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rock2  (Bio-Techne corporation)


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    Bio-Techne corporation rock2
    Rock2, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/nb100-593/ROCK2+Antibody/pm37873881-67-22-26
    Average 91 stars, based on 2 article reviews
    rock2 - by Bioz Stars, 2026-10
    91/100 stars

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    Related Articles

    Blocking Assay:

    Article Title: The role of KDM4A-mediated histone methylation on temozolomide resistance in glioma cells through the HUWE1/ROCK2 axis.
    Article Snippet: .. After blocking, the membranes were incubated overnight at 4 C with primary antibodies against KDM4A (1:5000, ab191433, Abcam Inc., Cambridge, MA, USA), ROCK2 (1:1000, NB100-593, NOVUS, Bio-Techne China Co. Ltd., Beijing, China), HUWE1 (1:1000, ab70161, Abcam), and β-actin (1:1000, ab8227, Abcam). .. Following washing with TBST buffer, the membranes were probed with horseradish peroxidase (HRP)-conjugated secondary antibodies (1:2000, ab6721, Abcam) for 2 h. Immunoreactivity was visualized using an enhanced chemiluminescence kit (Millipore, Billerica, MA, USA), and gray value analysis was performed using Image J software (National Institutes of Health, Bethesda, MD, USA), with β-actin as the internal reference.

    Incubation:

    Article Title: The role of KDM4A-mediated histone methylation on temozolomide resistance in glioma cells through the HUWE1/ROCK2 axis.
    Article Snippet: .. After blocking, the membranes were incubated overnight at 4 C with primary antibodies against KDM4A (1:5000, ab191433, Abcam Inc., Cambridge, MA, USA), ROCK2 (1:1000, NB100-593, NOVUS, Bio-Techne China Co. Ltd., Beijing, China), HUWE1 (1:1000, ab70161, Abcam), and β-actin (1:1000, ab8227, Abcam). .. Following washing with TBST buffer, the membranes were probed with horseradish peroxidase (HRP)-conjugated secondary antibodies (1:2000, ab6721, Abcam) for 2 h. Immunoreactivity was visualized using an enhanced chemiluminescence kit (Millipore, Billerica, MA, USA), and gray value analysis was performed using Image J software (National Institutes of Health, Bethesda, MD, USA), with β-actin as the internal reference.



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    KDM4A regulation of <t>ROCK2</t> and HUWE1 expression through histone demethylation. (A) Enrichment of KDM4A, H3K9me3, and H3K36me3 on ROCK2 and HUWE1 promoters assessed using ChIP. (B) Transcriptional levels of ROCK2 and HUWE1 evaluated by qRT‐PCR. (C) Protein expressions of ROCK2 and HUWE1 analyzed by Western blot. Each experiment was independently repeated three times. Data in panels (A–C) were analyzed using two‐way ANOVA, followed by Sidak's multiple comparisons test, * p < 0.05; ** p < 0.01.
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    KDM4A regulation of <t>ROCK2</t> and HUWE1 expression through histone demethylation. (A) Enrichment of KDM4A, H3K9me3, and H3K36me3 on ROCK2 and HUWE1 promoters assessed using ChIP. (B) Transcriptional levels of ROCK2 and HUWE1 evaluated by qRT‐PCR. (C) Protein expressions of ROCK2 and HUWE1 analyzed by Western blot. Each experiment was independently repeated three times. Data in panels (A–C) were analyzed using two‐way ANOVA, followed by Sidak's multiple comparisons test, * p < 0.05; ** p < 0.01.
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    Image Search Results


    KDM4A regulation of ROCK2 and HUWE1 expression through histone demethylation. (A) Enrichment of KDM4A, H3K9me3, and H3K36me3 on ROCK2 and HUWE1 promoters assessed using ChIP. (B) Transcriptional levels of ROCK2 and HUWE1 evaluated by qRT‐PCR. (C) Protein expressions of ROCK2 and HUWE1 analyzed by Western blot. Each experiment was independently repeated three times. Data in panels (A–C) were analyzed using two‐way ANOVA, followed by Sidak's multiple comparisons test, * p < 0.05; ** p < 0.01.

    Journal: The Kaohsiung Journal of Medical Sciences

    Article Title: The role of KDM4A‐mediated histone methylation on temozolomide resistance in glioma cells through the HUWE1 / ROCK2 axis

    doi: 10.1002/kjm2.12768

    Figure Lengend Snippet: KDM4A regulation of ROCK2 and HUWE1 expression through histone demethylation. (A) Enrichment of KDM4A, H3K9me3, and H3K36me3 on ROCK2 and HUWE1 promoters assessed using ChIP. (B) Transcriptional levels of ROCK2 and HUWE1 evaluated by qRT‐PCR. (C) Protein expressions of ROCK2 and HUWE1 analyzed by Western blot. Each experiment was independently repeated three times. Data in panels (A–C) were analyzed using two‐way ANOVA, followed by Sidak's multiple comparisons test, * p < 0.05; ** p < 0.01.

    Article Snippet: The antibodies used included ROCK2 (1:1000, NB100‐593, NOVUS) and HUWE1 (1:1000, ab70161, Abcam).

    Techniques: Expressing, Quantitative RT-PCR, Western Blot

    HUWE1 binding to ROCK2 and promotion of its ubiquitination degradation. (A) Binding relationship between HUWE1 and ROCK2 assessed by co‐immunoprecipitation, with IgG serving as the isotype control. (B) ROCK2 ubiquitination level in U251MG and T98G cells evaluated by co‐immunoprecipitation and Western blot, with IgG serving as the isotype control. (C) ROCK2 ubiquitination level detected after adding MG132 (DMSO treatment as control) to different transfected cells, with IgG serving as the isotype control. Each experiment was independently repeated three times.

    Journal: The Kaohsiung Journal of Medical Sciences

    Article Title: The role of KDM4A‐mediated histone methylation on temozolomide resistance in glioma cells through the HUWE1 / ROCK2 axis

    doi: 10.1002/kjm2.12768

    Figure Lengend Snippet: HUWE1 binding to ROCK2 and promotion of its ubiquitination degradation. (A) Binding relationship between HUWE1 and ROCK2 assessed by co‐immunoprecipitation, with IgG serving as the isotype control. (B) ROCK2 ubiquitination level in U251MG and T98G cells evaluated by co‐immunoprecipitation and Western blot, with IgG serving as the isotype control. (C) ROCK2 ubiquitination level detected after adding MG132 (DMSO treatment as control) to different transfected cells, with IgG serving as the isotype control. Each experiment was independently repeated three times.

    Article Snippet: The antibodies used included ROCK2 (1:1000, NB100‐593, NOVUS) and HUWE1 (1:1000, ab70161, Abcam).

    Techniques: Binding Assay, Ubiquitin Proteomics, Immunoprecipitation, Control, Western Blot, Transfection

    Partial Reversal of KDM4A Inhibition's Effect on TMZ Resistance in Glioma Cells by HUWE1 Inhibition. Two siRNAs (si‐HUWE1‐1 and si‐HUWE1‐2) were transfected into T98G cells, with si‐NC serving as the control. (A) Transfection efficiency assessed by qRT‐PCR, with si‐HUWE1‐1 selected for combined experiments with si‐KDM4A‐1 due to better transfection efficiency. (B) Expressions of ROCK2 and HUWE1 evaluated by Western blot. (C) ROCK2 ubiquitination level assessed by co‐immunoprecipitation, with IgG serving as the isotype control. (D) Cell viability after 48 h of TMZ treatment measured by CCK‐8 assay and the calculated IC50 value. (E) Cell proliferation ability after treating T98G cells with TMZ concentration of 365 μM for 48 h, evaluated by the clone formation assay. Each experiment was independently repeated three times. Data in panels A/D (right)/E were analyzed using one‐way ANOVA, while data in panels B/D (left) were analyzed using two‐way ANOVA, followed by Tukey's multiple comparisons test; ** p < 0.01.

    Journal: The Kaohsiung Journal of Medical Sciences

    Article Title: The role of KDM4A‐mediated histone methylation on temozolomide resistance in glioma cells through the HUWE1 / ROCK2 axis

    doi: 10.1002/kjm2.12768

    Figure Lengend Snippet: Partial Reversal of KDM4A Inhibition's Effect on TMZ Resistance in Glioma Cells by HUWE1 Inhibition. Two siRNAs (si‐HUWE1‐1 and si‐HUWE1‐2) were transfected into T98G cells, with si‐NC serving as the control. (A) Transfection efficiency assessed by qRT‐PCR, with si‐HUWE1‐1 selected for combined experiments with si‐KDM4A‐1 due to better transfection efficiency. (B) Expressions of ROCK2 and HUWE1 evaluated by Western blot. (C) ROCK2 ubiquitination level assessed by co‐immunoprecipitation, with IgG serving as the isotype control. (D) Cell viability after 48 h of TMZ treatment measured by CCK‐8 assay and the calculated IC50 value. (E) Cell proliferation ability after treating T98G cells with TMZ concentration of 365 μM for 48 h, evaluated by the clone formation assay. Each experiment was independently repeated three times. Data in panels A/D (right)/E were analyzed using one‐way ANOVA, while data in panels B/D (left) were analyzed using two‐way ANOVA, followed by Tukey's multiple comparisons test; ** p < 0.01.

    Article Snippet: The antibodies used included ROCK2 (1:1000, NB100‐593, NOVUS) and HUWE1 (1:1000, ab70161, Abcam).

    Techniques: Inhibition, Transfection, Control, Quantitative RT-PCR, Western Blot, Ubiquitin Proteomics, Immunoprecipitation, CCK-8 Assay, Concentration Assay, Tube Formation Assay

    Partial reversal of KDM4A inhibition's effect on TMZ resistance in glioma cells by ROCK2 overexpression. ROCK2 overexpression vector (oe‐ROCK2) was transfected into T98G cells, with oe‐NC serving as the control. (A) Transfection efficiency assessed by qRT‐PCR, followed by combined experiments with si‐KDM4A‐1. (B) Expressions of ROCK2 and HUWE1 evaluated by Western blot. (C) Cell viability after 48 h of TMZ treatment measured by CCK‐8 assay and the calculated IC50 value. (D) Cell proliferation ability after treating T98G cells with TMZ concentration of 365 μM for 48 h, evaluated by the clone formation assay. Each experiment was independently repeated three times. Data in panel A were analyzed using a t ‐test. Data in panels C (right)/D were analyzed using one‐way ANOVA, while data in panels B/C (left) were analyzed using two‐way ANOVA, followed by Tukey's multiple comparisons test; ** p < 0.01.

    Journal: The Kaohsiung Journal of Medical Sciences

    Article Title: The role of KDM4A‐mediated histone methylation on temozolomide resistance in glioma cells through the HUWE1 / ROCK2 axis

    doi: 10.1002/kjm2.12768

    Figure Lengend Snippet: Partial reversal of KDM4A inhibition's effect on TMZ resistance in glioma cells by ROCK2 overexpression. ROCK2 overexpression vector (oe‐ROCK2) was transfected into T98G cells, with oe‐NC serving as the control. (A) Transfection efficiency assessed by qRT‐PCR, followed by combined experiments with si‐KDM4A‐1. (B) Expressions of ROCK2 and HUWE1 evaluated by Western blot. (C) Cell viability after 48 h of TMZ treatment measured by CCK‐8 assay and the calculated IC50 value. (D) Cell proliferation ability after treating T98G cells with TMZ concentration of 365 μM for 48 h, evaluated by the clone formation assay. Each experiment was independently repeated three times. Data in panel A were analyzed using a t ‐test. Data in panels C (right)/D were analyzed using one‐way ANOVA, while data in panels B/C (left) were analyzed using two‐way ANOVA, followed by Tukey's multiple comparisons test; ** p < 0.01.

    Article Snippet: The antibodies used included ROCK2 (1:1000, NB100‐593, NOVUS) and HUWE1 (1:1000, ab70161, Abcam).

    Techniques: Inhibition, Over Expression, Plasmid Preparation, Transfection, Control, Quantitative RT-PCR, Western Blot, CCK-8 Assay, Concentration Assay, Tube Formation Assay

    Chinese glioma genome atlas database analysis of ROCK2 and HUWE1 in GBM. (A–D) ROCK2 and HUWE1 expressions in different WHO grades of GBM and recurrent or primary GBM. (E and F) Survival analysis of GBM patients with different ROCK2 and HUWE1 expressions.

    Journal: The Kaohsiung Journal of Medical Sciences

    Article Title: The role of KDM4A‐mediated histone methylation on temozolomide resistance in glioma cells through the HUWE1 / ROCK2 axis

    doi: 10.1002/kjm2.12768

    Figure Lengend Snippet: Chinese glioma genome atlas database analysis of ROCK2 and HUWE1 in GBM. (A–D) ROCK2 and HUWE1 expressions in different WHO grades of GBM and recurrent or primary GBM. (E and F) Survival analysis of GBM patients with different ROCK2 and HUWE1 expressions.

    Article Snippet: The antibodies used included ROCK2 (1:1000, NB100‐593, NOVUS) and HUWE1 (1:1000, ab70161, Abcam).

    Techniques:

    Mechanism of KDM4A in glioma cell resistance to TMZ. In glioma cells, KDM4A reduces H3K9me3 to promote ROCK2 expression and reduces H3K36me3 to inhibit HUWE1 expression through histone demethylation. This represses HUWE1 binding to ROCK2 and inhibits ubiquitin degradation of ROCK2, ultimately promoting glioma cell resistance to TMZ.

    Journal: The Kaohsiung Journal of Medical Sciences

    Article Title: The role of KDM4A‐mediated histone methylation on temozolomide resistance in glioma cells through the HUWE1 / ROCK2 axis

    doi: 10.1002/kjm2.12768

    Figure Lengend Snippet: Mechanism of KDM4A in glioma cell resistance to TMZ. In glioma cells, KDM4A reduces H3K9me3 to promote ROCK2 expression and reduces H3K36me3 to inhibit HUWE1 expression through histone demethylation. This represses HUWE1 binding to ROCK2 and inhibits ubiquitin degradation of ROCK2, ultimately promoting glioma cell resistance to TMZ.

    Article Snippet: The antibodies used included ROCK2 (1:1000, NB100‐593, NOVUS) and HUWE1 (1:1000, ab70161, Abcam).

    Techniques: Expressing, Binding Assay, Ubiquitin Proteomics