 for 6 h. Immunoprecipitation was performed with tau‐C antibody, and multi‐ubiquitin was detected by Western blotting showing increased ubiquitination level in Praja1‐dependent manner. Vertical line shows potential ubiquitinated tau ( n = 3). (C) Immunoprecipitated fraction using anti‐tau (JM) was analyzed by HA antibody in Neuro2a cells, resulting in Praja1 dependent increase in ubiquitination ( n = 3). (D) In vitro ubiquitination assay was performed for 1 h, 37 °C using E1, E2, His‐Praja1, His‐tau, Ubiquitin, and Mg‐ATP ( n = 3). (E) Immunostaining for FLAG‐Praja and tau in SH‐SY5Y cells transfected with both FLAG‐Praja1 and tau, treated with MG132 for 6 h. DAPI was applied for nuclear staining ( n = 3). Scale bar: 10 μm. Fluorescence intensity profiles along the indicated lines are plotted at the bottom. For statistical analyses, mean values were subjected to Student's t ‐test (n.s. P ≥ 0.10). Error bars indicate standard deviation. Error bars in the quantified immunofluorescence images were calculated using standard error.

    Article Snippet: For this purpose, 100 n m E1 (UBE1; #E‐305‐025, R&D systems), 1 μ m E2 (UBE2D3; #E2‐627‐100, R&D systems), 2 μ m His‐Praja1, 3 μ m His‐tau, 100 μ m ubiquitin (#U‐100H‐10 M, R&D systems), and 10 m m Mg‐ATP (#B‐20, R&D systems) were added to a total volume of 10 μL in phosphate buffer with 1 m m DTT.

    Techniques: Transfection, Fluorescence, Microscopy, Cotransfection, Immunoprecipitation, Ubiquitin Proteomics, Western Blot, In Vitro, Immunostaining, Staining, Standard Deviation, Immunofluorescence