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3 protocols using anti cycline

1

Western Blot Analysis of Cell Signaling

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Cells were lysed with radio immunoprecipitation assay buffer (RIPA) containing 1 mmol/L PMSF (Solarbio, China). Protein extractions were separated by 12% SDS-PAGE gels and transferred to polyvinylidene fluoride (PVDF) membranes (Millipore, Germany). The membranes were incubated overnight at 4 °C with primary antibodies specific for anti-β-actin, anti-CDK2, anti-CyclinD1, anti-CyclinE, anti-PCNA, and anti-P53 (1:1,000; Wanleibio), anti-Bcl-2, anti-Bax, anti-Caspase9, anti-FOXC1, and anti-MyoD1 (1:1,000; Abways Technology), anti-MyoG, (1:1,000; Abcam, Cambridge, England). After incubation with secondary antibodies, signals were detected using a chemiluminescence system (Bio-Rad, USA).
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2

Klotho Modulates Angiotensin II-Induced Vascular Remodeling

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Dulbecco’s modified Eagle’s medium (DMEM) was purchased from HyClone (HyClone, Logan, CT, USA). Fetal bovine serum (FBS) was purchased from ABGENT (San Diego, CA, USA). We purchased penicillin, streptomycin, and Angiotensin II from Sigma-Aldrich (St. Louis, MO, USA). The Cell Counting Kit-8 (CCK8) was purchased from Dojindo (Kumamoto, Japan). The rat recombinant Klotho protein was from Cloud-Clone Corporation (Houston, TX, USA). The antibodies used in this study were as follows: mouse monoclonal PCNA (PC10), rabbit polyclonal NF-κB p65 (C-20), rabbit polyclonal p-NF-κB p65 (Ser 536), rabbit polyclonal ERK1/2 (K-23), rabbit polyclonal p-ERK1/2 (Thr202/Tyr204), rabbit polyclonal anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (FL-335) (Santa Cruz Biotechnology, CA, USA); and rabbit polyclonal SM22α (Cloud-Clone Corp., Wuhan, China). Anti-CDK2, anti-CDK4, anti-cyclin D, and anti-cyclin E antibodies were purchased from Wanleibio, Shenyang, China, and anti-Akt and anti-phospho-Akt (Ser473) antibodies were from Cell Signaling (MA, USA). The reactivity with rat antigens is included in all of these antibodies. Through ImageJ software (NIH, USA), the signal intensity was quantified.
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3

Protein Expression Profiling in Bovine Myoblasts

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Total proteins of bovine myoblasts were prepared with radio immunoprecipitation assay (RIPA) lysis buffer (Solarbio, Beijing, China). Proteins were fractionated on 12% SDS-PAGE gels and transferred to polyvinylidene difluoride (PVDF) membranes (Thermo Fisher Scientific). Blots were incubated overnight with primary antibodies specific for anti-CyclinD1 (#ab226977), anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH, #ab9485), anti-MyoD (#ab16148) (Abcam, Cambridge, UK), anti-INSR (#WL02857), anti-PCNA (#WL01804), anti-CDK2 (#WL01543), anti-CyclinE (#WL01072), anti-Bcl-2 (#WL01556), anti-P53 (#WL01919), anti-P21 (#WL0362), anti-MyoG (#WL01132), anti-MyHC (#WL02785), and anti-Bax (#WL01637) (Wanleibio, Haerbin, China) at 4°C. After incubation with secondary antibodies, the membranes were quantified with the ChemiDoc XRS system (Bio-Rad, Hercules, CA, USA).
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