hoxa10  (Cell Signaling Technology Inc)


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  • 94

    Structured Review

    Cell Signaling Technology Inc hoxa10
    Primer Sequences for qPCR.
    Hoxa10, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hoxa10/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hoxa10 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis"

    Article Title: Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis

    Journal: Frontiers in Endocrinology

    doi: 10.3389/fendo.2022.928024

    Primer Sequences for qPCR.
    Figure Legend Snippet: Primer Sequences for qPCR.

    Techniques Used: Sequencing

    IL33 is aberrantly expressed in the endometria of women with adenomyosis. (A) IL33 and HOXA10 protein expression in normal (n = 20) and patients with adenomyosis (n = 20) was analyzed by Western blot. (B) The intensities of IL33 signals were quantified from the 20 samples and normalized. to GAPDH. ***p < 0.001. (C) The intensities of HOXA10 signals were quantified from the 20 samples and. normalized to GAPDH. **p < 0.01. (D) Correlation between IL33 and HOXA10 protein expression levels (r = 0.7788, p < 0.0001). (E) Timed mid-secretory endometrial biopsies from healthy control and infertile women with adenomyosis were analyzed using immunohistochemistry (IHC). Rabbit or Goat IgG was used as the negative control. The arrows show the decreased IL33 and HOXA10 conjugates in the endometrial epithelium cell. (F) The integrated optical densities (IOD) of the expression of IL33 and HOXA10 in the endometrium using Image-Pro Plus System 6.0 image analysis software. (G) The mean density of the expression of IL33 and HOXA10 in the endometrium. using Image-Pro Plus System 6.0 image analysis software.
    Figure Legend Snippet: IL33 is aberrantly expressed in the endometria of women with adenomyosis. (A) IL33 and HOXA10 protein expression in normal (n = 20) and patients with adenomyosis (n = 20) was analyzed by Western blot. (B) The intensities of IL33 signals were quantified from the 20 samples and normalized. to GAPDH. ***p < 0.001. (C) The intensities of HOXA10 signals were quantified from the 20 samples and. normalized to GAPDH. **p < 0.01. (D) Correlation between IL33 and HOXA10 protein expression levels (r = 0.7788, p < 0.0001). (E) Timed mid-secretory endometrial biopsies from healthy control and infertile women with adenomyosis were analyzed using immunohistochemistry (IHC). Rabbit or Goat IgG was used as the negative control. The arrows show the decreased IL33 and HOXA10 conjugates in the endometrial epithelium cell. (F) The integrated optical densities (IOD) of the expression of IL33 and HOXA10 in the endometrium using Image-Pro Plus System 6.0 image analysis software. (G) The mean density of the expression of IL33 and HOXA10 in the endometrium. using Image-Pro Plus System 6.0 image analysis software.

    Techniques Used: Expressing, Western Blot, Immunohistochemistry, Negative Control, Software

    IL33 could induce HOXA10 expression. (A) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 mRNA levels were measured by qRT-PCR. ***p < 0.001. (B) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (C) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 and HOXA10 protein levels were measured by Western blot. (D) Ishikawa cells were transfected with si-IL33 or negative control. IL33 mRNA levels. were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (E) Ishikawa cells were transfected with si-IL33 or negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (F) Ishikawa cells were transfected with si-IL33 or negative control. IL33 and HOXA10 protein levels were measured by Western blot.
    Figure Legend Snippet: IL33 could induce HOXA10 expression. (A) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 mRNA levels were measured by qRT-PCR. ***p < 0.001. (B) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (C) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 and HOXA10 protein levels were measured by Western blot. (D) Ishikawa cells were transfected with si-IL33 or negative control. IL33 mRNA levels. were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (E) Ishikawa cells were transfected with si-IL33 or negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (F) Ishikawa cells were transfected with si-IL33 or negative control. IL33 and HOXA10 protein levels were measured by Western blot.

    Techniques Used: Expressing, Transfection, Over Expression, Plasmid Preparation, Negative Control, Quantitative RT-PCR, Western Blot

    IL33 participates in embryo implantation. (A) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. IL33 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (B) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (C) Protein levels were normalized to GAPDH protein expression level in (B) (**p< 0.01, ***p < 0.001. vs control). (D) Western blot analysis of uterine IL33 during the peri-implantation period in mice, with the strongest decreased signal detected at 4.5 dpc. (E) Protein levels were normalized to GAPDH protein expression level in (D) (**p< 0.01, ***p < 0.001. vs control, n is shown in each group). (F) Ishikawa cells were transfected with ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (G) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01. (H) Ishikawa cells were transfected with Flag-IL33 (2 μg) as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies.
    Figure Legend Snippet: IL33 participates in embryo implantation. (A) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. IL33 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (B) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (C) Protein levels were normalized to GAPDH protein expression level in (B) (**p< 0.01, ***p < 0.001. vs control). (D) Western blot analysis of uterine IL33 during the peri-implantation period in mice, with the strongest decreased signal detected at 4.5 dpc. (E) Protein levels were normalized to GAPDH protein expression level in (D) (**p< 0.01, ***p < 0.001. vs control, n is shown in each group). (F) Ishikawa cells were transfected with ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (G) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01. (H) Ishikawa cells were transfected with Flag-IL33 (2 μg) as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies.

    Techniques Used: Quantitative RT-PCR, Western Blot, Expressing, Transfection, Luciferase, Co-Culture Assay

    ST2 silence dose not affect the IL33-promoted HOXA10 expression and embryo implantation in vitro. (A) Ishikawa cells were transfected with si-ST2 or negative control. ST2 mRNA levels were measured by qRT-PCR ** p < 0.01, *** p < 0.001. (B) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, IL33. was overexpression via the transfection of Flag-IL33. HOXA10 mRNA levels were measured by qRT-PCR. ** p < 0.01 (C) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg) were transfected into the cells, as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (D) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h. of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01.
    Figure Legend Snippet: ST2 silence dose not affect the IL33-promoted HOXA10 expression and embryo implantation in vitro. (A) Ishikawa cells were transfected with si-ST2 or negative control. ST2 mRNA levels were measured by qRT-PCR ** p < 0.01, *** p < 0.001. (B) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, IL33. was overexpression via the transfection of Flag-IL33. HOXA10 mRNA levels were measured by qRT-PCR. ** p < 0.01 (C) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg) were transfected into the cells, as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (D) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h. of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01.

    Techniques Used: Expressing, In Vitro, Transfection, Negative Control, Quantitative RT-PCR, Over Expression, Luciferase, Co-Culture Assay

    IL-33 enhances embryo implantation via phosphorylation of STAT3. (A) Ishikawa cells were transfected with Flag-IL33 (2 μg). IL33, STAT3 and p-STAT3 protein levels were analyzed by western blot analysis. (B) Ishikawa cells were transfected with siIL33 (50 or 100 nM), Whole-cell lysates. were analyzed by western blot analysis with the indicated antibodies. (C) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of Flag-IL33 (2 μg), Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (D) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. The luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05. (E) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before the. transfection of Flag-IL33 (2 μg). BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), *p < 0.05.
    Figure Legend Snippet: IL-33 enhances embryo implantation via phosphorylation of STAT3. (A) Ishikawa cells were transfected with Flag-IL33 (2 μg). IL33, STAT3 and p-STAT3 protein levels were analyzed by western blot analysis. (B) Ishikawa cells were transfected with siIL33 (50 or 100 nM), Whole-cell lysates. were analyzed by western blot analysis with the indicated antibodies. (C) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of Flag-IL33 (2 μg), Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (D) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. The luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05. (E) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before the. transfection of Flag-IL33 (2 μg). BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), *p < 0.05.

    Techniques Used: Transfection, Western Blot, Luciferase, Co-Culture Assay

    IL33 expression is decreased in a mouse model of adenomyosis. (A) HE staining confirmed that the mouse model of adenomyosis was successfully constructed. (B) Uterus from control mouse and adenomyosis mouse model were analyzed using immunohistochemistry (IHC). Rabbit IgG was used as the negative control. The arrows show the decreased IL33 conjugates in the endometrial cell epithelium. (C) IL33 and HOXA10 protein expression in control (n =10) and mouse with adenomyosis (n=10) was analyzed by Western blot. (D) The intensities of IL33 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (E) The intensities of HOXA10 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (F) Correlation between IL33 and HOXA10 protein expression levels (r = 0.8151, p < 0.0001).
    Figure Legend Snippet: IL33 expression is decreased in a mouse model of adenomyosis. (A) HE staining confirmed that the mouse model of adenomyosis was successfully constructed. (B) Uterus from control mouse and adenomyosis mouse model were analyzed using immunohistochemistry (IHC). Rabbit IgG was used as the negative control. The arrows show the decreased IL33 conjugates in the endometrial cell epithelium. (C) IL33 and HOXA10 protein expression in control (n =10) and mouse with adenomyosis (n=10) was analyzed by Western blot. (D) The intensities of IL33 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (E) The intensities of HOXA10 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (F) Correlation between IL33 and HOXA10 protein expression levels (r = 0.8151, p < 0.0001).

