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dna fe2 staining kit beyotime s10070s 1 × working dapi beyotime c1005 (Beyotime)

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Beyotime dna fe2 staining kit beyotime s10070s 1 × working dapi beyotime c1005
Dna Fe2 Staining Kit Beyotime S10070s 1 × Working Dapi Beyotime C1005, supplied by Beyotime, used in various techniques. Bioz Stars score: 99/100, based on 33033 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/dapi-stained+dna/DAPI/pm41475687-94-40-44
Average 99 stars, based on 33033 article reviews

dna fe2 staining kit beyotime s10070s 1 × working dapi beyotime c1005 - by Bioz Stars, 2026-10

99/100 stars

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Article Title: Sex-Stratified Characterization of Behavioral, Hippocampal, and Microglial Androgen Responses to Adolescent High-Fat Diet Consumption in Mice.
Article Snippet: .. Finally, the cell nuclei were stained with 4,6-diamidino-2-phenylindole (DAPI; C1027, 1:600; Beyotime, Shanghai, China). ..

Article Title: Zyxin protects against hypertensive nephropathy by restraining FAK/Skp2-CDK8/YAP signaling in tubular epithelial cells.
Article Snippet: 1 Department of Nephrology, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430022, China 2 Department of Nephrology, Huadong Hospital, Fudan University, Yan’an Road No. 221, Shanghai 200040, China Abstract Background Tubulointerstitial fibrosis and inflammation are hallmark pathological features of hypertensive nephropathy (HN), yet the underlying molecular mechanisms remain elusive.. Zyxin, a focal adhesion protein, has been implicated in hypertension-related pathologies, but its specific role in HN-induced tubulointerstitial injury remains undefined.. Methods An HN murine model was established via a multi-hit DOCA/Ang II + uninephrectomy + high salt approach.

Article Title: Targeting MMGT1 enhances immunotherapy efficacy in triple-negative breast cancer.
Article Snippet: The following day, Alexa Fluor 488-labeled goat anti-mouse IgG (Abcam, ab150113) or Alexa Fluor 594-labeled goat anti-rabbit IgG (Abcam, ab150080) was added and incubated for 1 h in the dark. .. Finally, nuclei were stained with DAPI (Beyotime, C1006) for 5 min, and images were captured using a confocal fluorescence microscope (Leica, Germany). ..

Article Title: Platelet-derived microparticles induce CD8 + T cell senescence in chronic kidney disease via the transfer of microRNA-550a-5p.
Article Snippet: .. Nuclei were stained with DAPI (Beyotime). .. Visualization was performed using a Zeiss LSM800 NLO confocal microscopy (Carl Zeiss).

Incubation:

Article Title: SERINC3 promotes oral squamous cell carcinoma progression and mitochondrial metabolic reprogramming involving c-MET/JNK/PGC-1α axis.
Article Snippet: .. Cells were incubated with the working solution (100 nM) at 37°C for 20 min and fixed with 4% paraformaldehyde for 20 min. Then cells were washed again with PBS and treated with a fluorescence quenching agent containing DAPI (Beyotime, P0131, China) to protect the fluorescent signal. ..

Glass:

Article Title: HOXA3 Knockdown Impairs hESC-Derived Thymic Epithelial-like Cell Differentiation and CXCL12-Associated Early T-Lineage Support.
Article Snippet: .. Nuclei were counterstained with DAPI (Beyotime, Biotechnology, Shanghai, China) for 10 min at room temperature in the dark, and coverslips were mounted onto glass slides using an anti-fade mounting medium (Beyotime, China). .. Images were acquired using a Zeiss 880 multiphoton laser scanning microscope (Zeiss, Oberkochen, Germany) or a Nikon single-photon confocal microscope (Nikon, Tokyo, Japan).

Fluorescence:

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Article Title: Multimodal Programming of Extracellular Vesicles via Nano-Primed SECCS-Based 3D Microenvironments for Coordinated Ferroptosis Suppression and Myogenic Regeneration in Diabetes.
Article Snippet: Chronic diabetic glucolipotoxicity is associated with progressive skeletal muscle atrophy, bone loss, cellular senescence, and ferroptotic injury.. Because ferroptosis inhibition alonemay not restore compromisedmyogenic capacity, we developed a combined stem cell-conditioning strategy integrating fullerol priming with the stem cell screen-enrich-combine(-biomaterials) circulating system (SECCS).. This integrated three-dimensional culture platform uses porous β-TCP granules and intermittent medium circulation to generate BMSCs-derived extracellular vesicles (EVs).

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$(A and B) DB008 engages PARP16 and reduces its MARylation in ovarian cancer cells. OVCAR3 cells ectopically expressing FLAG-PARP16 were treated with 0 – 10 µM DB008 for 4 hours. (A) 20 µg of lysate were subjected to click chemistry to visualize DB008 target engagement with in-gel fluorescence (arrow indicates expected band size for FLAG-PARP16). (B) FLAG-PARP16 was immunoprecipitated from the remaining lysate and its MARylation was assessed with Western blotting. (C and D) In situ detection of (C) PARP16 autoMARylation and (D) RPS6 transMARylation. PLA of FLAG and MAR in OVCAR3 cells subjected to Dox-induced expression of FLAG-PARP16 and treated with 0 or 1 µM DB008 for 16 hours (C), or RPS6 and MAR in OVCAR3 cells treated with 0 or 1 µM DB008 for 16 hours (D). DNA was stained with DAPI. Scale bar is 25 µm. (E and F) Quantification of PLA foci in panel C (E) and panel D (F). Each bar represents the mean + SEM; n = 3. Welch’s t-test; ** = p < 0.01. (G) DB008 reduces ribosome MARylation. OVCAR3 cells were treated with 0 or 1 µM DB008 for 16 hours. Ribosomes were fractionated by ultracentrifugation and ribosome MARylation was assessed by Western blotting. RPS6 was used as a loading control. (H and I) DB008 enhances protein synthesis. OVCAR3 cells were treated with 0 – 2 µM DB008 for 16 hours. The rate of protein synthesis was then assessed with a puromycin incorporation assay. (D) Western blot showing puromycin incorporation, COX20, and cleaved caspase-3. β-tubulin was used as a loading control. (E) Quantification of puromycin signal in D. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; * = p < 0.05, **** = p < 0.0001.$

Journal: bioRxiv

Article Title: PARP16 is a Druggable Regulator of Ribosome MARylation and Protein Homeostasis in Ovarian Cancer Cells

doi: 10.64898/2026.04.01.715986

Figure Lengend Snippet: (A and B) DB008 engages PARP16 and reduces its MARylation in ovarian cancer cells. OVCAR3 cells ectopically expressing FLAG-PARP16 were treated with 0 – 10 µM DB008 for 4 hours. (A) 20 µg of lysate were subjected to click chemistry to visualize DB008 target engagement with in-gel fluorescence (arrow indicates expected band size for FLAG-PARP16). (B) FLAG-PARP16 was immunoprecipitated from the remaining lysate and its MARylation was assessed with Western blotting. (C and D) In situ detection of (C) PARP16 autoMARylation and (D) RPS6 transMARylation. PLA of FLAG and MAR in OVCAR3 cells subjected to Dox-induced expression of FLAG-PARP16 and treated with 0 or 1 µM DB008 for 16 hours (C), or RPS6 and MAR in OVCAR3 cells treated with 0 or 1 µM DB008 for 16 hours (D). DNA was stained with DAPI. Scale bar is 25 µm. (E and F) Quantification of PLA foci in panel C (E) and panel D (F). Each bar represents the mean + SEM; n = 3. Welch’s t-test; ** = p < 0.01. (G) DB008 reduces ribosome MARylation. OVCAR3 cells were treated with 0 or 1 µM DB008 for 16 hours. Ribosomes were fractionated by ultracentrifugation and ribosome MARylation was assessed by Western blotting. RPS6 was used as a loading control. (H and I) DB008 enhances protein synthesis. OVCAR3 cells were treated with 0 – 2 µM DB008 for 16 hours. The rate of protein synthesis was then assessed with a puromycin incorporation assay. (D) Western blot showing puromycin incorporation, COX20, and cleaved caspase-3. β-tubulin was used as a loading control. (E) Quantification of puromycin signal in D. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; * = p < 0.05, **** = p < 0.0001.

Article Snippet: The stained cells were mounted on microslides using VectaShield Antifade Mounting Medium (Vector laboratories, H-1200-10) with DAPI DNA stain.

Techniques: Expressing, Drug discovery, Fluorescence, Immunoprecipitation, Western Blot, In Situ, Staining, Control

(A) Western blot showing PARP16 protein expression is abolished in OVCAR3 cells with PARP16 KO. β-actin was used as a loading control. (B) Immunofluorescence with the MAR detection reagent in OVCAR3 Control or PARP16 KO cells treated with 0 or 1 µM DB008 for 16 hours. The DNA was stained with DAPI. Scale bar = 25 µm. (C) The DB008-dependent increase in protein synthesis requires PARP16 expression. OVCAR3 Control or PARP16 KO cells were treated with 0 or 1 µM DB008 for 16 hours. Protein synthesis was then assessed with a puromycin incorporation assay. β-tubulin was used as a loading control. (D) The DB008-dependent increase in protein aggregation requires PARP16 expression. OVCAR3 Control or PARP16 KO cells were treated with 0 or 1 µM DB008 for 16 hours. Protein aggregation was then assessed with the proteostat aggresome detection reagent. The DNA was stained with DAPI. Scale bar = 25 µm. (E) DB008 reduces growth of control but not OVCAR3 PARP16 KO cells. Cells were treated with 0 or 1 µM DB008 for 1 week. Cell growth was then determined with crystal violet staining. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; ** = p < 0.005; ns indicates no significance. (F) DB008 inhibits the anchorage-independent growth of ovarian cancer cells. OVCAR3 cells were grown in soft agar with media containing 0 – 1 µM DB008 for 3 weeks, replenishing media once per week. Anchorage-independent growth was then measured with crystal violet staining. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; * = p < 0.05, **** = p < 0.0001.

Journal: bioRxiv

Article Title: PARP16 is a Druggable Regulator of Ribosome MARylation and Protein Homeostasis in Ovarian Cancer Cells

doi: 10.64898/2026.04.01.715986

Figure Lengend Snippet: (A) Western blot showing PARP16 protein expression is abolished in OVCAR3 cells with PARP16 KO. β-actin was used as a loading control. (B) Immunofluorescence with the MAR detection reagent in OVCAR3 Control or PARP16 KO cells treated with 0 or 1 µM DB008 for 16 hours. The DNA was stained with DAPI. Scale bar = 25 µm. (C) The DB008-dependent increase in protein synthesis requires PARP16 expression. OVCAR3 Control or PARP16 KO cells were treated with 0 or 1 µM DB008 for 16 hours. Protein synthesis was then assessed with a puromycin incorporation assay. β-tubulin was used as a loading control. (D) The DB008-dependent increase in protein aggregation requires PARP16 expression. OVCAR3 Control or PARP16 KO cells were treated with 0 or 1 µM DB008 for 16 hours. Protein aggregation was then assessed with the proteostat aggresome detection reagent. The DNA was stained with DAPI. Scale bar = 25 µm. (E) DB008 reduces growth of control but not OVCAR3 PARP16 KO cells. Cells were treated with 0 or 1 µM DB008 for 1 week. Cell growth was then determined with crystal violet staining. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; ** = p < 0.005; ns indicates no significance. (F) DB008 inhibits the anchorage-independent growth of ovarian cancer cells. OVCAR3 cells were grown in soft agar with media containing 0 – 1 µM DB008 for 3 weeks, replenishing media once per week. Anchorage-independent growth was then measured with crystal violet staining. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; * = p < 0.05, **** = p < 0.0001.

Article Snippet: The stained cells were mounted on microslides using VectaShield Antifade Mounting Medium (Vector laboratories, H-1200-10) with DAPI DNA stain.

Techniques: Western Blot, Expressing, Control, Immunofluorescence, Staining

(A and B) Inhibition by DB008 requires PARP16 C169. (A) IP-Western showing PARP16 MARylation ( top panel ) or PARylation levels in whole cell extracts (WCE; bottom panel ) of OVCAR3 PARP16 KO cells stably expressing FLAG-PARP16 or FLAG-PARP16 C169S after treatment with 1 µM DB008 for 4 hours. (B) Quantification of MAR signal from A. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; * = p < 0.05; ns indicates no significance. (C) Anchorage-independent growth is unaffected in cells expressing PARP16 C169S. OVCAR3 PARP16 KO cells stably expressing PARP16 WT or PARP16 C169S were grown in soft agar with media containing 0 or 1 µM DB008 for 3 weeks, replenishing media once per week. Anchorage-independent growth was then measured with crystal violet staining. Quantification of crystal violet absorbance in B. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; * = p < 0.05; ns indicates no significance. (D and E) The DB008-dependent increase in protein synthesis requires PARP16 C169. (D) OVCAR3 PARP16 KO cells stably expressing PARP16 WT or PARP16 C169S were treated with 0 or 1 µM DB008 for 16 hours. Protein synthesis was then assessed with a puromycin incorporation assay. β-tubulin was used as a loading control. (E) Quantification of puromycin signal in D. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; ** = p < 0.01; ns indicates no significance. (F) The DB008-dependent increase in protein aggregation requires PARP16 C169. OVCAR3 PARP16 KO cells stably expressing PARP16 WT or PARP16 C169S were treated with 0 or 1 µM DB008 for 16 hours. Protein aggregation was then assessed with the proteostat aggresome detection reagent. The DNA was stained with DAPI. Scale bar = 25 µm.

Journal: bioRxiv

Article Title: PARP16 is a Druggable Regulator of Ribosome MARylation and Protein Homeostasis in Ovarian Cancer Cells

doi: 10.64898/2026.04.01.715986

Figure Lengend Snippet: (A and B) Inhibition by DB008 requires PARP16 C169. (A) IP-Western showing PARP16 MARylation ( top panel ) or PARylation levels in whole cell extracts (WCE; bottom panel ) of OVCAR3 PARP16 KO cells stably expressing FLAG-PARP16 or FLAG-PARP16 C169S after treatment with 1 µM DB008 for 4 hours. (B) Quantification of MAR signal from A. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; * = p < 0.05; ns indicates no significance. (C) Anchorage-independent growth is unaffected in cells expressing PARP16 C169S. OVCAR3 PARP16 KO cells stably expressing PARP16 WT or PARP16 C169S were grown in soft agar with media containing 0 or 1 µM DB008 for 3 weeks, replenishing media once per week. Anchorage-independent growth was then measured with crystal violet staining. Quantification of crystal violet absorbance in B. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; * = p < 0.05; ns indicates no significance. (D and E) The DB008-dependent increase in protein synthesis requires PARP16 C169. (D) OVCAR3 PARP16 KO cells stably expressing PARP16 WT or PARP16 C169S were treated with 0 or 1 µM DB008 for 16 hours. Protein synthesis was then assessed with a puromycin incorporation assay. β-tubulin was used as a loading control. (E) Quantification of puromycin signal in D. Each bar represents the mean + SEM; n = 3. Bars marked with asterisks are significantly different from the control; ANOVA; ** = p < 0.01; ns indicates no significance. (F) The DB008-dependent increase in protein aggregation requires PARP16 C169. OVCAR3 PARP16 KO cells stably expressing PARP16 WT or PARP16 C169S were treated with 0 or 1 µM DB008 for 16 hours. Protein aggregation was then assessed with the proteostat aggresome detection reagent. The DNA was stained with DAPI. Scale bar = 25 µm.

Article Snippet: The stained cells were mounted on microslides using VectaShield Antifade Mounting Medium (Vector laboratories, H-1200-10) with DAPI DNA stain.

Techniques: Inhibition, Western Blot, Stable Transfection, Expressing, Control, Staining

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