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recombinant human sirt1  (R&D Systems)


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    Structured Review

    R&D Systems recombinant human sirt1
    SOD3 acetylated with 1 mM sNHSAc and then deacetylated by <t>SIRT1</t> or SIRT3 was incubated with furin overnight at 37 °C. All samples shown in (A) are incubated with furin, acetylation blocks furin cleavage as seen by a change in electrophoretic mobility in SDS-PAGE, and SIRT3 restores this shift (AI), the uncropped blot is included in . SIRT3 has an observed MW of 33.5 kDa and can be seen as a band above cleaved SOD3. Anti-acetylated-lysine immunoblotting confirms acetylation and deacetylation of these samples (AII). The shift in SOD3 mass was also evaluated by intact mass spectrometry, integration of the deconvoluted spectra from 25700 to 27900 amu was performed and divided by the integration of 28075–28925 amu. This cleavage ratio for the AcSOD3 no-furin sample was subtracted from the cleavage ratio for each treatment and normalized to the SOD3 +furin sample. Percent cleavage is therefore relative to defining the SOD3 + furin cleavage ratio as 100 % or complete cleavage. SIRT1 restored 5.9 % of furin cleavage and SIRT3 restored 85.0 % (B).
    Recombinant Human Sirt1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/sirt1+protein/Recombinant+Human+Sirtuin+1%2FSIRT1+Protein%2C+CF/pmc12774472-51-0-7
    Average 93 stars, based on 5 article reviews
    recombinant human sirt1 - by Bioz Stars, 2026-10
    93/100 stars

    Images

    1) Product Images from "Deacetylation of SOD3 by sirtuins restores furin cleavage"

    Article Title: Deacetylation of SOD3 by sirtuins restores furin cleavage

    Journal: Redox biochemistry and chemistry

    doi: 10.1016/j.rbc.2025.100062

    SOD3 acetylated with 1 mM sNHSAc and then deacetylated by SIRT1 or SIRT3 was incubated with furin overnight at 37 °C. All samples shown in (A) are incubated with furin, acetylation blocks furin cleavage as seen by a change in electrophoretic mobility in SDS-PAGE, and SIRT3 restores this shift (AI), the uncropped blot is included in . SIRT3 has an observed MW of 33.5 kDa and can be seen as a band above cleaved SOD3. Anti-acetylated-lysine immunoblotting confirms acetylation and deacetylation of these samples (AII). The shift in SOD3 mass was also evaluated by intact mass spectrometry, integration of the deconvoluted spectra from 25700 to 27900 amu was performed and divided by the integration of 28075–28925 amu. This cleavage ratio for the AcSOD3 no-furin sample was subtracted from the cleavage ratio for each treatment and normalized to the SOD3 +furin sample. Percent cleavage is therefore relative to defining the SOD3 + furin cleavage ratio as 100 % or complete cleavage. SIRT1 restored 5.9 % of furin cleavage and SIRT3 restored 85.0 % (B).
    Figure Legend Snippet: SOD3 acetylated with 1 mM sNHSAc and then deacetylated by SIRT1 or SIRT3 was incubated with furin overnight at 37 °C. All samples shown in (A) are incubated with furin, acetylation blocks furin cleavage as seen by a change in electrophoretic mobility in SDS-PAGE, and SIRT3 restores this shift (AI), the uncropped blot is included in . SIRT3 has an observed MW of 33.5 kDa and can be seen as a band above cleaved SOD3. Anti-acetylated-lysine immunoblotting confirms acetylation and deacetylation of these samples (AII). The shift in SOD3 mass was also evaluated by intact mass spectrometry, integration of the deconvoluted spectra from 25700 to 27900 amu was performed and divided by the integration of 28075–28925 amu. This cleavage ratio for the AcSOD3 no-furin sample was subtracted from the cleavage ratio for each treatment and normalized to the SOD3 +furin sample. Percent cleavage is therefore relative to defining the SOD3 + furin cleavage ratio as 100 % or complete cleavage. SIRT1 restored 5.9 % of furin cleavage and SIRT3 restored 85.0 % (B).