    Techniques Used: Expressing, Staining, Construct, Immunohistochemistry, Negative Control, Western Blot

    hoxa10  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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  • Team
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  • 94

    Structured Review

    Cell Signaling Technology Inc hoxa10
    Primer Sequences for qPCR.
    Hoxa10, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hoxa10/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hoxa10 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis"

    Article Title: Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis

    Journal: Frontiers in Endocrinology

    doi: 10.3389/fendo.2022.928024

    Primer Sequences for qPCR.
    Figure Legend Snippet: Primer Sequences for qPCR.

    Techniques Used: Sequencing

    IL33 is aberrantly expressed in the endometria of women with adenomyosis. (A) IL33 and HOXA10 protein expression in normal (n = 20) and patients with adenomyosis (n = 20) was analyzed by Western blot. (B) The intensities of IL33 signals were quantified from the 20 samples and normalized. to GAPDH. ***p < 0.001. (C) The intensities of HOXA10 signals were quantified from the 20 samples and. normalized to GAPDH. **p < 0.01. (D) Correlation between IL33 and HOXA10 protein expression levels (r = 0.7788, p < 0.0001). (E) Timed mid-secretory endometrial biopsies from healthy control and infertile women with adenomyosis were analyzed using immunohistochemistry (IHC). Rabbit or Goat IgG was used as the negative control. The arrows show the decreased IL33 and HOXA10 conjugates in the endometrial epithelium cell. (F) The integrated optical densities (IOD) of the expression of IL33 and HOXA10 in the endometrium using Image-Pro Plus System 6.0 image analysis software. (G) The mean density of the expression of IL33 and HOXA10 in the endometrium. using Image-Pro Plus System 6.0 image analysis software.
    Figure Legend Snippet: IL33 is aberrantly expressed in the endometria of women with adenomyosis. (A) IL33 and HOXA10 protein expression in normal (n = 20) and patients with adenomyosis (n = 20) was analyzed by Western blot. (B) The intensities of IL33 signals were quantified from the 20 samples and normalized. to GAPDH. ***p < 0.001. (C) The intensities of HOXA10 signals were quantified from the 20 samples and. normalized to GAPDH. **p < 0.01. (D) Correlation between IL33 and HOXA10 protein expression levels (r = 0.7788, p < 0.0001). (E) Timed mid-secretory endometrial biopsies from healthy control and infertile women with adenomyosis were analyzed using immunohistochemistry (IHC). Rabbit or Goat IgG was used as the negative control. The arrows show the decreased IL33 and HOXA10 conjugates in the endometrial epithelium cell. (F) The integrated optical densities (IOD) of the expression of IL33 and HOXA10 in the endometrium using Image-Pro Plus System 6.0 image analysis software. (G) The mean density of the expression of IL33 and HOXA10 in the endometrium. using Image-Pro Plus System 6.0 image analysis software.

    Techniques Used: Expressing, Western Blot, Immunohistochemistry, Negative Control, Software

    IL33 could induce HOXA10 expression. (A) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 mRNA levels were measured by qRT-PCR. ***p < 0.001. (B) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (C) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 and HOXA10 protein levels were measured by Western blot. (D) Ishikawa cells were transfected with si-IL33 or negative control. IL33 mRNA levels. were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (E) Ishikawa cells were transfected with si-IL33 or negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (F) Ishikawa cells were transfected with si-IL33 or negative control. IL33 and HOXA10 protein levels were measured by Western blot.
    Figure Legend Snippet: IL33 could induce HOXA10 expression. (A) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 mRNA levels were measured by qRT-PCR. ***p < 0.001. (B) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (C) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 and HOXA10 protein levels were measured by Western blot. (D) Ishikawa cells were transfected with si-IL33 or negative control. IL33 mRNA levels. were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (E) Ishikawa cells were transfected with si-IL33 or negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (F) Ishikawa cells were transfected with si-IL33 or negative control. IL33 and HOXA10 protein levels were measured by Western blot.

    Techniques Used: Expressing, Transfection, Over Expression, Plasmid Preparation, Negative Control, Quantitative RT-PCR, Western Blot

    IL33 participates in embryo implantation. (A) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. IL33 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (B) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (C) Protein levels were normalized to GAPDH protein expression level in (B) (**p< 0.01, ***p < 0.001. vs control). (D) Western blot analysis of uterine IL33 during the peri-implantation period in mice, with the strongest decreased signal detected at 4.5 dpc. (E) Protein levels were normalized to GAPDH protein expression level in (D) (**p< 0.01, ***p < 0.001. vs control, n is shown in each group). (F) Ishikawa cells were transfected with ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (G) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01. (H) Ishikawa cells were transfected with Flag-IL33 (2 μg) as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies.
    Figure Legend Snippet: IL33 participates in embryo implantation. (A) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. IL33 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (B) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (C) Protein levels were normalized to GAPDH protein expression level in (B) (**p< 0.01, ***p < 0.001. vs control). (D) Western blot analysis of uterine IL33 during the peri-implantation period in mice, with the strongest decreased signal detected at 4.5 dpc. (E) Protein levels were normalized to GAPDH protein expression level in (D) (**p< 0.01, ***p < 0.001. vs control, n is shown in each group). (F) Ishikawa cells were transfected with ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (G) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01. (H) Ishikawa cells were transfected with Flag-IL33 (2 μg) as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies.

    Techniques Used: Quantitative RT-PCR, Western Blot, Expressing, Transfection, Luciferase, Co-Culture Assay

    ST2 silence dose not affect the IL33-promoted HOXA10 expression and embryo implantation in vitro. (A) Ishikawa cells were transfected with si-ST2 or negative control. ST2 mRNA levels were measured by qRT-PCR ** p < 0.01, *** p < 0.001. (B) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, IL33. was overexpression via the transfection of Flag-IL33. HOXA10 mRNA levels were measured by qRT-PCR. ** p < 0.01 (C) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg) were transfected into the cells, as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (D) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h. of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01.
    Figure Legend Snippet: ST2 silence dose not affect the IL33-promoted HOXA10 expression and embryo implantation in vitro. (A) Ishikawa cells were transfected with si-ST2 or negative control. ST2 mRNA levels were measured by qRT-PCR ** p < 0.01, *** p < 0.001. (B) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, IL33. was overexpression via the transfection of Flag-IL33. HOXA10 mRNA levels were measured by qRT-PCR. ** p < 0.01 (C) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg) were transfected into the cells, as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (D) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h. of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01.

    Techniques Used: Expressing, In Vitro, Transfection, Negative Control, Quantitative RT-PCR, Over Expression, Luciferase, Co-Culture Assay

    IL-33 enhances embryo implantation via phosphorylation of STAT3. (A) Ishikawa cells were transfected with Flag-IL33 (2 μg). IL33, STAT3 and p-STAT3 protein levels were analyzed by western blot analysis. (B) Ishikawa cells were transfected with siIL33 (50 or 100 nM), Whole-cell lysates. were analyzed by western blot analysis with the indicated antibodies. (C) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of Flag-IL33 (2 μg), Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (D) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. The luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05. (E) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before the. transfection of Flag-IL33 (2 μg). BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), *p < 0.05.
    Figure Legend Snippet: IL-33 enhances embryo implantation via phosphorylation of STAT3. (A) Ishikawa cells were transfected with Flag-IL33 (2 μg). IL33, STAT3 and p-STAT3 protein levels were analyzed by western blot analysis. (B) Ishikawa cells were transfected with siIL33 (50 or 100 nM), Whole-cell lysates. were analyzed by western blot analysis with the indicated antibodies. (C) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of Flag-IL33 (2 μg), Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (D) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. The luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05. (E) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before the. transfection of Flag-IL33 (2 μg). BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), *p < 0.05.

    Techniques Used: Transfection, Western Blot, Luciferase, Co-Culture Assay

    IL33 expression is decreased in a mouse model of adenomyosis. (A) HE staining confirmed that the mouse model of adenomyosis was successfully constructed. (B) Uterus from control mouse and adenomyosis mouse model were analyzed using immunohistochemistry (IHC). Rabbit IgG was used as the negative control. The arrows show the decreased IL33 conjugates in the endometrial cell epithelium. (C) IL33 and HOXA10 protein expression in control (n =10) and mouse with adenomyosis (n=10) was analyzed by Western blot. (D) The intensities of IL33 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (E) The intensities of HOXA10 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (F) Correlation between IL33 and HOXA10 protein expression levels (r = 0.8151, p < 0.0001).
    Figure Legend Snippet: IL33 expression is decreased in a mouse model of adenomyosis. (A) HE staining confirmed that the mouse model of adenomyosis was successfully constructed. (B) Uterus from control mouse and adenomyosis mouse model were analyzed using immunohistochemistry (IHC). Rabbit IgG was used as the negative control. The arrows show the decreased IL33 conjugates in the endometrial cell epithelium. (C) IL33 and HOXA10 protein expression in control (n =10) and mouse with adenomyosis (n=10) was analyzed by Western blot. (D) The intensities of IL33 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (E) The intensities of HOXA10 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (F) Correlation between IL33 and HOXA10 protein expression levels (r = 0.8151, p < 0.0001).

    Techniques Used: Expressing, Staining, Construct, Immunohistochemistry, Negative Control, Western Blot

    hoxa10  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc hoxa10
    <t>HOXA10</t> is a downstream target of miR-588. (a) Starbase was used for target prediction between HOAX10 and miR-388. (b-e) The combination between HOXA10 and miR-588 was conducted through the dual-luciferase reporter (b-c) and RIP assays (d-e). (f) HOXA10 mRNA expression was examined via RT-qPCR. (g) The relationship between HOXA10 and miR-588 expression was analyzed by Pearson’s correlation. (h-i) The protein level of HOXA10 was measured via western blotting. ** P < 0.01, *** P < 0.001, **** P < 0.0001.
    Hoxa10, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Circ_0010235 Regulates HOXA10 Expression to Promote Malignant Phenotypes and Radioresistance in Non-small Cell Lung Cancer Cells Via Decoying miR-588"

    Article Title: Circ_0010235 Regulates HOXA10 Expression to Promote Malignant Phenotypes and Radioresistance in Non-small Cell Lung Cancer Cells Via Decoying miR-588

    Journal: Balkan Medical Journal

    doi: 10.4274/balkanmedj.galenos.2022.2022-2-50

    HOXA10 is a downstream target of miR-588. (a) Starbase was used for target prediction between HOAX10 and miR-388. (b-e) The combination between HOXA10 and miR-588 was conducted through the dual-luciferase reporter (b-c) and RIP assays (d-e). (f) HOXA10 mRNA expression was examined via RT-qPCR. (g) The relationship between HOXA10 and miR-588 expression was analyzed by Pearson’s correlation. (h-i) The protein level of HOXA10 was measured via western blotting. ** P < 0.01, *** P < 0.001, **** P < 0.0001.
    Figure Legend Snippet: HOXA10 is a downstream target of miR-588. (a) Starbase was used for target prediction between HOAX10 and miR-388. (b-e) The combination between HOXA10 and miR-588 was conducted through the dual-luciferase reporter (b-c) and RIP assays (d-e). (f) HOXA10 mRNA expression was examined via RT-qPCR. (g) The relationship between HOXA10 and miR-588 expression was analyzed by Pearson’s correlation. (h-i) The protein level of HOXA10 was measured via western blotting. ** P < 0.01, *** P < 0.001, **** P < 0.0001.

    Techniques Used: Luciferase, Expressing, Quantitative RT-PCR, Western Blot

    MiR-588 acts as a tumor inhibitor and radiation sensitizer by targeting HOXA10. The transfection of miR-NC, miR-588, miR-588+pcDNA, and miR-588+HOXA10 was performed in A549 and H1299 cells. (a) Western blotting was used for the analysis of HOXA10 protein expression. (b-c) The CCK-8 and EdU assays were used to determine cell viability (b) and proliferation (c), respectively. (d) Flow cytometry was used for apoptosis examination. (e-f) The transwell and wound healing assays were applied for the assessment of invasion (e) and migration (f), respectively. (g-h) Western blotting was applied for the detection of c-myc and cleaved-caspase-3. (i-j) The colony formation assay was used for survival analysis after cells were treated with radiation. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.
    Figure Legend Snippet: MiR-588 acts as a tumor inhibitor and radiation sensitizer by targeting HOXA10. The transfection of miR-NC, miR-588, miR-588+pcDNA, and miR-588+HOXA10 was performed in A549 and H1299 cells. (a) Western blotting was used for the analysis of HOXA10 protein expression. (b-c) The CCK-8 and EdU assays were used to determine cell viability (b) and proliferation (c), respectively. (d) Flow cytometry was used for apoptosis examination. (e-f) The transwell and wound healing assays were applied for the assessment of invasion (e) and migration (f), respectively. (g-h) Western blotting was applied for the detection of c-myc and cleaved-caspase-3. (i-j) The colony formation assay was used for survival analysis after cells were treated with radiation. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001.

    Techniques Used: Transfection, Western Blot, Expressing, CCK-8 Assay, Flow Cytometry, Migration, Colony Assay

    Circ_0010235 could upregulate HOXA10 by sponging miR-588 in NSCLC cells. (a) Western blotting conducted to determine the protein expression of HOXA10 in the si-NC, si-circ_0010235, si-circ_0010235+anti-miR-NC, or si-circ_0010235+anti-miR-588 transfection group. ** P < 0.01, *** P < 0.001, **** P < 0.0001.
    Figure Legend Snippet: Circ_0010235 could upregulate HOXA10 by sponging miR-588 in NSCLC cells. (a) Western blotting conducted to determine the protein expression of HOXA10 in the si-NC, si-circ_0010235, si-circ_0010235+anti-miR-NC, or si-circ_0010235+anti-miR-588 transfection group. ** P < 0.01, *** P < 0.001, **** P < 0.0001.

    Techniques Used: Western Blot, Expressing, Transfection

    Graphical abstract of circ_0010235/miR-588/HOXA10 axis in NSCLC progression and radioresistance.
    Figure Legend Snippet: Graphical abstract of circ_0010235/miR-588/HOXA10 axis in NSCLC progression and radioresistance.

    Techniques Used:

    anti hoxa10  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti hoxa10
    <t>HOXA10</t> and BCL2 expressions were elevated in GC tissues. A and B, qRT‐PCR and western blot indicated that the expression of HOXA10 was higher in GC tissues (qRT‐PCR values were arranged from low to high). C, HOXA10 was elevated in the STAD reanalyzed from GEPIA. D, HOXA10 ranked fourth of the top 25 overexpressed genes in the STAD from UALCAN. E, Higher expression of HOXA10, BCL2 demonstrated lower overall survival rate in GC patients reanalyzed from the Kaplan‐Meier Plotter. F, Representative immunohistochemical staining showed that HOXA10, BCL2, and Ki67 were upregulated in GC tissues. Original magnification, 100× (200× for insert images). GC, gastric cancer; qRT‐PCR, quantitative real‐time polymerase chain reaction; STAD, stomach adenocarcinoma dataset
    Anti Hoxa10, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    1) Product Images from "HOXA10 induces BCL2 expression, inhibits apoptosis, and promotes cell proliferation in gastric cancer"

    Article Title: HOXA10 induces BCL2 expression, inhibits apoptosis, and promotes cell proliferation in gastric cancer

    Journal: Cancer Medicine

    doi: 10.1002/cam4.2440

    HOXA10 and BCL2 expressions were elevated in GC tissues. A and B, qRT‐PCR and western blot indicated that the expression of HOXA10 was higher in GC tissues (qRT‐PCR values were arranged from low to high). C, HOXA10 was elevated in the STAD reanalyzed from GEPIA. D, HOXA10 ranked fourth of the top 25 overexpressed genes in the STAD from UALCAN. E, Higher expression of HOXA10, BCL2 demonstrated lower overall survival rate in GC patients reanalyzed from the Kaplan‐Meier Plotter. F, Representative immunohistochemical staining showed that HOXA10, BCL2, and Ki67 were upregulated in GC tissues. Original magnification, 100× (200× for insert images). GC, gastric cancer; qRT‐PCR, quantitative real‐time polymerase chain reaction; STAD, stomach adenocarcinoma dataset
    Figure Legend Snippet: HOXA10 and BCL2 expressions were elevated in GC tissues. A and B, qRT‐PCR and western blot indicated that the expression of HOXA10 was higher in GC tissues (qRT‐PCR values were arranged from low to high). C, HOXA10 was elevated in the STAD reanalyzed from GEPIA. D, HOXA10 ranked fourth of the top 25 overexpressed genes in the STAD from UALCAN. E, Higher expression of HOXA10, BCL2 demonstrated lower overall survival rate in GC patients reanalyzed from the Kaplan‐Meier Plotter. F, Representative immunohistochemical staining showed that HOXA10, BCL2, and Ki67 were upregulated in GC tissues. Original magnification, 100× (200× for insert images). GC, gastric cancer; qRT‐PCR, quantitative real‐time polymerase chain reaction; STAD, stomach adenocarcinoma dataset

    Techniques Used: Quantitative RT-PCR, Western Blot, Expressing, Immunohistochemical staining, Staining, Real-time Polymerase Chain Reaction

    HOXA10 promoted proliferation and repressed apoptosis in GC cells. A and B, The CCK‐8 assay showed that HOXA10 knockdown inhibited cell growth but could be partly rescued by transfecting with BCL2‐overexpressing plasmid. And, HOXA10 overexpression promoted cell growth but could be partially impaired with treatment of BCL2 selective inhibitor ABT‐199. C and D, HOXA10 knockdown inhibited colony formation in BGC‐823 cells while HOXA10 overexpression enhanced colony formation in AGS and HGC‐27 cells. E and F, The cell apoptosis assay showed the percentage of apoptotic cells was higher in HOXA10‐knockdown cells (BGC‐823‐sh‐HOXA10, NCI‐N87‐sh‐HOXA10) compared with the control cells, but could be partly reduced by transfecting with BCL2‐overexpressing plasmid. And, the portion of apoptotic cells was lower in HOXA10‐overexpressinig cells (AGS‐HOXA10‐OV, HGC‐27‐HOXA10‐OV) compared with the corresponding control cells, but could be partially rescued with treatment of ABT‐199. ** P < .01, *** P < .001. CCK‐8, cell counting kit‐8. GC, gastric cancer
    Figure Legend Snippet: HOXA10 promoted proliferation and repressed apoptosis in GC cells. A and B, The CCK‐8 assay showed that HOXA10 knockdown inhibited cell growth but could be partly rescued by transfecting with BCL2‐overexpressing plasmid. And, HOXA10 overexpression promoted cell growth but could be partially impaired with treatment of BCL2 selective inhibitor ABT‐199. C and D, HOXA10 knockdown inhibited colony formation in BGC‐823 cells while HOXA10 overexpression enhanced colony formation in AGS and HGC‐27 cells. E and F, The cell apoptosis assay showed the percentage of apoptotic cells was higher in HOXA10‐knockdown cells (BGC‐823‐sh‐HOXA10, NCI‐N87‐sh‐HOXA10) compared with the control cells, but could be partly reduced by transfecting with BCL2‐overexpressing plasmid. And, the portion of apoptotic cells was lower in HOXA10‐overexpressinig cells (AGS‐HOXA10‐OV, HGC‐27‐HOXA10‐OV) compared with the corresponding control cells, but could be partially rescued with treatment of ABT‐199. ** P < .01, *** P < .001. CCK‐8, cell counting kit‐8. GC, gastric cancer

    Techniques Used: CCK-8 Assay, Plasmid Preparation, Over Expression, Apoptosis Assay, Cell Counting

    HOXA10 promoted tumor growth in the nude mice xenograft tumor formation assay. A, Tumors formed by AGS‐HOXA10‐OV cells demonstrated an elevation of bioluminescent signal. B‐D, The weight and volume of tumors formed by AGS cells in different groups. HOXA10 overexpression promoted xenograft tumor growth in nude mice. E‐H, The weight and volume of tumors formed by NCI‐N87 cells showed HOXA10 knockdown inhibited xenograft tumor growth in nude mice. I and J, Representative immunohistochemical staining of HOXA10, BCL2, and Ki67 in xenograft tumors. Original magnification, 200×. * P < .05
    Figure Legend Snippet: HOXA10 promoted tumor growth in the nude mice xenograft tumor formation assay. A, Tumors formed by AGS‐HOXA10‐OV cells demonstrated an elevation of bioluminescent signal. B‐D, The weight and volume of tumors formed by AGS cells in different groups. HOXA10 overexpression promoted xenograft tumor growth in nude mice. E‐H, The weight and volume of tumors formed by NCI‐N87 cells showed HOXA10 knockdown inhibited xenograft tumor growth in nude mice. I and J, Representative immunohistochemical staining of HOXA10, BCL2, and Ki67 in xenograft tumors. Original magnification, 200×. * P < .05

    Techniques Used: Tube Formation Assay, Over Expression, Immunohistochemical staining, Staining

    The bioinformatics analysis, qRT‐PCR, western blot, and ChIP‐qPCR assay revealed that HOXA10 might induce BCL2 expression via binding to its promoter region. A, The “TF‐gene interactions” analysis of HOXA10 and BCL2 in the database NetworkAnalyst. B, A PPI network was built between HOXA10 and BCL2 with the database STRING. C, qRT‐PCR showed the relative BCL2 mRNA level in different cells with changed HOXA10 expression. D, Expression of BCL2, Bax, cleaved forms of Caspase‐9, Caspase‐3, and PARP in different GC cells with altered HOXA10 expression. E, HOXA10 binding motif acquired from JASPAR and the relative primer position within the BCL2 promoter region. F, ChIP‐qPCR assay indicated the possible positive HOXA10 binding sites across the BCL2 promoter region. G, 3% agarose gel electrophoresis of ChIP‐qPCR products. ** P < .01, *** P < .001. ChIP‐qPCR, chromatin immunoprecipitation and quantitative PCR; PPI, protein‐protein interaction; qRT‐PCR, quantitative real‐time polymerase chain reaction; TF‐gene, transcription factor‐gene
    Figure Legend Snippet: The bioinformatics analysis, qRT‐PCR, western blot, and ChIP‐qPCR assay revealed that HOXA10 might induce BCL2 expression via binding to its promoter region. A, The “TF‐gene interactions” analysis of HOXA10 and BCL2 in the database NetworkAnalyst. B, A PPI network was built between HOXA10 and BCL2 with the database STRING. C, qRT‐PCR showed the relative BCL2 mRNA level in different cells with changed HOXA10 expression. D, Expression of BCL2, Bax, cleaved forms of Caspase‐9, Caspase‐3, and PARP in different GC cells with altered HOXA10 expression. E, HOXA10 binding motif acquired from JASPAR and the relative primer position within the BCL2 promoter region. F, ChIP‐qPCR assay indicated the possible positive HOXA10 binding sites across the BCL2 promoter region. G, 3% agarose gel electrophoresis of ChIP‐qPCR products. ** P < .01, *** P < .001. ChIP‐qPCR, chromatin immunoprecipitation and quantitative PCR; PPI, protein‐protein interaction; qRT‐PCR, quantitative real‐time polymerase chain reaction; TF‐gene, transcription factor‐gene

    Techniques Used: Quantitative RT-PCR, Western Blot, Expressing, Binding Assay, Agarose Gel Electrophoresis, Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction

    anti hoxa10  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti hoxa10
    <t>HOXA10</t> and BCL2 expressions were elevated in GC tissues. A and B, qRT‐PCR and western blot indicated that the expression of HOXA10 was higher in GC tissues (qRT‐PCR values were arranged from low to high). C, HOXA10 was elevated in the STAD reanalyzed from GEPIA. D, HOXA10 ranked fourth of the top 25 overexpressed genes in the STAD from UALCAN. E, Higher expression of HOXA10, BCL2 demonstrated lower overall survival rate in GC patients reanalyzed from the Kaplan‐Meier Plotter. F, Representative immunohistochemical staining showed that HOXA10, BCL2, and Ki67 were upregulated in GC tissues. Original magnification, 100× (200× for insert images). GC, gastric cancer; qRT‐PCR, quantitative real‐time polymerase chain reaction; STAD, stomach adenocarcinoma dataset
    Anti Hoxa10, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti hoxa10/product/Cell Signaling Technology Inc
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti hoxa10 - by Bioz Stars, 2023-02
    94/100 stars

    Images

    1) Product Images from "HOXA10 induces BCL2 expression, inhibits apoptosis, and promotes cell proliferation in gastric cancer"

    Article Title: HOXA10 induces BCL2 expression, inhibits apoptosis, and promotes cell proliferation in gastric cancer

    Journal: Cancer Medicine

    doi: 10.1002/cam4.2440

    HOXA10 and BCL2 expressions were elevated in GC tissues. A and B, qRT‐PCR and western blot indicated that the expression of HOXA10 was higher in GC tissues (qRT‐PCR values were arranged from low to high). C, HOXA10 was elevated in the STAD reanalyzed from GEPIA. D, HOXA10 ranked fourth of the top 25 overexpressed genes in the STAD from UALCAN. E, Higher expression of HOXA10, BCL2 demonstrated lower overall survival rate in GC patients reanalyzed from the Kaplan‐Meier Plotter. F, Representative immunohistochemical staining showed that HOXA10, BCL2, and Ki67 were upregulated in GC tissues. Original magnification, 100× (200× for insert images). GC, gastric cancer; qRT‐PCR, quantitative real‐time polymerase chain reaction; STAD, stomach adenocarcinoma dataset
    Figure Legend Snippet: HOXA10 and BCL2 expressions were elevated in GC tissues. A and B, qRT‐PCR and western blot indicated that the expression of HOXA10 was higher in GC tissues (qRT‐PCR values were arranged from low to high). C, HOXA10 was elevated in the STAD reanalyzed from GEPIA. D, HOXA10 ranked fourth of the top 25 overexpressed genes in the STAD from UALCAN. E, Higher expression of HOXA10, BCL2 demonstrated lower overall survival rate in GC patients reanalyzed from the Kaplan‐Meier Plotter. F, Representative immunohistochemical staining showed that HOXA10, BCL2, and Ki67 were upregulated in GC tissues. Original magnification, 100× (200× for insert images). GC, gastric cancer; qRT‐PCR, quantitative real‐time polymerase chain reaction; STAD, stomach adenocarcinoma dataset

    Techniques Used: Quantitative RT-PCR, Western Blot, Expressing, Immunohistochemical staining, Staining, Real-time Polymerase Chain Reaction

    HOXA10 promoted proliferation and repressed apoptosis in GC cells. A and B, The CCK‐8 assay showed that HOXA10 knockdown inhibited cell growth but could be partly rescued by transfecting with BCL2‐overexpressing plasmid. And, HOXA10 overexpression promoted cell growth but could be partially impaired with treatment of BCL2 selective inhibitor ABT‐199. C and D, HOXA10 knockdown inhibited colony formation in BGC‐823 cells while HOXA10 overexpression enhanced colony formation in AGS and HGC‐27 cells. E and F, The cell apoptosis assay showed the percentage of apoptotic cells was higher in HOXA10‐knockdown cells (BGC‐823‐sh‐HOXA10, NCI‐N87‐sh‐HOXA10) compared with the control cells, but could be partly reduced by transfecting with BCL2‐overexpressing plasmid. And, the portion of apoptotic cells was lower in HOXA10‐overexpressinig cells (AGS‐HOXA10‐OV, HGC‐27‐HOXA10‐OV) compared with the corresponding control cells, but could be partially rescued with treatment of ABT‐199. ** P < .01, *** P < .001. CCK‐8, cell counting kit‐8. GC, gastric cancer
    Figure Legend Snippet: HOXA10 promoted proliferation and repressed apoptosis in GC cells. A and B, The CCK‐8 assay showed that HOXA10 knockdown inhibited cell growth but could be partly rescued by transfecting with BCL2‐overexpressing plasmid. And, HOXA10 overexpression promoted cell growth but could be partially impaired with treatment of BCL2 selective inhibitor ABT‐199. C and D, HOXA10 knockdown inhibited colony formation in BGC‐823 cells while HOXA10 overexpression enhanced colony formation in AGS and HGC‐27 cells. E and F, The cell apoptosis assay showed the percentage of apoptotic cells was higher in HOXA10‐knockdown cells (BGC‐823‐sh‐HOXA10, NCI‐N87‐sh‐HOXA10) compared with the control cells, but could be partly reduced by transfecting with BCL2‐overexpressing plasmid. And, the portion of apoptotic cells was lower in HOXA10‐overexpressinig cells (AGS‐HOXA10‐OV, HGC‐27‐HOXA10‐OV) compared with the corresponding control cells, but could be partially rescued with treatment of ABT‐199. ** P < .01, *** P < .001. CCK‐8, cell counting kit‐8. GC, gastric cancer

    Techniques Used: CCK-8 Assay, Plasmid Preparation, Over Expression, Apoptosis Assay, Cell Counting

    HOXA10 promoted tumor growth in the nude mice xenograft tumor formation assay. A, Tumors formed by AGS‐HOXA10‐OV cells demonstrated an elevation of bioluminescent signal. B‐D, The weight and volume of tumors formed by AGS cells in different groups. HOXA10 overexpression promoted xenograft tumor growth in nude mice. E‐H, The weight and volume of tumors formed by NCI‐N87 cells showed HOXA10 knockdown inhibited xenograft tumor growth in nude mice. I and J, Representative immunohistochemical staining of HOXA10, BCL2, and Ki67 in xenograft tumors. Original magnification, 200×. * P < .05
    Figure Legend Snippet: HOXA10 promoted tumor growth in the nude mice xenograft tumor formation assay. A, Tumors formed by AGS‐HOXA10‐OV cells demonstrated an elevation of bioluminescent signal. B‐D, The weight and volume of tumors formed by AGS cells in different groups. HOXA10 overexpression promoted xenograft tumor growth in nude mice. E‐H, The weight and volume of tumors formed by NCI‐N87 cells showed HOXA10 knockdown inhibited xenograft tumor growth in nude mice. I and J, Representative immunohistochemical staining of HOXA10, BCL2, and Ki67 in xenograft tumors. Original magnification, 200×. * P < .05

    Techniques Used: Tube Formation Assay, Over Expression, Immunohistochemical staining, Staining

    The bioinformatics analysis, qRT‐PCR, western blot, and ChIP‐qPCR assay revealed that HOXA10 might induce BCL2 expression via binding to its promoter region. A, The “TF‐gene interactions” analysis of HOXA10 and BCL2 in the database NetworkAnalyst. B, A PPI network was built between HOXA10 and BCL2 with the database STRING. C, qRT‐PCR showed the relative BCL2 mRNA level in different cells with changed HOXA10 expression. D, Expression of BCL2, Bax, cleaved forms of Caspase‐9, Caspase‐3, and PARP in different GC cells with altered HOXA10 expression. E, HOXA10 binding motif acquired from JASPAR and the relative primer position within the BCL2 promoter region. F, ChIP‐qPCR assay indicated the possible positive HOXA10 binding sites across the BCL2 promoter region. G, 3% agarose gel electrophoresis of ChIP‐qPCR products. ** P < .01, *** P < .001. ChIP‐qPCR, chromatin immunoprecipitation and quantitative PCR; PPI, protein‐protein interaction; qRT‐PCR, quantitative real‐time polymerase chain reaction; TF‐gene, transcription factor‐gene
    Figure Legend Snippet: The bioinformatics analysis, qRT‐PCR, western blot, and ChIP‐qPCR assay revealed that HOXA10 might induce BCL2 expression via binding to its promoter region. A, The “TF‐gene interactions” analysis of HOXA10 and BCL2 in the database NetworkAnalyst. B, A PPI network was built between HOXA10 and BCL2 with the database STRING. C, qRT‐PCR showed the relative BCL2 mRNA level in different cells with changed HOXA10 expression. D, Expression of BCL2, Bax, cleaved forms of Caspase‐9, Caspase‐3, and PARP in different GC cells with altered HOXA10 expression. E, HOXA10 binding motif acquired from JASPAR and the relative primer position within the BCL2 promoter region. F, ChIP‐qPCR assay indicated the possible positive HOXA10 binding sites across the BCL2 promoter region. G, 3% agarose gel electrophoresis of ChIP‐qPCR products. ** P < .01, *** P < .001. ChIP‐qPCR, chromatin immunoprecipitation and quantitative PCR; PPI, protein‐protein interaction; qRT‐PCR, quantitative real‐time polymerase chain reaction; TF‐gene, transcription factor‐gene

    Techniques Used: Quantitative RT-PCR, Western Blot, Expressing, Binding Assay, Agarose Gel Electrophoresis, Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction

    hoxa10  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc hoxa10
    NS with elevated V1G1 levels are characterized by upregulation of Homeodomain-containing genes. a) The indicated transcripts were analyzed by qPCR in primary NS or differentiated cultures. Bars, mean ± SEM (n = 4). b,) Representative NS cultures with high (NS92 and 97) or low (NS88 and 121) V1G1 expression were analyzed for the indicated proteins expression by western blotting. Vinculin was a loading control. c) The homeodomain proteins <t>HOXA10,</t> HOXA7 or POU3F2 were analyzed by immunofluorescence in NS with Low or High V1G1 levels. Scale bars, 50 μm.
    Hoxa10, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hoxa10 - by Bioz Stars, 2023-02
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    1) Product Images from "Specific V-ATPase expression sub-classifies IDHwt lower-grade gliomas and impacts glioma growth in vivo"

    Article Title: Specific V-ATPase expression sub-classifies IDHwt lower-grade gliomas and impacts glioma growth in vivo

    Journal: EBioMedicine

    doi: 10.1016/j.ebiom.2019.01.052

    NS with elevated V1G1 levels are characterized by upregulation of Homeodomain-containing genes. a) The indicated transcripts were analyzed by qPCR in primary NS or differentiated cultures. Bars, mean ± SEM (n = 4). b,) Representative NS cultures with high (NS92 and 97) or low (NS88 and 121) V1G1 expression were analyzed for the indicated proteins expression by western blotting. Vinculin was a loading control. c) The homeodomain proteins HOXA10, HOXA7 or POU3F2 were analyzed by immunofluorescence in NS with Low or High V1G1 levels. Scale bars, 50 μm.
    Figure Legend Snippet: NS with elevated V1G1 levels are characterized by upregulation of Homeodomain-containing genes. a) The indicated transcripts were analyzed by qPCR in primary NS or differentiated cultures. Bars, mean ± SEM (n = 4). b,) Representative NS cultures with high (NS92 and 97) or low (NS88 and 121) V1G1 expression were analyzed for the indicated proteins expression by western blotting. Vinculin was a loading control. c) The homeodomain proteins HOXA10, HOXA7 or POU3F2 were analyzed by immunofluorescence in NS with Low or High V1G1 levels. Scale bars, 50 μm.

    Techniques Used: Expressing, Western Blot, Immunofluorescence

    anti arhgef6  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti arhgef6
    Anti Arhgef6, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti hoxa10  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc hoxa10
    Primer Sequences for qPCR.
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    <t>HOXA10</t> and BCL2 expressions were elevated in GC tissues. A and B, qRT‐PCR and western blot indicated that the expression of HOXA10 was higher in GC tissues (qRT‐PCR values were arranged from low to high). C, HOXA10 was elevated in the STAD reanalyzed from GEPIA. D, HOXA10 ranked fourth of the top 25 overexpressed genes in the STAD from UALCAN. E, Higher expression of HOXA10, BCL2 demonstrated lower overall survival rate in GC patients reanalyzed from the Kaplan‐Meier Plotter. F, Representative immunohistochemical staining showed that HOXA10, BCL2, and Ki67 were upregulated in GC tissues. Original magnification, 100× (200× for insert images). GC, gastric cancer; qRT‐PCR, quantitative real‐time polymerase chain reaction; STAD, stomach adenocarcinoma dataset
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    <t>HOXA10</t> and BCL2 expressions were elevated in GC tissues. A and B, qRT‐PCR and western blot indicated that the expression of HOXA10 was higher in GC tissues (qRT‐PCR values were arranged from low to high). C, HOXA10 was elevated in the STAD reanalyzed from GEPIA. D, HOXA10 ranked fourth of the top 25 overexpressed genes in the STAD from UALCAN. E, Higher expression of HOXA10, BCL2 demonstrated lower overall survival rate in GC patients reanalyzed from the Kaplan‐Meier Plotter. F, Representative immunohistochemical staining showed that HOXA10, BCL2, and Ki67 were upregulated in GC tissues. Original magnification, 100× (200× for insert images). GC, gastric cancer; qRT‐PCR, quantitative real‐time polymerase chain reaction; STAD, stomach adenocarcinoma dataset
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    Primer Sequences for qPCR.

    Journal: Frontiers in Endocrinology

    Article Title: Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis

    doi: 10.3389/fendo.2022.928024

    Figure Lengend Snippet: Primer Sequences for qPCR.

    Article Snippet: Immunoblotting was performed with primary antibodies against IL33 (Proteintech, USA, 1:1000), HOXA10 (Cell Signaling Technology, USA, 1:1000), ITGB3 (Cell Signaling Technology, USA, 1:1000), STAT3 (Cell Signaling Technology, USA, 1:1000), p-STAT3 (Cell Signaling Technology, USA, 1:1000) or GAPDH (Bioworld Technology, USA, 1:10000), followed by incubation with a horseradish peroxidase (HRP)-conjugated secondary antibody.

    Techniques: Sequencing

    IL33 is aberrantly expressed in the endometria of women with adenomyosis. (A) IL33 and HOXA10 protein expression in normal (n = 20) and patients with adenomyosis (n = 20) was analyzed by Western blot. (B) The intensities of IL33 signals were quantified from the 20 samples and normalized. to GAPDH. ***p < 0.001. (C) The intensities of HOXA10 signals were quantified from the 20 samples and. normalized to GAPDH. **p < 0.01. (D) Correlation between IL33 and HOXA10 protein expression levels (r = 0.7788, p < 0.0001). (E) Timed mid-secretory endometrial biopsies from healthy control and infertile women with adenomyosis were analyzed using immunohistochemistry (IHC). Rabbit or Goat IgG was used as the negative control. The arrows show the decreased IL33 and HOXA10 conjugates in the endometrial epithelium cell. (F) The integrated optical densities (IOD) of the expression of IL33 and HOXA10 in the endometrium using Image-Pro Plus System 6.0 image analysis software. (G) The mean density of the expression of IL33 and HOXA10 in the endometrium. using Image-Pro Plus System 6.0 image analysis software.

    Journal: Frontiers in Endocrinology

    Article Title: Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis

    doi: 10.3389/fendo.2022.928024

    Figure Lengend Snippet: IL33 is aberrantly expressed in the endometria of women with adenomyosis. (A) IL33 and HOXA10 protein expression in normal (n = 20) and patients with adenomyosis (n = 20) was analyzed by Western blot. (B) The intensities of IL33 signals were quantified from the 20 samples and normalized. to GAPDH. ***p < 0.001. (C) The intensities of HOXA10 signals were quantified from the 20 samples and. normalized to GAPDH. **p < 0.01. (D) Correlation between IL33 and HOXA10 protein expression levels (r = 0.7788, p < 0.0001). (E) Timed mid-secretory endometrial biopsies from healthy control and infertile women with adenomyosis were analyzed using immunohistochemistry (IHC). Rabbit or Goat IgG was used as the negative control. The arrows show the decreased IL33 and HOXA10 conjugates in the endometrial epithelium cell. (F) The integrated optical densities (IOD) of the expression of IL33 and HOXA10 in the endometrium using Image-Pro Plus System 6.0 image analysis software. (G) The mean density of the expression of IL33 and HOXA10 in the endometrium. using Image-Pro Plus System 6.0 image analysis software.

    Article Snippet: Immunoblotting was performed with primary antibodies against IL33 (Proteintech, USA, 1:1000), HOXA10 (Cell Signaling Technology, USA, 1:1000), ITGB3 (Cell Signaling Technology, USA, 1:1000), STAT3 (Cell Signaling Technology, USA, 1:1000), p-STAT3 (Cell Signaling Technology, USA, 1:1000) or GAPDH (Bioworld Technology, USA, 1:10000), followed by incubation with a horseradish peroxidase (HRP)-conjugated secondary antibody.

    Techniques: Expressing, Western Blot, Immunohistochemistry, Negative Control, Software

    IL33 could induce HOXA10 expression. (A) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 mRNA levels were measured by qRT-PCR. ***p < 0.001. (B) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (C) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 and HOXA10 protein levels were measured by Western blot. (D) Ishikawa cells were transfected with si-IL33 or negative control. IL33 mRNA levels. were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (E) Ishikawa cells were transfected with si-IL33 or negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (F) Ishikawa cells were transfected with si-IL33 or negative control. IL33 and HOXA10 protein levels were measured by Western blot.

    Journal: Frontiers in Endocrinology

    Article Title: Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis

    doi: 10.3389/fendo.2022.928024

    Figure Lengend Snippet: IL33 could induce HOXA10 expression. (A) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 mRNA levels were measured by qRT-PCR. ***p < 0.001. (B) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (C) Ishikawa cells were transfected with overexpression plasmid Flag-IL33 or pcmv-Flag negative control. IL33 and HOXA10 protein levels were measured by Western blot. (D) Ishikawa cells were transfected with si-IL33 or negative control. IL33 mRNA levels. were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (E) Ishikawa cells were transfected with si-IL33 or negative control. HOXA10 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (F) Ishikawa cells were transfected with si-IL33 or negative control. IL33 and HOXA10 protein levels were measured by Western blot.

    Article Snippet: Immunoblotting was performed with primary antibodies against IL33 (Proteintech, USA, 1:1000), HOXA10 (Cell Signaling Technology, USA, 1:1000), ITGB3 (Cell Signaling Technology, USA, 1:1000), STAT3 (Cell Signaling Technology, USA, 1:1000), p-STAT3 (Cell Signaling Technology, USA, 1:1000) or GAPDH (Bioworld Technology, USA, 1:10000), followed by incubation with a horseradish peroxidase (HRP)-conjugated secondary antibody.

    Techniques: Expressing, Transfection, Over Expression, Plasmid Preparation, Negative Control, Quantitative RT-PCR, Western Blot

    IL33 participates in embryo implantation. (A) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. IL33 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (B) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (C) Protein levels were normalized to GAPDH protein expression level in (B) (**p< 0.01, ***p < 0.001. vs control). (D) Western blot analysis of uterine IL33 during the peri-implantation period in mice, with the strongest decreased signal detected at 4.5 dpc. (E) Protein levels were normalized to GAPDH protein expression level in (D) (**p< 0.01, ***p < 0.001. vs control, n is shown in each group). (F) Ishikawa cells were transfected with ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (G) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01. (H) Ishikawa cells were transfected with Flag-IL33 (2 μg) as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies.

    Journal: Frontiers in Endocrinology

    Article Title: Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis

    doi: 10.3389/fendo.2022.928024

    Figure Lengend Snippet: IL33 participates in embryo implantation. (A) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. IL33 mRNA levels were measured by qRT-PCR. **p < 0.01, ***p < 0.001. (B) Ishikawa cells were administered estrogen (10 –8 M) and progesterone (10 –6 M) at different times, as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (C) Protein levels were normalized to GAPDH protein expression level in (B) (**p< 0.01, ***p < 0.001. vs control). (D) Western blot analysis of uterine IL33 during the peri-implantation period in mice, with the strongest decreased signal detected at 4.5 dpc. (E) Protein levels were normalized to GAPDH protein expression level in (D) (**p< 0.01, ***p < 0.001. vs control, n is shown in each group). (F) Ishikawa cells were transfected with ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (G) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01. (H) Ishikawa cells were transfected with Flag-IL33 (2 μg) as indicated. Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies.

    Article Snippet: Immunoblotting was performed with primary antibodies against IL33 (Proteintech, USA, 1:1000), HOXA10 (Cell Signaling Technology, USA, 1:1000), ITGB3 (Cell Signaling Technology, USA, 1:1000), STAT3 (Cell Signaling Technology, USA, 1:1000), p-STAT3 (Cell Signaling Technology, USA, 1:1000) or GAPDH (Bioworld Technology, USA, 1:10000), followed by incubation with a horseradish peroxidase (HRP)-conjugated secondary antibody.

    Techniques: Quantitative RT-PCR, Western Blot, Expressing, Transfection, Luciferase, Co-Culture Assay

    ST2 silence dose not affect the IL33-promoted HOXA10 expression and embryo implantation in vitro. (A) Ishikawa cells were transfected with si-ST2 or negative control. ST2 mRNA levels were measured by qRT-PCR ** p < 0.01, *** p < 0.001. (B) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, IL33. was overexpression via the transfection of Flag-IL33. HOXA10 mRNA levels were measured by qRT-PCR. ** p < 0.01 (C) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg) were transfected into the cells, as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (D) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h. of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01.

    Journal: Frontiers in Endocrinology

    Article Title: Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis

    doi: 10.3389/fendo.2022.928024

    Figure Lengend Snippet: ST2 silence dose not affect the IL33-promoted HOXA10 expression and embryo implantation in vitro. (A) Ishikawa cells were transfected with si-ST2 or negative control. ST2 mRNA levels were measured by qRT-PCR ** p < 0.01, *** p < 0.001. (B) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, IL33. was overexpression via the transfection of Flag-IL33. HOXA10 mRNA levels were measured by qRT-PCR. ** p < 0.01 (C) Ishikawa cells were transfected with si-ST2 or negative control. After 24h, ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg) were transfected into the cells, as indicated. After 48 h, the luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05, **p < 0.01. (D) BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h. of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), **p < 0.01.

    Article Snippet: Immunoblotting was performed with primary antibodies against IL33 (Proteintech, USA, 1:1000), HOXA10 (Cell Signaling Technology, USA, 1:1000), ITGB3 (Cell Signaling Technology, USA, 1:1000), STAT3 (Cell Signaling Technology, USA, 1:1000), p-STAT3 (Cell Signaling Technology, USA, 1:1000) or GAPDH (Bioworld Technology, USA, 1:10000), followed by incubation with a horseradish peroxidase (HRP)-conjugated secondary antibody.

    Techniques: Expressing, In Vitro, Transfection, Negative Control, Quantitative RT-PCR, Over Expression, Luciferase, Co-Culture Assay

    IL-33 enhances embryo implantation via phosphorylation of STAT3. (A) Ishikawa cells were transfected with Flag-IL33 (2 μg). IL33, STAT3 and p-STAT3 protein levels were analyzed by western blot analysis. (B) Ishikawa cells were transfected with siIL33 (50 or 100 nM), Whole-cell lysates. were analyzed by western blot analysis with the indicated antibodies. (C) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of Flag-IL33 (2 μg), Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (D) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. The luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05. (E) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before the. transfection of Flag-IL33 (2 μg). BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), *p < 0.05.

    Journal: Frontiers in Endocrinology

    Article Title: Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis

    doi: 10.3389/fendo.2022.928024

    Figure Lengend Snippet: IL-33 enhances embryo implantation via phosphorylation of STAT3. (A) Ishikawa cells were transfected with Flag-IL33 (2 μg). IL33, STAT3 and p-STAT3 protein levels were analyzed by western blot analysis. (B) Ishikawa cells were transfected with siIL33 (50 or 100 nM), Whole-cell lysates. were analyzed by western blot analysis with the indicated antibodies. (C) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of Flag-IL33 (2 μg), Whole-cell lysates were analyzed by western blot analysis with the indicated antibodies. (D) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before. the transfection of ITGB3-Luc, Myc-HOXA10 (2 μg), and Flag-IL33 (2 μg), as indicated. The luciferase activities were measured and are presented as fold induction. Values represent the mean ± SEM (n = 3), *p < 0.05. (E) Ishikawa cells were administrated with cryptotanshinone (4.6 μM) for 8h before the. transfection of Flag-IL33 (2 μg). BeWo spheroids (150–200 μm diameter) were attached to Ishikawa cells after 2 h of co-culture. Adhesion experiments with BeWo spheroids attached to the Ishikawa cell monolayer. The data are the average of three independent experiments. An ANOVA test was used to compare the percentage of the attached spheroids with each treatment in comparison to the control. The error bars indicate SD of three independent experiments. Values represent the mean ± SEM (n = 3), *p < 0.05.

    Article Snippet: Immunoblotting was performed with primary antibodies against IL33 (Proteintech, USA, 1:1000), HOXA10 (Cell Signaling Technology, USA, 1:1000), ITGB3 (Cell Signaling Technology, USA, 1:1000), STAT3 (Cell Signaling Technology, USA, 1:1000), p-STAT3 (Cell Signaling Technology, USA, 1:1000) or GAPDH (Bioworld Technology, USA, 1:10000), followed by incubation with a horseradish peroxidase (HRP)-conjugated secondary antibody.

    Techniques: Transfection, Western Blot, Luciferase, Co-Culture Assay

    IL33 expression is decreased in a mouse model of adenomyosis. (A) HE staining confirmed that the mouse model of adenomyosis was successfully constructed. (B) Uterus from control mouse and adenomyosis mouse model were analyzed using immunohistochemistry (IHC). Rabbit IgG was used as the negative control. The arrows show the decreased IL33 conjugates in the endometrial cell epithelium. (C) IL33 and HOXA10 protein expression in control (n =10) and mouse with adenomyosis (n=10) was analyzed by Western blot. (D) The intensities of IL33 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (E) The intensities of HOXA10 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (F) Correlation between IL33 and HOXA10 protein expression levels (r = 0.8151, p < 0.0001).

    Journal: Frontiers in Endocrinology

    Article Title: Decreased intracellular IL-33 impairs endometrial receptivity in women with adenomyosis

    doi: 10.3389/fendo.2022.928024

    Figure Lengend Snippet: IL33 expression is decreased in a mouse model of adenomyosis. (A) HE staining confirmed that the mouse model of adenomyosis was successfully constructed. (B) Uterus from control mouse and adenomyosis mouse model were analyzed using immunohistochemistry (IHC). Rabbit IgG was used as the negative control. The arrows show the decreased IL33 conjugates in the endometrial cell epithelium. (C) IL33 and HOXA10 protein expression in control (n =10) and mouse with adenomyosis (n=10) was analyzed by Western blot. (D) The intensities of IL33 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (E) The intensities of HOXA10 signals were quantified from the 10 samples and normalized to GAPDH. **p < 0.01. (F) Correlation between IL33 and HOXA10 protein expression levels (r = 0.8151, p < 0.0001).

    Article Snippet: Immunoblotting was performed with primary antibodies against IL33 (Proteintech, USA, 1:1000), HOXA10 (Cell Signaling Technology, USA, 1:1000), ITGB3 (Cell Signaling Technology, USA, 1:1000), STAT3 (Cell Signaling Technology, USA, 1:1000), p-STAT3 (Cell Signaling Technology, USA, 1:1000) or GAPDH (Bioworld Technology, USA, 1:10000), followed by incubation with a horseradish peroxidase (HRP)-conjugated secondary antibody.

    Techniques: Expressing, Staining, Construct, Immunohistochemistry, Negative Control, Western Blot

    HOXA10 and BCL2 expressions were elevated in GC tissues. A and B, qRT‐PCR and western blot indicated that the expression of HOXA10 was higher in GC tissues (qRT‐PCR values were arranged from low to high). C, HOXA10 was elevated in the STAD reanalyzed from GEPIA. D, HOXA10 ranked fourth of the top 25 overexpressed genes in the STAD from UALCAN. E, Higher expression of HOXA10, BCL2 demonstrated lower overall survival rate in GC patients reanalyzed from the Kaplan‐Meier Plotter. F, Representative immunohistochemical staining showed that HOXA10, BCL2, and Ki67 were upregulated in GC tissues. Original magnification, 100× (200× for insert images). GC, gastric cancer; qRT‐PCR, quantitative real‐time polymerase chain reaction; STAD, stomach adenocarcinoma dataset

    Journal: Cancer Medicine

    Article Title: HOXA10 induces BCL2 expression, inhibits apoptosis, and promotes cell proliferation in gastric cancer

    doi: 10.1002/cam4.2440

    Figure Lengend Snippet: HOXA10 and BCL2 expressions were elevated in GC tissues. A and B, qRT‐PCR and western blot indicated that the expression of HOXA10 was higher in GC tissues (qRT‐PCR values were arranged from low to high). C, HOXA10 was elevated in the STAD reanalyzed from GEPIA. D, HOXA10 ranked fourth of the top 25 overexpressed genes in the STAD from UALCAN. E, Higher expression of HOXA10, BCL2 demonstrated lower overall survival rate in GC patients reanalyzed from the Kaplan‐Meier Plotter. F, Representative immunohistochemical staining showed that HOXA10, BCL2, and Ki67 were upregulated in GC tissues. Original magnification, 100× (200× for insert images). GC, gastric cancer; qRT‐PCR, quantitative real‐time polymerase chain reaction; STAD, stomach adenocarcinoma dataset

    Article Snippet: Chromatin solutions were, respectively, incubated with antibodies anti‐HOXA10 (Santa Cruz, USA), anti‐Histone H3, and anti‐normal rabbit IgG (CST, USA).

    Techniques: Quantitative RT-PCR, Western Blot, Expressing, Immunohistochemical staining, Staining, Real-time Polymerase Chain Reaction

    HOXA10 promoted proliferation and repressed apoptosis in GC cells. A and B, The CCK‐8 assay showed that HOXA10 knockdown inhibited cell growth but could be partly rescued by transfecting with BCL2‐overexpressing plasmid. And, HOXA10 overexpression promoted cell growth but could be partially impaired with treatment of BCL2 selective inhibitor ABT‐199. C and D, HOXA10 knockdown inhibited colony formation in BGC‐823 cells while HOXA10 overexpression enhanced colony formation in AGS and HGC‐27 cells. E and F, The cell apoptosis assay showed the percentage of apoptotic cells was higher in HOXA10‐knockdown cells (BGC‐823‐sh‐HOXA10, NCI‐N87‐sh‐HOXA10) compared with the control cells, but could be partly reduced by transfecting with BCL2‐overexpressing plasmid. And, the portion of apoptotic cells was lower in HOXA10‐overexpressinig cells (AGS‐HOXA10‐OV, HGC‐27‐HOXA10‐OV) compared with the corresponding control cells, but could be partially rescued with treatment of ABT‐199. ** P < .01, *** P < .001. CCK‐8, cell counting kit‐8. GC, gastric cancer

    Journal: Cancer Medicine

    Article Title: HOXA10 induces BCL2 expression, inhibits apoptosis, and promotes cell proliferation in gastric cancer

    doi: 10.1002/cam4.2440

    Figure Lengend Snippet: HOXA10 promoted proliferation and repressed apoptosis in GC cells. A and B, The CCK‐8 assay showed that HOXA10 knockdown inhibited cell growth but could be partly rescued by transfecting with BCL2‐overexpressing plasmid. And, HOXA10 overexpression promoted cell growth but could be partially impaired with treatment of BCL2 selective inhibitor ABT‐199. C and D, HOXA10 knockdown inhibited colony formation in BGC‐823 cells while HOXA10 overexpression enhanced colony formation in AGS and HGC‐27 cells. E and F, The cell apoptosis assay showed the percentage of apoptotic cells was higher in HOXA10‐knockdown cells (BGC‐823‐sh‐HOXA10, NCI‐N87‐sh‐HOXA10) compared with the control cells, but could be partly reduced by transfecting with BCL2‐overexpressing plasmid. And, the portion of apoptotic cells was lower in HOXA10‐overexpressinig cells (AGS‐HOXA10‐OV, HGC‐27‐HOXA10‐OV) compared with the corresponding control cells, but could be partially rescued with treatment of ABT‐199. ** P < .01, *** P < .001. CCK‐8, cell counting kit‐8. GC, gastric cancer

    Article Snippet: Chromatin solutions were, respectively, incubated with antibodies anti‐HOXA10 (Santa Cruz, USA), anti‐Histone H3, and anti‐normal rabbit IgG (CST, USA).

    Techniques: CCK-8 Assay, Plasmid Preparation, Over Expression, Apoptosis Assay, Cell Counting

    HOXA10 promoted tumor growth in the nude mice xenograft tumor formation assay. A, Tumors formed by AGS‐HOXA10‐OV cells demonstrated an elevation of bioluminescent signal. B‐D, The weight and volume of tumors formed by AGS cells in different groups. HOXA10 overexpression promoted xenograft tumor growth in nude mice. E‐H, The weight and volume of tumors formed by NCI‐N87 cells showed HOXA10 knockdown inhibited xenograft tumor growth in nude mice. I and J, Representative immunohistochemical staining of HOXA10, BCL2, and Ki67 in xenograft tumors. Original magnification, 200×. * P < .05

    Journal: Cancer Medicine

    Article Title: HOXA10 induces BCL2 expression, inhibits apoptosis, and promotes cell proliferation in gastric cancer

    doi: 10.1002/cam4.2440

    Figure Lengend Snippet: HOXA10 promoted tumor growth in the nude mice xenograft tumor formation assay. A, Tumors formed by AGS‐HOXA10‐OV cells demonstrated an elevation of bioluminescent signal. B‐D, The weight and volume of tumors formed by AGS cells in different groups. HOXA10 overexpression promoted xenograft tumor growth in nude mice. E‐H, The weight and volume of tumors formed by NCI‐N87 cells showed HOXA10 knockdown inhibited xenograft tumor growth in nude mice. I and J, Representative immunohistochemical staining of HOXA10, BCL2, and Ki67 in xenograft tumors. Original magnification, 200×. * P < .05

    Article Snippet: Chromatin solutions were, respectively, incubated with antibodies anti‐HOXA10 (Santa Cruz, USA), anti‐Histone H3, and anti‐normal rabbit IgG (CST, USA).

    Techniques: Tube Formation Assay, Over Expression, Immunohistochemical staining, Staining

    The bioinformatics analysis, qRT‐PCR, western blot, and ChIP‐qPCR assay revealed that HOXA10 might induce BCL2 expression via binding to its promoter region. A, The “TF‐gene interactions” analysis of HOXA10 and BCL2 in the database NetworkAnalyst. B, A PPI network was built between HOXA10 and BCL2 with the database STRING. C, qRT‐PCR showed the relative BCL2 mRNA level in different cells with changed HOXA10 expression. D, Expression of BCL2, Bax, cleaved forms of Caspase‐9, Caspase‐3, and PARP in different GC cells with altered HOXA10 expression. E, HOXA10 binding motif acquired from JASPAR and the relative primer position within the BCL2 promoter region. F, ChIP‐qPCR assay indicated the possible positive HOXA10 binding sites across the BCL2 promoter region. G, 3% agarose gel electrophoresis of ChIP‐qPCR products. ** P < .01, *** P < .001. ChIP‐qPCR, chromatin immunoprecipitation and quantitative PCR; PPI, protein‐protein interaction; qRT‐PCR, quantitative real‐time polymerase chain reaction; TF‐gene, transcription factor‐gene

    Journal: Cancer Medicine

    Article Title: HOXA10 induces BCL2 expression, inhibits apoptosis, and promotes cell proliferation in gastric cancer

    doi: 10.1002/cam4.2440

    Figure Lengend Snippet: The bioinformatics analysis, qRT‐PCR, western blot, and ChIP‐qPCR assay revealed that HOXA10 might induce BCL2 expression via binding to its promoter region. A, The “TF‐gene interactions” analysis of HOXA10 and BCL2 in the database NetworkAnalyst. B, A PPI network was built between HOXA10 and BCL2 with the database STRING. C, qRT‐PCR showed the relative BCL2 mRNA level in different cells with changed HOXA10 expression. D, Expression of BCL2, Bax, cleaved forms of Caspase‐9, Caspase‐3, and PARP in different GC cells with altered HOXA10 expression. E, HOXA10 binding motif acquired from JASPAR and the relative primer position within the BCL2 promoter region. F, ChIP‐qPCR assay indicated the possible positive HOXA10 binding sites across the BCL2 promoter region. G, 3% agarose gel electrophoresis of ChIP‐qPCR products. ** P < .01, *** P < .001. ChIP‐qPCR, chromatin immunoprecipitation and quantitative PCR; PPI, protein‐protein interaction; qRT‐PCR, quantitative real‐time polymerase chain reaction; TF‐gene, transcription factor‐gene

    Article Snippet: Chromatin solutions were, respectively, incubated with antibodies anti‐HOXA10 (Santa Cruz, USA), anti‐Histone H3, and anti‐normal rabbit IgG (CST, USA).

    Techniques: Quantitative RT-PCR, Western Blot, Expressing, Binding Assay, Agarose Gel Electrophoresis, Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction