Journal: Translational Oncology

Article Title: Downregulation of PIP4K2C inhibits the breast cancer cell proliferation, migration and invasion

doi: 10.1016/j.tranon.2025.102420

Figure Lengend Snippet: The mRNA expression of PIP4K2C in pan-cancer. (A) The mRNA expression of PIP4K2C in 33 tumors in TCGA GTEx samples (ns, p > 0.05; * p < 0.05; ** p < 0.01; *** p < 0.001). (B) PIP4K2C expression in the breast cancer tissues and unpaired normal samples. (C) The expression level of PIP4K2C in the breast cancer tissues and the paired normal samples. ACC, adrenocortical carcinoma; BLCA, bladder urothelial carcinoma; BRCA, breast invasive carcinoma; CESC, cervical and endocervical cancers; CHOL, cholangiocarcinoma; COAD, colon adenocarcinoma; DLBC, lymphoid neoplasm diffuse large B-cell lymphoma; ESCA, esophageal carcinoma; GBM, glioblastoma multiforme; HNSC, head and neck squamous cell carcinoma; KICH, kidney chromophobe; KIRC, kidney renal clear cell carcinoma; KIRP, kidney renal papillary cell carcinoma; LAML, acute myeloid leukemia; LGG, brain lower grade glioma; LIHC, liver hepatocellular carcinoma; LUAD, lung adenocarcinoma; LUSC, lung squamous cell carcinoma; MESO, mesothelioma; OV, ovarian serous cystadenocarcinoma; PAAD, pancreatic adenocarcinoma; PCPG, pheochromocytoma and paraganglioma; PRAD, prostate adenocarcinoma; READ, rectum adenocarcinoma; SARC, sarcoma; SKCM, skin cutaneous melanoma; STAD, stomach adenocarcinoma; STES, stomach and esophageal carcinoma; TGCT, testicular germ cell tumors; THCA, thyroid carcinoma; THYM, thymoma; UCEC, uterine corpus endometrial carcinoma; UCS, uterine carcinosarcoma; UVM, uveal melanoma.

Article Snippet: In this assay, primary antibody PIP4K2C (1:100, CUSABIO, CSB-PA819455LA01HU) and secondary antibodies Goat anti-rabbit IgG H&L (Alexa Fluor® 488) (1:400, abcam, ab150077) were used.

Techniques: Expressing

Journal: Translational Oncology

Article Title: Downregulation of PIP4K2C inhibits the breast cancer cell proliferation, migration and invasion

doi: 10.1016/j.tranon.2025.102420

Figure Lengend Snippet: mRNA expression and protein levels of PIP4K2C in breast cancer cell lines and tissues. (A) The expression level of PIP4K2C in the normal mammary gland cell line MCF-10A and breast cancer cell lines (MDA-MB-231, MDA-MB-468, MCF7, ZR751 and BT20) was determined using qPCR. * P < 0.05, *** P < 0.01 vs MCF-10A. (B) The protein levels of PIP4K2C in cell lines were measured by western blot. (C) The expression level of PIP4K2C in the breast cancer tissues and the paired normal samples. (D) The protein levels of PIP4K2C in the breast cancer tissues and the paired normal samples. (E) The immunofluorescence staining of the breast cancer tissues and the paired normal samples. (F) The IHC images of PIP4K2C in normal and tumor tissues.

Article Snippet: In this assay, primary antibody PIP4K2C (1:100, CUSABIO, CSB-PA819455LA01HU) and secondary antibodies Goat anti-rabbit IgG H&L (Alexa Fluor® 488) (1:400, abcam, ab150077) were used.

Techniques: Expressing, Western Blot, Immunofluorescence, Staining

Journal: Translational Oncology

Article Title: Downregulation of PIP4K2C inhibits the breast cancer cell proliferation, migration and invasion

doi: 10.1016/j.tranon.2025.102420

Figure Lengend Snippet: PIP4K2C was knocked down by siRNA. (A-B) The transfection efficiency of MDA-MB-468 was detected at mRNA expression and protein levels, respectively. (C-D) The transfection efficiency of MCF7 was detected at mRNA expression and protein levels (48 h), respectively.

Article Snippet: In this assay, primary antibody PIP4K2C (1:100, CUSABIO, CSB-PA819455LA01HU) and secondary antibodies Goat anti-rabbit IgG H&L (Alexa Fluor® 488) (1:400, abcam, ab150077) were used.

Techniques: Transfection, Expressing

Journal: Translational Oncology

Article Title: Downregulation of PIP4K2C inhibits the breast cancer cell proliferation, migration and invasion

doi: 10.1016/j.tranon.2025.102420

Figure Lengend Snippet: PIP4K2C was overexpressed in MCF 10A by transfection. (A) The transfection efficiency was detected at mRNA expression. (B) overexpression of PIP4K2C resulted in increased proliferation.

Article Snippet: In this assay, primary antibody PIP4K2C (1:100, CUSABIO, CSB-PA819455LA01HU) and secondary antibodies Goat anti-rabbit IgG H&L (Alexa Fluor® 488) (1:400, abcam, ab150077) were used.

Techniques: Transfection, Expressing, Over Expression

Journal: Translational Oncology

Article Title: Downregulation of PIP4K2C inhibits the breast cancer cell proliferation, migration and invasion

doi: 10.1016/j.tranon.2025.102420

Figure Lengend Snippet: Inhibition of PIP4K2C suppressed the proliferation, migration and invasion of MDA-MB-468 and MCF7 cells. (A) Knockdown of PIP4K2C by siRNA resulted in reduced proliferation. (B) The reduced cell migration rate was evaluated by wound healing assay. The percentage of wound closure at 24 and 48 h was calculated using ImageJ based on the change in scratch area from time 0 h. (C-D) The cell migration and invasion ability were detected by transwell assay.

Article Snippet: In this assay, primary antibody PIP4K2C (1:100, CUSABIO, CSB-PA819455LA01HU) and secondary antibodies Goat anti-rabbit IgG H&L (Alexa Fluor® 488) (1:400, abcam, ab150077) were used.

Techniques: Inhibition, Migration, Knockdown, Wound Healing Assay, Transwell Assay

Journal: Translational Oncology

Article Title: Downregulation of PIP4K2C inhibits the breast cancer cell proliferation, migration and invasion

doi: 10.1016/j.tranon.2025.102420

Figure Lengend Snippet: Down-regulation of PIP4K2C enhanced the protein levels of LC3II/LC3I.

Article Snippet: In this assay, primary antibody PIP4K2C (1:100, CUSABIO, CSB-PA819455LA01HU) and secondary antibodies Goat anti-rabbit IgG H&L (Alexa Fluor® 488) (1:400, abcam, ab150077) were used.

Techniques:

Journal: Advanced Science

Article Title: Serine/Threonine Kinase 33 as a Novel Target of Bufalin in Treatment of Triple‐Negative Breast Cancer

doi: 10.1002/advs.202506253

Figure Lengend Snippet: STK33 promotes TNBC cell proliferation by increasing the protein stability of CCAR1. A) The proteins immunoprecipitated by anti‐Flag antibody were analyzed by mass spectrometry, and the number of peptides for each protein identified was listed. B) 293T cells were transfected with Flag‐STK33 and HA‐CCAR1 plasmids, and then subjected to immunoprecipitation with anti‐Flag or anti‐HA antibodies. The lysates and immunoprecipitates were then blotted. C) MDA‐MB‐231 cells were transfected with an HA‐CCAR1 plasmid, and immunofluorescence staining was performed to detect the localization of HA (red) and STK33 (green) within the cells. D) The expression of STK33 and CCAR1 in MDA‐MB‐231 xenograft were measured by western blot. E) MDA‐MB‐231 and HCC1806 cells were transfected with STK33 siRNA or non‐targeting siRNA, and the expression of STK33 and CCAR1 was measured by western blot. F) 293T cells were transfected with Flag‐STK33 and HA‐CCAR1, and then subjected to immunoprecipitation with anti‐HA antibody, and the phosphorylation of CCAR1 was measured by western blot using p‐Ser/Thr antibody. G) MDA‐MB‐231 and HCC1806 cells were transfected with STK33 siRNA, followed by treatment with 10 µ m MG132 for 4h before harvest. The expression of STK33 and CCAR1 was measured by western blot. H) MDA‐MB‐231 cells were transfected with STK33 siRNA or non‐targeting siRNA, and followed treated with 10µg mL −1 of cycloheximide (CHX) and harvested at the indicated time points. The protein levels of CCAR1 and STK33 were detected by western blot. I) 293T cells were transfected with HA‐CCAR1, MYC‐Ub, or Flag‐STK33 plasmids, followed by treatment with MG132 (10 µ m ) for 10 h before harvest. Then the cell lysates were subjected to immunoprecipitation with anti‐HA antibody and blotted with anti‐MYC antibody. J) MDA‐MB‐231 cells were transfected with STK33 siRNA, and then transfected with HA‐CCAR1, the expression of STK33 and HA was measured by western blot. K) MDA‐MB‐231 cells were transfected with STK33 siRNA, and then transfected with HA‐CCAR1, and cell proliferation was measured by the colony formation assay. The data are presented as mean ± SD of three independent experiments. One‐way ANOVA was used to determine statistical significance, *** P < 0.001, **** P < 0.0001.

Article Snippet: The CCAR1 antibody (CSB‐PA816898ESR1HU) was purchased from CUSABIO (https://www.cusabio.com/).

Techniques: Immunoprecipitation, Mass Spectrometry, Transfection, Plasmid Preparation, Immunofluorescence, Staining, Expressing, Western Blot, Phospho-proteomics, Colony Assay

Journal: Advanced Science

Article Title: Serine/Threonine Kinase 33 as a Novel Target of Bufalin in Treatment of Triple‐Negative Breast Cancer

doi: 10.1002/advs.202506253

Figure Lengend Snippet: High expression of the STK33‐CCAR1 axis is correlated with poor survival in patients with TNBC. A) Representative IHC staining for STK33 and CCAR1 in TNBC. Cases 1 and 2 are representative of a patient with STK33‐high TNBC. Cases 3 and 4 are representative of a patient with STK33‐low TNBC. B, C) Pearson's correlation analyses of STK33 and CCAR1. D) IHC analyses of STK33 and CCAR1 levels in breast cancer tissues from the Human Protein Atlas database (https://www.proteinatlas.org/). E) Pearson's correlation analyses of STK33 and CCAR1 mRNA levels in liver hepatocellular carcinoma from the TIMER web server (https://cistrome.shinyapps.io/timer/). F) Pearson's correlation analyses of STK33 and CCAR1 mRNA levels in diffuse large B‐cell lymphoma from the TIMER web server (https://cistrome.shinyapps.io/timer/). G) The correlation between STK33 expression and the histology grade in TNBC patients, the data are presented as mean ± SD, one‐way ANOVA was used to determine statistical significance, P < 0.05 was considered to be statistically significant. H) The correlation between CCAR1 expression and the histology grade in TNBC patients, the data are presented as mean ± SD, one‐way ANOVA was used to determine statistical significance, P < 0.05 was considered to be statistically significant. I) Kaplan–Meier plots of the overall survival based on CCAR1 expression in TNBC patients. J) Kaplan–Meier curves of overall survival based on STK33 and CCAR1 expression in TNBC patients.

Article Snippet: The CCAR1 antibody (CSB‐PA816898ESR1HU) was purchased from CUSABIO (https://www.cusabio.com/).

Techniques: Expressing, Immunohistochemistry

Journal: Advanced Science

Article Title: Serine/Threonine Kinase 33 as a Novel Target of Bufalin in Treatment of Triple‐Negative Breast Cancer

doi: 10.1002/advs.202506253

Figure Lengend Snippet: Bufalin exerts anti‐cancer activity in animal TNBC model and in patient‐derived TNBC organoids. 4‐week‐old female nude mice were inoculated with MDA‐MB‐231 cells. The tumor‐bearing mice were subsequently given the indicated treatment. A) Subcutaneous tumors were excised and photographed at the end of the experiment. B) Tumor sizes were measured on the specified days, and the data are presented as mean ± SD of 7 mice. One‐way ANOVA was used to determine statistical significance; P < 0.05 was considered to be statistically significant. C) Tumor weights were measured at the end of the experiments, and the data are presented as mean ± SD of 7 mice. One‐way ANOVA was used to determine statistical significance; P < 0.05 was considered to be statistically significant. D) Representative immunohistostaining images for detecting Ki67 expression in the tumor specimens. E) Representative immunohistostaining images for detecting STK33 expression in the tumor specimens. F) Western blot analysis of the STK33 and CCAR1 protein expression in xenograft tumors following the indicated treatment. G) Mice liver functions were measured at the end of the experiments, and the data are presented as mean ± SD of 7 mice. One‐way ANOVA was used to determine statistical significance, ns, P > 0.05. ALT, alanine aminotransferase; AST, aspartate aminotransferase. H) Mice kidney functions were measured at the end of the experiments, and the data are presented as mean ± SD of 7 mice. One‐way ANOVA was used to determine statistical significance, ns, P > 0.05. BUN, blood urea nitrogen. I) Representative images of TNBC patient‐derived organoids (Scale bar 50µm). J–L) The proliferation curve of TNBC PDOs treated with Bufalin, the data are presented as mean ± SD of three independent experiments. One‐way ANOVA was used to determine statistical significance; P < 0.05 was considered to be statistically significant. M) Spearman correlation analysis between STK33 expression and the IC 50 of TNBC PDOs.

Article Snippet: The CCAR1 antibody (CSB‐PA816898ESR1HU) was purchased from CUSABIO (https://www.cusabio.com/).

Techniques: Activity Assay, Derivative Assay, Expressing, Western Blot

Journal: Advanced Science

Article Title: Serine/Threonine Kinase 33 as a Novel Target of Bufalin in Treatment of Triple‐Negative Breast Cancer

doi: 10.1002/advs.202506253

Figure Lengend Snippet: Regulatory signaling pathway of Bufalin in TNBC. In this study, we identified STK33 as a putative target of Bufalin. Bufalin disrupts the interaction between STK33 and HSP90, thereby promoting the ubiquitination and proteasomal degradation of STK33. Furthermore, STK33 is highly expressed in TNBC and enhances TNBC cell proliferation by phosphorylating and stabilizing CCAR1. Targeted degradation of STK33 by Bufalin significantly inhibits TNBC growth, highlighting its potential as a promising therapeutic candidate for TNBC treatment. Created in BioRender. Jiang, S. (2025) https://BioRender.com/00nde1g .

Article Snippet: The CCAR1 antibody (CSB‐PA816898ESR1HU) was purchased from CUSABIO (https://www.cusabio.com/).

Techniques: Ubiquitin Proteomics

Journal: International Journal of Molecular Sciences

Article Title: Canonical and Non-Canonical Localization of Tight Junction Proteins during Early Murine Cranial Development

doi: 10.3390/ijms25031426

Figure Lengend Snippet: ZO-1 shows the strongest expression on the apical surface of the mouse neuroepithelium. ( A ): Confocal images show a representative coronal section of mouse cranial neural folds with immunofluorescence co-staining detecting ZO-1 (yellow) and integrin alpha 4 (ITGA4, magenta) at embryonic stage E 8.5 (9 somites, 9s). The overlay image of all channels (merge) is shown at the top of panel ( A ), followed below by the individual channel images, showing the signals for ITGA4 (magenta) and ZO-1 (yellow). Nuclei are stained with DAPI (cyan). Scale bar: 50 µm. Immunofluorescence staining for ITGA4 was performed to label the basolateral cellular domains. ZO-1 showed the strongest signals in the neuroectoderm (NE) and less strong signals in the non-neuronal ectoderm (NNE) and the mesenchymal cells, underlying the neuronal ectoderm. ( A′ ): Higher magnification of boxed area in ( A ). The overlay image of all channels is shown at the top of panel ( A′ ), followed below by the individual channel image, showing the signals for ZO-1 (yellow). Scale bar: 5 µm. ZO-1 was localized to the apical cell–cell junctions. ( B ): Confocal images show representative coronal section of mouse cranial neural folds with immunofluorescence co-staining detecting ZO-1 (yellow) and ITGA4 (magenta) at embryonic stage E 9.0 (13 somites, 13s). The overlay image of all channels is shown at the left of panel ( B ), followed to the right by the individual channel images, showing the signals for ITGA4 (magenta) and ZO-1 (yellow). Nuclei are stained with DAPI (cyan). Scale bar: 50 µm. ZO-1 showed the strongest signals in the neuroectoderm (NE) and less strong signals in the non-neuronal ectoderm (NNE) and mesenchymal cells. ( C ): E 8.0 whole-mount mouse embryos (6 somites, 6s) were immunofluorescence co-labelled for ZO-1 (yellow) and ITGA4 (magenta). The overlay image of both channels is shown at the top of panel ( C ), followed below by the individual channel image showing the signals for ZO-1 (yellow). The frontal view on the whole-mount forebrains, imaged using confocal microscopy, is shown. Scale bar: 50 µm. ( C′ ): Magnification of boxed area indicated in ( C ) with merged-channel image at the top, showing ITGA4 (magenta) and ZO-1 (yellow) signals and ZO-1 single-channel image below. Scale bar: 10 µm.

Article Snippet: Rabbit ITGA4 , Cusabio, Houston TX, USA, CSB-PA011867LA01HU , 1:200.

Techniques: Expressing, Immunofluorescence, Staining, Confocal Microscopy

Journal: International Journal of Molecular Sciences

Article Title: Canonical and Non-Canonical Localization of Tight Junction Proteins during Early Murine Cranial Development

doi: 10.3390/ijms25031426

Figure Lengend Snippet: List of antibodies.

Article Snippet: Rabbit ITGA4 , Cusabio, Houston TX, USA, CSB-PA011867LA01HU , 1:200.

Techniques:

Journal: bioRxiv

Article Title: TFIIB-related factor 1 is a nucleolar protein that promotes RNA polymerase I-directed transcription and tumour cell growth

doi: 10.1101/2022.02.20.481212

Figure Lengend Snippet: (A) BRF1 and TIF-1A were co-localized in the nucleoli of HeLa cells. IF staining was performed using the BRF1 and TIF-1A antibodies. The scale bar in each image represents 2.5 μm. ( B ) BRF1 and RPA40 were co-localized in the nucleoli of HeLa cells. IF staining was performed using BRF1 antibody and RPA40 antibody. The scale bar in each image represents 2.5 μm. ( C ) The co-localization analysis between BRF1 and TIF-1A using the nucleolar particles purified from HeLa cells. The scale bar in each image represents 2.5 μm. ( D ) The co-localization analysis between BRF1 and RPA43 using the nucleoli particles purified from HeLa cells. The scale bar in each image represents 5 μm. ( E ) Components of the Pol I transcription machinery could be precipitated by the BRF1 antibody. HeLa nuclear extract was prepared and used for BRF1 IP assays. BRF1-binding proteins in the IP samples were detected by Western blot using the antibodies as indicated in the panel. ( F , G ) BRF1 could be precipitated by the antibodies against Pol I-related proteins. IP assays were performed with the antibodies against TBP, TIF-1A, TAF1A, UBF, and RPA43, respectively. BRF1 ( F ) and proteins as indicated ( G ) were detected by Western blot. Figure 6-figure supplement 1. The co-localization analysis between BRF1 and Pol III transcription factors in HeLa cells. Figure 6-figure supplement 2. BRF1 binds to TFIIIC subunit GTF3C2 and SL1 subunit TAF1B. Figure 6-source data, Figure 6-figure supplement 2-source data

Article Snippet: IP assays were performed using normal IgG, BRF1 antibody and the antibodies against UBF (ab244287, Abcam), TIF-1A (ab251933, Abcam), TBP (ab28175, abcam), TAF1A (SC-393600, Santa Cruz Biotech), GTF3C2 (SC-81406, Santa Cruz Biotech), TAF1B (CSB-PA684476ESR1HU, CUSABio) and RPA43 (Ab99305, Abcam), respectively.

Techniques: Staining, Purification, Binding Assay, Western Blot

Journal: bioRxiv

Article Title: TFIIB-related factor 1 is a nucleolar protein that promotes RNA polymerase I-directed transcription and tumour cell growth

doi: 10.1101/2022.02.20.481212

Figure Lengend Snippet: (A) BRF1 IP results showing BRF1 association with GTF3C2 and TAF1B. IP assays were performed using BRF1 antibody and HeLa nuclear extract. BRF1-bound protein was detected by Western blot using the antibodies as indicated. ( B ) GTF3C2 IP result showing GT3C2 association with BRF1. IP assays were performed using GTF3C2 antibody and HeLa nuclear extract. GTF3C2-bound protein was detected by Western blot using the antibodies as indicated. ( C ) TAF1B IP result showing TAF1B association with BRF1. IP assays were performed using TAF1B antibody and HeLa nuclear extract. TAF1B-bound protein was detected by Western blot using the antibodies as indicated.

Article Snippet: IP assays were performed using normal IgG, BRF1 antibody and the antibodies against UBF (ab244287, Abcam), TIF-1A (ab251933, Abcam), TBP (ab28175, abcam), TAF1A (SC-393600, Santa Cruz Biotech), GTF3C2 (SC-81406, Santa Cruz Biotech), TAF1B (CSB-PA684476ESR1HU, CUSABio) and RPA43 (Ab99305, Abcam), respectively.

Techniques: Western Blot

Journal: Journal of Cancer

Article Title: PRMT7 Inhibits the Proliferation and Migration of Gastric Cancer Cells by Suppressing the PI3K/AKT Pathway via PTEN.

doi: 10.7150/jca.88102

Figure Lengend Snippet: Figure 1. PRMT7 is expressed at low levels in gastric cancer tissues. A Immunohistochemical analyses were performed to observe PRMT7 expression in gastric cancer: a) normal gastric tissue; b) high-medium differentiated gastric cancer tissue; c) poorly differentiated gastric cancer tissue. B Western blot analysis of PRMT7 protein expression levels in 30 paired gastric cancer tissues and adjacent normal mucosal tissues. N: normal mucosa adjacent to cancer; T: tumor tissue. C PRMT7 expression in the GES-1 cell line and various gastric cancer cell lines. ***P < 0.001.

Article Snippet: Sections were incubated with rabbit anti-Homo sapiens (Human) PRMT7 polyclonal antibody (CSB-PA885738LA01HU, CUSABIO, Wuhan, China) at 1:100 dilution overnight at 4°C followed by a goat anti-rabbit/mouse secondary antibody.

Techniques: Immunohistochemical staining, Expressing, Western Blot

Journal: Journal of Cancer

Article Title: PRMT7 Inhibits the Proliferation and Migration of Gastric Cancer Cells by Suppressing the PI3K/AKT Pathway via PTEN.

doi: 10.7150/jca.88102

Figure Lengend Snippet: Figure 2. PRMT7 inhibited gastric cancer cell proliferation and migration. A The knockdown and overexpression efficiency of the PRMT7 was detected by western blot and RT-qPCR. B CCK-8 assays were performed to compare experimental groups with the si-NC group, and PRMT7 downregulation promoted cell growth, while PRMT7 overexpression did not. C Colony formation experiments were performed and the number of colonies in the experimental group was compared to that in the si-NC group, and

Article Snippet: Sections were incubated with rabbit anti-Homo sapiens (Human) PRMT7 polyclonal antibody (CSB-PA885738LA01HU, CUSABIO, Wuhan, China) at 1:100 dilution overnight at 4°C followed by a goat anti-rabbit/mouse secondary antibody.

Techniques: Migration, Knockdown, Over Expression, Western Blot, Quantitative RT-PCR, CCK-8 Assay

Journal: Journal of Cancer

Article Title: PRMT7 Inhibits the Proliferation and Migration of Gastric Cancer Cells by Suppressing the PI3K/AKT Pathway via PTEN.

doi: 10.7150/jca.88102

Figure Lengend Snippet: Figure 3. Effect of PRMT7 expression on PTEN and downstream PI3K/AKT signaling pathway. Western blot was used to detect the effect of low/high PRMT7 expression on the expression of PTEN and related proteins in the downstream PI3K/AKT signaling pathway. *P < 0.05, **P < 0.01, ***P < 0.001 and ns: no significance.

Article Snippet: Sections were incubated with rabbit anti-Homo sapiens (Human) PRMT7 polyclonal antibody (CSB-PA885738LA01HU, CUSABIO, Wuhan, China) at 1:100 dilution overnight at 4°C followed by a goat anti-rabbit/mouse secondary antibody.

Techniques: Expressing, Western Blot

Journal: Journal of Cancer

Article Title: PRMT7 Inhibits the Proliferation and Migration of Gastric Cancer Cells by Suppressing the PI3K/AKT Pathway via PTEN.

doi: 10.7150/jca.88102

Figure Lengend Snippet: Figure 4. PRMT7 plays a tumor suppressor role dependent on PTEN. A Effect of PRMT7 overexpression on the viability of PTEN-deficient gastric cancer cells. B Effect of PRMT7 overexpression on the proliferation of PTEN-deficient gastric cancer cells. C Effect of PRMT7 overexpression on the migration of PTEN-deficient gastric cancer cells. D

Article Snippet: Sections were incubated with rabbit anti-Homo sapiens (Human) PRMT7 polyclonal antibody (CSB-PA885738LA01HU, CUSABIO, Wuhan, China) at 1:100 dilution overnight at 4°C followed by a goat anti-rabbit/mouse secondary antibody.

Techniques: Over Expression, Migration

Journal: Journal of Cancer

Article Title: PRMT7 Inhibits the Proliferation and Migration of Gastric Cancer Cells by Suppressing the PI3K/AKT Pathway via PTEN.

doi: 10.7150/jca.88102

Figure Lengend Snippet: Figure 5. PRMT7 affects gastric cancer cell proliferation and migration via the PI3K/AKT signaling pathway. A CCK-8 assay was used to detect the effect of LY294002 on the viability of gastric cancer cells. B Colony formation assay was used to detect the effect of LY294002 on the proliferation of gastric cancer cells. C Transwell assay was used to

Article Snippet: Sections were incubated with rabbit anti-Homo sapiens (Human) PRMT7 polyclonal antibody (CSB-PA885738LA01HU, CUSABIO, Wuhan, China) at 1:100 dilution overnight at 4°C followed by a goat anti-rabbit/mouse secondary antibody.

Techniques: Migration, CCK-8 Assay, Colony Assay, Transwell Assay

Journal: Journal of Cancer

Article Title: PRMT7 Inhibits the Proliferation and Migration of Gastric Cancer Cells by Suppressing the PI3K/AKT Pathway via PTEN.

doi: 10.7150/jca.88102

Figure Lengend Snippet: Figure 6. PRMT7 interacts with PTEN and promotes PTEN methylation. A RT-qPCR was used to detect the expression of PTEN mRNA in the transfected cells. B Endogenous PTEN and PRMT7 immunoprecipitation occurred in AGS cells. C Exogenous PTEN and PRMT7 co-immunoprecipitated in AGS cells. D AGS cells transfected with PRMT7 siRNA and overexpression plasmid were subjected to co-immunoprecipitation with PTEN antibody, followed by detection of PTEN methylation level with MMA antibody. *P < 0.05, **P < 0.01, ***P < 0.001 and ns: no significance.

