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hdac7 recombinant protein  (Sino Biological)


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    Structured Review

    Sino Biological hdac7 recombinant protein
    Hdac7 Recombinant Protein, supplied by Sino Biological, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/hdac7+recombinant+protein/HDAC7%2C+Active/pm41444923-167-0-6
    Average 93 stars, based on 2 article reviews
    hdac7 recombinant protein - by Bioz Stars, 2026-10
    93/100 stars

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    Recombinant:

    Article Title: Histone deacetylase HDAC7 restricts CD8 + T cell tumor infiltration and limits immunotherapy sensitivity in bladder cancer: reversal by pinocembrin
    Article Snippet: To determine the binding affinity of HDAC7 with Pinocembrin, microscale thermophoresis (MST) was performed using Monolith NT.115 (NanoTemper Technologies GmbH, Munich, Germany) and standard capillaries. .. HDAC7 recombinant protein was obtained from SIGNALCHEM (cat. H89-31G), and Pinocembrin was obtained from the MedChemExpress (CAS: 205370-59−8). .. The HDAC7 recombinant protein was labeled with the fluorescent dye Red-NHS using NanoTemper’s labeling kit MO-L011 MonolithTM according to the manufacturer’s instructions.

    Article Title: Histone deacetylase HDAC7 restricts CD8 + T cell tumor infiltration and limits immunotherapy sensitivity in bladder cancer: reversal by pinocembrin.
    Article Snippet: To determine the binding affinity of HDAC7 with Pinocembrin, microscale thermophoresis (MST) was performed using Monolith NT.115 (NanoTemper Technologies GmbH, Munich, Germany) and standard capillaries. .. HDAC7 recombinant protein was obtained from SIGNALCHEM (cat. H89-31G), and Pinocembrin was obtained from the MedChemExpress (CAS: 205370-59−8). .. The HDAC7 recombinant protein was labeled with the fluorescent dye Red-NHS using NanoTemper’s labeling kit MO-L011 MonolithTM according to the manufacturer’s instructions.



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    Figure 4. <t>HDAC7</t> protein stability is dependent on SIK1 kinase activity. (A) Western blot for total and phosphorylated HDAC4, HDAC5, and HDAC7 in NRVMs treated with or without siRNA against Sik1 and with or without PE (100 μM, 24 hours). α-Tubulin was used as loading control (n = 5). (B) qRT-PCR expression for Hdac7 (n = 6). Bars denote mean ± SEM. (C and D) Western blot for total and phosphorylated HDAC4, HDAC5, and HDAC7 in NRVMs treated with or without HG-9-91-01 (1 μM) or YKL-05-099 (1 μM). α-Tubulin was used as loading control (n = 4). (E) Western blot for total and phosphorylated HDAC7 in WT and SIK1-KO sham/TAC LV cardiac tissue. Vinculin was used as loading control (n = 4). (F) In vitro kinase assay with recombinant HDAC7 and GST- tagged SIK1 plus YKL-05-099 (1 μM). SIK1 consensus sequence is shown below (representative Western blots, n = 3). (G) Western blot from NRVMs treated with YKL-05-099 (1 μM) and the proteasome inhibitor bortezomib (BZ) (5 nM, 16 hours) (representative Western blots, n = 3). All box plots show minimum, maximum, and median with 25th to 75th percentile range. ***P < 0.001, ****P < 0.0001, by 1-way ANOVA with Tukey’s multiple comparisons test.
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    Figure 4. <t>HDAC7</t> protein stability is dependent on SIK1 kinase activity. (A) Western blot for total and phosphorylated HDAC4, HDAC5, and HDAC7 in NRVMs treated with or without siRNA against Sik1 and with or without PE (100 μM, 24 hours). α-Tubulin was used as loading control (n = 5). (B) qRT-PCR expression for Hdac7 (n = 6). Bars denote mean ± SEM. (C and D) Western blot for total and phosphorylated HDAC4, HDAC5, and HDAC7 in NRVMs treated with or without HG-9-91-01 (1 μM) or YKL-05-099 (1 μM). α-Tubulin was used as loading control (n = 4). (E) Western blot for total and phosphorylated HDAC7 in WT and SIK1-KO sham/TAC LV cardiac tissue. Vinculin was used as loading control (n = 4). (F) In vitro kinase assay with recombinant HDAC7 and GST- tagged SIK1 plus YKL-05-099 (1 μM). SIK1 consensus sequence is shown below (representative Western blots, n = 3). (G) Western blot from NRVMs treated with YKL-05-099 (1 μM) and the proteasome inhibitor bortezomib (BZ) (5 nM, 16 hours) (representative Western blots, n = 3). All box plots show minimum, maximum, and median with 25th to 75th percentile range. ***P < 0.001, ****P < 0.0001, by 1-way ANOVA with Tukey’s multiple comparisons test.
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    Figure 4. <t>HDAC7</t> protein stability is dependent on SIK1 kinase activity. (A) Western blot for total and phosphorylated HDAC4, HDAC5, and HDAC7 in NRVMs treated with or without siRNA against Sik1 and with or without PE (100 μM, 24 hours). α-Tubulin was used as loading control (n = 5). (B) qRT-PCR expression for Hdac7 (n = 6). Bars denote mean ± SEM. (C and D) Western blot for total and phosphorylated HDAC4, HDAC5, and HDAC7 in NRVMs treated with or without HG-9-91-01 (1 μM) or YKL-05-099 (1 μM). α-Tubulin was used as loading control (n = 4). (E) Western blot for total and phosphorylated HDAC7 in WT and SIK1-KO sham/TAC LV cardiac tissue. Vinculin was used as loading control (n = 4). (F) In vitro kinase assay with recombinant HDAC7 and GST- tagged SIK1 plus YKL-05-099 (1 μM). SIK1 consensus sequence is shown below (representative Western blots, n = 3). (G) Western blot from NRVMs treated with YKL-05-099 (1 μM) and the proteasome inhibitor bortezomib (BZ) (5 nM, 16 hours) (representative Western blots, n = 3). All box plots show minimum, maximum, and median with 25th to 75th percentile range. ***P < 0.001, ****P < 0.0001, by 1-way ANOVA with Tukey’s multiple comparisons test.
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    Figure 4. HDAC7 protein stability is dependent on SIK1 kinase activity. (A) Western blot for total and phosphorylated HDAC4, HDAC5, and HDAC7 in NRVMs treated with or without siRNA against Sik1 and with or without PE (100 μM, 24 hours). α-Tubulin was used as loading control (n = 5). (B) qRT-PCR expression for Hdac7 (n = 6). Bars denote mean ± SEM. (C and D) Western blot for total and phosphorylated HDAC4, HDAC5, and HDAC7 in NRVMs treated with or without HG-9-91-01 (1 μM) or YKL-05-099 (1 μM). α-Tubulin was used as loading control (n = 4). (E) Western blot for total and phosphorylated HDAC7 in WT and SIK1-KO sham/TAC LV cardiac tissue. Vinculin was used as loading control (n = 4). (F) In vitro kinase assay with recombinant HDAC7 and GST- tagged SIK1 plus YKL-05-099 (1 μM). SIK1 consensus sequence is shown below (representative Western blots, n = 3). (G) Western blot from NRVMs treated with YKL-05-099 (1 μM) and the proteasome inhibitor bortezomib (BZ) (5 nM, 16 hours) (representative Western blots, n = 3). All box plots show minimum, maximum, and median with 25th to 75th percentile range. ***P < 0.001, ****P < 0.0001, by 1-way ANOVA with Tukey’s multiple comparisons test.

    Journal: Journal of Clinical Investigation

    Article Title: Salt-inducible kinase 1 maintains HDAC7 stability to promote pathologic cardiac remodeling

    doi: 10.1172/jci133753

    Figure Lengend Snippet: Figure 4. HDAC7 protein stability is dependent on SIK1 kinase activity. (A) Western blot for total and phosphorylated HDAC4, HDAC5, and HDAC7 in NRVMs treated with or without siRNA against Sik1 and with or without PE (100 μM, 24 hours). α-Tubulin was used as loading control (n = 5). (B) qRT-PCR expression for Hdac7 (n = 6). Bars denote mean ± SEM. (C and D) Western blot for total and phosphorylated HDAC4, HDAC5, and HDAC7 in NRVMs treated with or without HG-9-91-01 (1 μM) or YKL-05-099 (1 μM). α-Tubulin was used as loading control (n = 4). (E) Western blot for total and phosphorylated HDAC7 in WT and SIK1-KO sham/TAC LV cardiac tissue. Vinculin was used as loading control (n = 4). (F) In vitro kinase assay with recombinant HDAC7 and GST- tagged SIK1 plus YKL-05-099 (1 μM). SIK1 consensus sequence is shown below (representative Western blots, n = 3). (G) Western blot from NRVMs treated with YKL-05-099 (1 μM) and the proteasome inhibitor bortezomib (BZ) (5 nM, 16 hours) (representative Western blots, n = 3). All box plots show minimum, maximum, and median with 25th to 75th percentile range. ***P < 0.001, ****P < 0.0001, by 1-way ANOVA with Tukey’s multiple comparisons test.

    Article Snippet: Ten nanograms of recombinant SIK1 (Thermo Fisher Scientific) and 100 ng of recombinant HDAC7 (Origene) were incubated in a final volume of 40 μL containing 1× kinase buffer (CST) supplemented with 100 μM ATP.

    Techniques: Activity Assay, Western Blot, Control, Quantitative RT-PCR, Expressing, In Vitro, Kinase Assay, Recombinant, Sequencing

    Figure 5. Loss of HDAC7 protects against pathologic cardiac remodeling in vitro. (A) NRVMs treated with siRNA against Hdac7 and immunostained for α-actinin (green) and nuclei (blue). Scale bars: 40 μm. (B) Cell area of NRVMs (n = 108). Bars denote mean ± SD. (C) qRT-PCR expression for Nppa and Nppb (n = 6). (D) MEF2 dual luciferase reporter assay. Values were normalized to Renilla luciferase control (n = 6). (E) NRVMs infected with adenovirus harboring GFP-HDAC7 or GFP alone and immunostained for α-actinin (red) and nuclei (blue). Scale bars: 40 μm. (F) Cell area of NRVMs (n = 58–63). Bars denote mean ± SD. (G) qRT-PCR expression for canonical heart failure–associated genes (n = 6). Data are shown as means ± SEM unless noted. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001, by 1-way ANOVA with Tukey’s multiple comparisons test.

    Journal: Journal of Clinical Investigation

    Article Title: Salt-inducible kinase 1 maintains HDAC7 stability to promote pathologic cardiac remodeling

    doi: 10.1172/jci133753

    Figure Lengend Snippet: Figure 5. Loss of HDAC7 protects against pathologic cardiac remodeling in vitro. (A) NRVMs treated with siRNA against Hdac7 and immunostained for α-actinin (green) and nuclei (blue). Scale bars: 40 μm. (B) Cell area of NRVMs (n = 108). Bars denote mean ± SD. (C) qRT-PCR expression for Nppa and Nppb (n = 6). (D) MEF2 dual luciferase reporter assay. Values were normalized to Renilla luciferase control (n = 6). (E) NRVMs infected with adenovirus harboring GFP-HDAC7 or GFP alone and immunostained for α-actinin (red) and nuclei (blue). Scale bars: 40 μm. (F) Cell area of NRVMs (n = 58–63). Bars denote mean ± SD. (G) qRT-PCR expression for canonical heart failure–associated genes (n = 6). Data are shown as means ± SEM unless noted. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001, by 1-way ANOVA with Tukey’s multiple comparisons test.

    Article Snippet: Ten nanograms of recombinant SIK1 (Thermo Fisher Scientific) and 100 ng of recombinant HDAC7 (Origene) were incubated in a final volume of 40 μL containing 1× kinase buffer (CST) supplemented with 100 μM ATP.

    Techniques: In Vitro, Quantitative RT-PCR, Expressing, Luciferase, Reporter Assay, Control, Infection

    Figure 6. HDAC7 indirectly regulates c-Myc expression. qRT-PCR (n = 6) and Western blotting (n = 4) for c-Myc expression in NRVMs treated with siRNA against Hdac7 (A and B), Ad-HDAC7 (C and D), or YKL-05-099 (1 μM) (E and F). All box plots show minimum, maximum, and median with 25th to 75th percentile range. (G) Western blotting of cytoplasmic (C) and nuclear (N) fractions of NRVMs treated with 1 μM YKL-05-099 plus 100 μM PE. TATA box–binding protein (TBP) and GAPDH were used as nuclear and cytoplasmic markers, respectively (representative Western blots, n = 3). (H) NRVMs treated with adenovirus harboring GFP-HDAC7 or GFP alone, followed by transfection of siRNA probes against c-Myc or scramble control. Immunostained for α-actinin (red) and nuclei (blue). Scale bars: 40 μm. (I) Cell area of NRVMs (n = 100). Bars denote mean ± SD. (J) qRT-PCR expression for Nppa and Nppb (n = 6). Data are shown as means ± SEM unless noted. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001, by 1-way ANOVA with Tukey’s multiple compar- isons test.

    Journal: Journal of Clinical Investigation

    Article Title: Salt-inducible kinase 1 maintains HDAC7 stability to promote pathologic cardiac remodeling

    doi: 10.1172/jci133753

    Figure Lengend Snippet: Figure 6. HDAC7 indirectly regulates c-Myc expression. qRT-PCR (n = 6) and Western blotting (n = 4) for c-Myc expression in NRVMs treated with siRNA against Hdac7 (A and B), Ad-HDAC7 (C and D), or YKL-05-099 (1 μM) (E and F). All box plots show minimum, maximum, and median with 25th to 75th percentile range. (G) Western blotting of cytoplasmic (C) and nuclear (N) fractions of NRVMs treated with 1 μM YKL-05-099 plus 100 μM PE. TATA box–binding protein (TBP) and GAPDH were used as nuclear and cytoplasmic markers, respectively (representative Western blots, n = 3). (H) NRVMs treated with adenovirus harboring GFP-HDAC7 or GFP alone, followed by transfection of siRNA probes against c-Myc or scramble control. Immunostained for α-actinin (red) and nuclei (blue). Scale bars: 40 μm. (I) Cell area of NRVMs (n = 100). Bars denote mean ± SD. (J) qRT-PCR expression for Nppa and Nppb (n = 6). Data are shown as means ± SEM unless noted. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001, by 1-way ANOVA with Tukey’s multiple compar- isons test.

    Article Snippet: Ten nanograms of recombinant SIK1 (Thermo Fisher Scientific) and 100 ng of recombinant HDAC7 (Origene) were incubated in a final volume of 40 μL containing 1× kinase buffer (CST) supplemented with 100 μM ATP.

    Techniques: Expressing, Quantitative RT-PCR, Western Blot, Binding Assay, Transfection, Control

    Figure 7. Proposed working model. Our proposed working model implicates a prohypertrophic SIK1/HDAC7 signaling axis in cardiac myocytes and a departure from the canonical model of class IIa HDAC function.

    Journal: Journal of Clinical Investigation

    Article Title: Salt-inducible kinase 1 maintains HDAC7 stability to promote pathologic cardiac remodeling

    doi: 10.1172/jci133753

    Figure Lengend Snippet: Figure 7. Proposed working model. Our proposed working model implicates a prohypertrophic SIK1/HDAC7 signaling axis in cardiac myocytes and a departure from the canonical model of class IIa HDAC function.

    Article Snippet: Ten nanograms of recombinant SIK1 (Thermo Fisher Scientific) and 100 ng of recombinant HDAC7 (Origene) were incubated in a final volume of 40 μL containing 1× kinase buffer (CST) supplemented with 100 μM ATP.

    Techniques: