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Bioss rabbit anti cyclin e1 antibody
Rabbit Anti Cyclin E1 Antibody, supplied by Bioss, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech cyclin e1 rabbit polyclonal antibody
Fig. 1 Oleanonic acid inhibited the proliferation of glioma cells in U87 and U251 cells (A) Chemical structural formula of oleanonic acid. The cells were treated with indicated concentration of oleanonic acid or oleanolic acid for 24 h, and then cell viability was measured by MTT assay in (B) U87, (C) U251 and (D) HEB cells. The experiments have been repeated three times. The values represent as means ± SD. *P < 0.05 versus control. After incubation with oleanonic acid (50 μmol/L) for 24 or 48 h, the protein expressions of <t>cyclin</t> D1 and <t>cyclin</t> <t>E1</t> were measured by western blot in (E) U87 and (F) U251 cells. The experiments have been repeated three times. The values represent as means ± SD. *P < 0.05 versus control.
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OriGene cyclin e1 ap06082pu n
EGFR or GPER silencing restore palbociclib sensitivity in MCF7/PalbR cells. A Representative pictures of spheroids (a single spheroid/well) from MCF7/PalbR/shRNA and MCF7/PalbR/shEGFR spheroid cultures grown for 6 days on agar-coated plates. B Quantification of spheroid growth; values of MCF7/PalbR/shRNA cells were set as 100% upon which the number of MCF7/PalbR/shEGFR cells was determined. C Efficacy of EGFR silencing in MCF7/PalbR/shEGFR cells. D Representative pictures of spheroids (a single spheroid/well) from the MCF7/PalbR/shRNA and MCF7/PalbR/shGPER spheroid cultures grown for 6 days on agar-coated plates. Scale bar 500 μm. E Quantification of spheroid growth; values of MCF7/PalbR/shRNA cells were set as 100% upon which the number of MCF7/PalbR/shGPER cells was determined. F Efficacy of GPER silencing in MCF7/PalbR/shGPER cells. G Colony formation assay in in MCF7/PalbR/shRNA and MCF7/PalbR/shGPER cells. Plates were stained with Crystal Violet and colonies were counted following 10 days of incubation. ( H ). I Protein levels of cyclin D1, <t>cyclin</t> <t>E1</t> and GPER in MCF7/PalbR/shRNA and MCF7/PalbR/shGPER cells. Side panels show densitometric analyses of the blots normalized to β-actin, which served as loading control. Values represent the mean ± SD of three independent experiments performed in triplicate. (*) indicates p < 0.05. Kaplan-Meier survival curves representing the overall survival ( J ) and relapse-free survival ( K ) in ER-positive BC patients of the METABRIC database, based on low vs high EGFR and GPER mRNA levels (median values were used as threshold)
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Fig. 1 Oleanonic acid inhibited the proliferation of glioma cells in U87 and U251 cells (A) Chemical structural formula of oleanonic acid. The cells were treated with indicated concentration of oleanonic acid or oleanolic acid for 24 h, and then cell viability was measured by MTT assay in (B) U87, (C) U251 and (D) HEB cells. The experiments have been repeated three times. The values represent as means ± SD. *P < 0.05 versus control. After incubation with oleanonic acid (50 μmol/L) for 24 or 48 h, the protein expressions of cyclin D1 and cyclin E1 were measured by western blot in (E) U87 and (F) U251 cells. The experiments have been repeated three times. The values represent as means ± SD. *P < 0.05 versus control.

Journal: Food Science and Human Wellness

Article Title: Oleanonic acid inhibits glioma growth by inactivating STAT3 via upregulating SIRT6 in nude mice

doi: 10.26599/fshw.2024.9250347

Figure Lengend Snippet: Fig. 1 Oleanonic acid inhibited the proliferation of glioma cells in U87 and U251 cells (A) Chemical structural formula of oleanonic acid. The cells were treated with indicated concentration of oleanonic acid or oleanolic acid for 24 h, and then cell viability was measured by MTT assay in (B) U87, (C) U251 and (D) HEB cells. The experiments have been repeated three times. The values represent as means ± SD. *P < 0.05 versus control. After incubation with oleanonic acid (50 μmol/L) for 24 or 48 h, the protein expressions of cyclin D1 and cyclin E1 were measured by western blot in (E) U87 and (F) U251 cells. The experiments have been repeated three times. The values represent as means ± SD. *P < 0.05 versus control.

Article Snippet: Cyclin E1 rabbit polyclonal antibody (11554-1-AP), cyclin D1 mouse monoclonal antibody (60186-1-Ig), SIRT1 mouse monoclonal antibody (60303-1-Ig), rabbit polyclonal antibody (13572-1-AP) and alpha-tubulin rabbit polyclonal antibody (11224-1-AP) were obtained from Proteintech (PTG, Chicago, IL, USA).

Techniques: Concentration Assay, MTT Assay, Control, Incubation, Western Blot

EGFR or GPER silencing restore palbociclib sensitivity in MCF7/PalbR cells. A Representative pictures of spheroids (a single spheroid/well) from MCF7/PalbR/shRNA and MCF7/PalbR/shEGFR spheroid cultures grown for 6 days on agar-coated plates. B Quantification of spheroid growth; values of MCF7/PalbR/shRNA cells were set as 100% upon which the number of MCF7/PalbR/shEGFR cells was determined. C Efficacy of EGFR silencing in MCF7/PalbR/shEGFR cells. D Representative pictures of spheroids (a single spheroid/well) from the MCF7/PalbR/shRNA and MCF7/PalbR/shGPER spheroid cultures grown for 6 days on agar-coated plates. Scale bar 500 μm. E Quantification of spheroid growth; values of MCF7/PalbR/shRNA cells were set as 100% upon which the number of MCF7/PalbR/shGPER cells was determined. F Efficacy of GPER silencing in MCF7/PalbR/shGPER cells. G Colony formation assay in in MCF7/PalbR/shRNA and MCF7/PalbR/shGPER cells. Plates were stained with Crystal Violet and colonies were counted following 10 days of incubation. ( H ). I Protein levels of cyclin D1, cyclin E1 and GPER in MCF7/PalbR/shRNA and MCF7/PalbR/shGPER cells. Side panels show densitometric analyses of the blots normalized to β-actin, which served as loading control. Values represent the mean ± SD of three independent experiments performed in triplicate. (*) indicates p < 0.05. Kaplan-Meier survival curves representing the overall survival ( J ) and relapse-free survival ( K ) in ER-positive BC patients of the METABRIC database, based on low vs high EGFR and GPER mRNA levels (median values were used as threshold)

Journal: Journal of Experimental & Clinical Cancer Research : CR

Article Title: The G Protein Estrogen Receptor (GPER) is involved in the resistance to the CDK4/6 inhibitor palbociclib in breast cancer

doi: 10.1186/s13046-024-03096-7

Figure Lengend Snippet: EGFR or GPER silencing restore palbociclib sensitivity in MCF7/PalbR cells. A Representative pictures of spheroids (a single spheroid/well) from MCF7/PalbR/shRNA and MCF7/PalbR/shEGFR spheroid cultures grown for 6 days on agar-coated plates. B Quantification of spheroid growth; values of MCF7/PalbR/shRNA cells were set as 100% upon which the number of MCF7/PalbR/shEGFR cells was determined. C Efficacy of EGFR silencing in MCF7/PalbR/shEGFR cells. D Representative pictures of spheroids (a single spheroid/well) from the MCF7/PalbR/shRNA and MCF7/PalbR/shGPER spheroid cultures grown for 6 days on agar-coated plates. Scale bar 500 μm. E Quantification of spheroid growth; values of MCF7/PalbR/shRNA cells were set as 100% upon which the number of MCF7/PalbR/shGPER cells was determined. F Efficacy of GPER silencing in MCF7/PalbR/shGPER cells. G Colony formation assay in in MCF7/PalbR/shRNA and MCF7/PalbR/shGPER cells. Plates were stained with Crystal Violet and colonies were counted following 10 days of incubation. ( H ). I Protein levels of cyclin D1, cyclin E1 and GPER in MCF7/PalbR/shRNA and MCF7/PalbR/shGPER cells. Side panels show densitometric analyses of the blots normalized to β-actin, which served as loading control. Values represent the mean ± SD of three independent experiments performed in triplicate. (*) indicates p < 0.05. Kaplan-Meier survival curves representing the overall survival ( J ) and relapse-free survival ( K ) in ER-positive BC patients of the METABRIC database, based on low vs high EGFR and GPER mRNA levels (median values were used as threshold)

Article Snippet: Equal amounts of whole-protein extract were resolved on an 8% or 10% SDS-polyacrylamide gel and transferred to nitrocellulose membranes (Merck, Milan, Italy), which were probed with primary antibodies against ERα (F-10), EGFR (A-10), c-Fos (E-8), EGR1 (S-25), Cyr61 (A-10), p21 (H164), phosphorylated ERK1/2 (E-4), ERK2 (C-14), and β-actin (AC-15) (Santa Cruz Biotechnology, DBA, Milan, Italy), GPER (AB137479; Abcam, DBA, Milan, Italy), pAKT (4060) and AKT (9272) (Cell Signaling, Euroclone, Milan, Italy), cyclin D1 (TA801655) and cyclin E1 (AP06082PU-N) (purchased from OriGene Technologies, DBA, Milan, Italy) , and then revealed using the chemiluminescent substrate for western blotting Clarity™ Western ECL Substrate (Bio-Rad, Milan, Italy).

Techniques: shRNA, Colony Assay, Staining, Incubation, Control