Article Snippet: Sections were incubated with rabbit anti-Homo sapiens (Human) PRMT7 polyclonal antibody (CSB-PA885738LA01HU, CUSABIO, Wuhan, China) at 1:100 dilution overnight at 4°C followed by a goat anti-rabbit/mouse secondary antibody.

Techniques: Methylation, Quantitative RT-PCR, Expressing, Transfection, Immunoprecipitation, Over Expression, Plasmid Preparation

Journal: Journal of translational autoimmunity

Article Title: Antiphospholipid antibodies induce proinflammatory and procoagulant pathways in endothelial cells.

doi: 10.1016/j.jtauto.2023.100202

Figure Lengend Snippet: Fig. 3. Immunofluorescent antibody staining in naïve and treated HUVECs. AK. The mixture of APS total IgG and β2GPI induces a pronounced increase of the protein levels of the proinflammatory cytokines IL-6, IL-8 as well the transcription factor NF-κB1 and cell adhesion molecules Tissue Factor, ICAM-1, VCAM-1, Eselectin, P- selectin and TGFR1. There was no significant difference for the TGFR1 molecule (3 J). Visual analysis revealed that all the inflammatory mediators and adhesion molecules presented statistically significant difference between the untreated and treated endothelial cells (3 K).

Article Snippet: Coverslips were incubated overnight at 4 ◦C with primary antibodies against IL-6 (5 μg/ ml, CSB-PA06757A0Rb, Cusabio), IL-8 (5 μg/ml, CSB-MA083271A0m, Cusabio), NF-κB1 (5 μg/ml, CSB-PA190132, Cusabio), TGF-β2 (5 μg/ ml, CSB- PA07319A0Rb, Cusabio), Tissue Factor (5 μg/ml, 4509, American Diagnostica), ICAM-1 (5 μg/ml, AF796, R&D Systems), VCAM-1 (4 μg/ml, sc-18854, Santa Cruz Biotechnology), E-selectin (4 μg/ml, sc-271267, Santa Cruz Biotechnology), P-selectin (4 μg/ml,sc137054, Santa Cruz Biotechnology) and TGFR1 (5 μg/ml,CSBPA023451LA01HU, Cusabio).

Techniques: Staining

Journal: Journal of translational autoimmunity

Article Title: Antiphospholipid antibodies induce proinflammatory and procoagulant pathways in endothelial cells.

doi: 10.1016/j.jtauto.2023.100202

Figure Lengend Snippet: Fig. 5. Immunofluorescent antibody staining in placenta biopsies from APS patients and healthy women. A-K Placenta biopsies derived from APS patients as well as Healthy Donors show increased signal intensity for IL-6, IL-8, NF-κB1, ICAM1, VCAM-1, E-selectin, P-selectin, TGF-β2, and TGFR1 (5A-5D, 5F-5J). Slight difference in fluorescence intensity between HD and APS patient was observed for Tissue Factor (5E). Increased signal intensity was observed as well for the TNF-α molecule in the APS placenta biopsies (5 K).

Article Snippet: Coverslips were incubated overnight at 4 ◦C with primary antibodies against IL-6 (5 μg/ ml, CSB-PA06757A0Rb, Cusabio), IL-8 (5 μg/ml, CSB-MA083271A0m, Cusabio), NF-κB1 (5 μg/ml, CSB-PA190132, Cusabio), TGF-β2 (5 μg/ ml, CSB- PA07319A0Rb, Cusabio), Tissue Factor (5 μg/ml, 4509, American Diagnostica), ICAM-1 (5 μg/ml, AF796, R&D Systems), VCAM-1 (4 μg/ml, sc-18854, Santa Cruz Biotechnology), E-selectin (4 μg/ml, sc-271267, Santa Cruz Biotechnology), P-selectin (4 μg/ml,sc137054, Santa Cruz Biotechnology) and TGFR1 (5 μg/ml,CSBPA023451LA01HU, Cusabio).

Techniques: Staining, Derivative Assay, Fluorescence