    Techniques Used: Incubation, SDS Page, Western Blot, Mass Spectrometry

    Acetylated SOD3 was incubated with SIRT1 or SIRT3 and 2 mM NAD + for 30 min at 37 °C. Global deacetylation of SOD3 was evaluated by anti-acetylated-lysine immunoblotting (AI) and quantified by densitometry with normalization to total protein visualized with TCE labeling (AII). Data are expressed as mean with SD; a one-way ANOVA was performed on triplicates *p < 0.05, **p < 0.01. Site specific deacetylation was quantified by proteomics of trypsin digests in terms of fold change compared to acetylated SOD3 (B). ND indicates that acetylation at this site was not found in Ctrl SOD3.
    Figure Legend Snippet: Acetylated SOD3 was incubated with SIRT1 or SIRT3 and 2 mM NAD + for 30 min at 37 °C. Global deacetylation of SOD3 was evaluated by anti-acetylated-lysine immunoblotting (AI) and quantified by densitometry with normalization to total protein visualized with TCE labeling (AII). Data are expressed as mean with SD; a one-way ANOVA was performed on triplicates *p < 0.05, **p < 0.01. Site specific deacetylation was quantified by proteomics of trypsin digests in terms of fold change compared to acetylated SOD3 (B). ND indicates that acetylation at this site was not found in Ctrl SOD3.

    Techniques Used: Incubation, Western Blot, Labeling

    Related Articles

    Purification:

    Article Title: Acetylation of Mammalian ADA3 Is Required for Its Functional Roles in Histone Acetylation and Cell Proliferation
    Article Snippet: .. Briefly, 1 μg of bacterially purified GST or GST-ADA3 protein bound to beads was used as bait and incubated with 300 ng of baculovirally purified SIRT1 protein, purchased from R&D Systems (catalog no. 7714-DA). ..

    Article Title: Acetylation of Mammalian ADA3 Is Required for Its Functional Roles in Histone Acetylation and Cell Proliferation
    Article Snippet: .. Briefly 1 μg of bacterially 170 purified GST or GST-ADA3 proteins bound to beads were used as bait and incubated with 300 171 ng of baculovirally purified SIRT1 protein purchased from R&D Systems (Catalog#7714-DA). ..

    Incubation:

    Article Title: Acetylation of Mammalian ADA3 Is Required for Its Functional Roles in Histone Acetylation and Cell Proliferation
    Article Snippet: .. Briefly, 1 μg of bacterially purified GST or GST-ADA3 protein bound to beads was used as bait and incubated with 300 ng of baculovirally purified SIRT1 protein, purchased from R&D Systems (catalog no. 7714-DA). ..

    Article Title: Acetylation of Mammalian ADA3 Is Required for Its Functional Roles in Histone Acetylation and Cell Proliferation
    Article Snippet: .. Briefly 1 μg of bacterially 170 purified GST or GST-ADA3 proteins bound to beads were used as bait and incubated with 300 171 ng of baculovirally purified SIRT1 protein purchased from R&D Systems (Catalog#7714-DA). ..



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    Image Search Results


    SOD3 acetylated with 1 mM sNHSAc and then deacetylated by SIRT1 or SIRT3 was incubated with furin overnight at 37 °C. All samples shown in (A) are incubated with furin, acetylation blocks furin cleavage as seen by a change in electrophoretic mobility in SDS-PAGE, and SIRT3 restores this shift (AI), the uncropped blot is included in . SIRT3 has an observed MW of 33.5 kDa and can be seen as a band above cleaved SOD3. Anti-acetylated-lysine immunoblotting confirms acetylation and deacetylation of these samples (AII). The shift in SOD3 mass was also evaluated by intact mass spectrometry, integration of the deconvoluted spectra from 25700 to 27900 amu was performed and divided by the integration of 28075–28925 amu. This cleavage ratio for the AcSOD3 no-furin sample was subtracted from the cleavage ratio for each treatment and normalized to the SOD3 +furin sample. Percent cleavage is therefore relative to defining the SOD3 + furin cleavage ratio as 100 % or complete cleavage. SIRT1 restored 5.9 % of furin cleavage and SIRT3 restored 85.0 % (B).

    Journal: Redox biochemistry and chemistry

    Article Title: Deacetylation of SOD3 by sirtuins restores furin cleavage

    doi: 10.1016/j.rbc.2025.100062

    Figure Lengend Snippet: SOD3 acetylated with 1 mM sNHSAc and then deacetylated by SIRT1 or SIRT3 was incubated with furin overnight at 37 °C. All samples shown in (A) are incubated with furin, acetylation blocks furin cleavage as seen by a change in electrophoretic mobility in SDS-PAGE, and SIRT3 restores this shift (AI), the uncropped blot is included in . SIRT3 has an observed MW of 33.5 kDa and can be seen as a band above cleaved SOD3. Anti-acetylated-lysine immunoblotting confirms acetylation and deacetylation of these samples (AII). The shift in SOD3 mass was also evaluated by intact mass spectrometry, integration of the deconvoluted spectra from 25700 to 27900 amu was performed and divided by the integration of 28075–28925 amu. This cleavage ratio for the AcSOD3 no-furin sample was subtracted from the cleavage ratio for each treatment and normalized to the SOD3 +furin sample. Percent cleavage is therefore relative to defining the SOD3 + furin cleavage ratio as 100 % or complete cleavage. SIRT1 restored 5.9 % of furin cleavage and SIRT3 restored 85.0 % (B).

    Article Snippet: Cloning, expression, purification of the Human Sirtuin (SIRT1): The amino acid sequence of human encoding sirtuin protein (SIRT1) (Uniprot ID: Q96EB6 ) was synthesized from Twist Biosciences.

    Techniques: Incubation, SDS Page, Western Blot, Mass Spectrometry

    Acetylated SOD3 was incubated with SIRT1 or SIRT3 and 2 mM NAD + for 30 min at 37 °C. Global deacetylation of SOD3 was evaluated by anti-acetylated-lysine immunoblotting (AI) and quantified by densitometry with normalization to total protein visualized with TCE labeling (AII). Data are expressed as mean with SD; a one-way ANOVA was performed on triplicates *p < 0.05, **p < 0.01. Site specific deacetylation was quantified by proteomics of trypsin digests in terms of fold change compared to acetylated SOD3 (B). ND indicates that acetylation at this site was not found in Ctrl SOD3.

    Journal: Redox biochemistry and chemistry

    Article Title: Deacetylation of SOD3 by sirtuins restores furin cleavage

    doi: 10.1016/j.rbc.2025.100062

    Figure Lengend Snippet: Acetylated SOD3 was incubated with SIRT1 or SIRT3 and 2 mM NAD + for 30 min at 37 °C. Global deacetylation of SOD3 was evaluated by anti-acetylated-lysine immunoblotting (AI) and quantified by densitometry with normalization to total protein visualized with TCE labeling (AII). Data are expressed as mean with SD; a one-way ANOVA was performed on triplicates *p < 0.05, **p < 0.01. Site specific deacetylation was quantified by proteomics of trypsin digests in terms of fold change compared to acetylated SOD3 (B). ND indicates that acetylation at this site was not found in Ctrl SOD3.

    Article Snippet: Cloning, expression, purification of the Human Sirtuin (SIRT1): The amino acid sequence of human encoding sirtuin protein (SIRT1) (Uniprot ID: Q96EB6 ) was synthesized from Twist Biosciences.

    Techniques: Incubation, Western Blot, Labeling

    SOD3 acetylated with 1 mM sNHSAc and then deacetylated by SIRT1 or SIRT3 was incubated with furin overnight at 37 °C. All samples shown in (A) are incubated with furin, acetylation blocks furin cleavage as seen by a change in electrophoretic mobility in SDS-PAGE, and SIRT3 restores this shift (AI), the uncropped blot is included in . SIRT3 has an observed MW of 33.5 kDa and can be seen as a band above cleaved SOD3. Anti-acetylated-lysine immunoblotting confirms acetylation and deacetylation of these samples (AII). The shift in SOD3 mass was also evaluated by intact mass spectrometry, integration of the deconvoluted spectra from 25700 to 27900 amu was performed and divided by the integration of 28075–28925 amu. This cleavage ratio for the AcSOD3 no-furin sample was subtracted from the cleavage ratio for each treatment and normalized to the SOD3 +furin sample. Percent cleavage is therefore relative to defining the SOD3 + furin cleavage ratio as 100 % or complete cleavage. SIRT1 restored 5.9 % of furin cleavage and SIRT3 restored 85.0 % (B).

    Journal: Redox biochemistry and chemistry

    Article Title: Deacetylation of SOD3 by sirtuins restores furin cleavage

    doi: 10.1016/j.rbc.2025.100062

    Figure Lengend Snippet: SOD3 acetylated with 1 mM sNHSAc and then deacetylated by SIRT1 or SIRT3 was incubated with furin overnight at 37 °C. All samples shown in (A) are incubated with furin, acetylation blocks furin cleavage as seen by a change in electrophoretic mobility in SDS-PAGE, and SIRT3 restores this shift (AI), the uncropped blot is included in . SIRT3 has an observed MW of 33.5 kDa and can be seen as a band above cleaved SOD3. Anti-acetylated-lysine immunoblotting confirms acetylation and deacetylation of these samples (AII). The shift in SOD3 mass was also evaluated by intact mass spectrometry, integration of the deconvoluted spectra from 25700 to 27900 amu was performed and divided by the integration of 28075–28925 amu. This cleavage ratio for the AcSOD3 no-furin sample was subtracted from the cleavage ratio for each treatment and normalized to the SOD3 +furin sample. Percent cleavage is therefore relative to defining the SOD3 + furin cleavage ratio as 100 % or complete cleavage. SIRT1 restored 5.9 % of furin cleavage and SIRT3 restored 85.0 % (B).

    Article Snippet: Recombinant human SIRT1 (#7714-DA-050) was purchased from R&D Systems (Minneapolis, MN), or expressed in-house, and percent purity as >95 % was demonstrated by SDS-PAGE.

    Techniques: Incubation, SDS Page, Western Blot, Mass Spectrometry

    Acetylated SOD3 was incubated with SIRT1 or SIRT3 and 2 mM NAD + for 30 min at 37 °C. Global deacetylation of SOD3 was evaluated by anti-acetylated-lysine immunoblotting (AI) and quantified by densitometry with normalization to total protein visualized with TCE labeling (AII). Data are expressed as mean with SD; a one-way ANOVA was performed on triplicates *p < 0.05, **p < 0.01. Site specific deacetylation was quantified by proteomics of trypsin digests in terms of fold change compared to acetylated SOD3 (B). ND indicates that acetylation at this site was not found in Ctrl SOD3.

    Journal: Redox biochemistry and chemistry

    Article Title: Deacetylation of SOD3 by sirtuins restores furin cleavage

    doi: 10.1016/j.rbc.2025.100062

    Figure Lengend Snippet: Acetylated SOD3 was incubated with SIRT1 or SIRT3 and 2 mM NAD + for 30 min at 37 °C. Global deacetylation of SOD3 was evaluated by anti-acetylated-lysine immunoblotting (AI) and quantified by densitometry with normalization to total protein visualized with TCE labeling (AII). Data are expressed as mean with SD; a one-way ANOVA was performed on triplicates *p < 0.05, **p < 0.01. Site specific deacetylation was quantified by proteomics of trypsin digests in terms of fold change compared to acetylated SOD3 (B). ND indicates that acetylation at this site was not found in Ctrl SOD3.

    Article Snippet: Recombinant human SIRT1 (#7714-DA-050) was purchased from R&D Systems (Minneapolis, MN), or expressed in-house, and percent purity as >95 % was demonstrated by SDS-PAGE.

    Techniques: Incubation, Western Blot, Labeling