Rpl19

Manufactured by Santa Cruz Biotechnology

Sourced in United States, Switzerland

RPL19 is a protein that is a component of the 60S ribosomal subunit. It plays a role in the translation of messenger RNA into proteins.

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Lab products found in correlation

3 protocols using rpl19

Immunoblotting Analysis of Key Signaling Proteins

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Western blots were performed with first antibodies listed below; p-Akt (#4060, Cell Signaling), Akt (#9272, Cell Signaling), p-Erk1/2 (#4370, Cell Signaling), Erk1/2 (#4695, Cell Signaling), p-IκBα (#9246, Cell Signaling), IκBα (sc-371, Santa Cruz), SYK (sc-1240, Santa Cruz), PLCγ1 (#5690, Cell Signaling), PIK3CD (sc-7176, Santa Cruz), RasGRP3 (#3334, Cell Signaling), PKCβI (sc-209, Santa Cruz), PKCβII (sc-210, Santa Cruz), IKKβ (sc-8014, Santa Cruz), MYD88 (#4283, Cell Signaling), NIK (#4994, Cell Signaling, protein was visualized by MG132 pretreatment.), FLAG (F3165, SIGMA), β-actin (sc-69879, Santa Cruz), p-RPS6 (#4858, Cell Signaling), RPS6 (#2317, Cell Signaling), RPL19 (sc-1000830, Santa Cruz), Ago2 (RN005M, MBL), GW182 (RN033P, MBL). Ras activation was assayed by comparing the amount of Ras-GTP and total Ras in identical cell lysates. The Ras-GTP was collected by pull-down with GST-Raf (Ras binding domain, Jena Bioscience). Alkaline phosphatase-conjugated anti-mouse and anti-rabbit secondary antibodies were from Promega. The blots were detected by BCIP/NBT substrate (Promega).

Yamagishi M., Katano H., Hishima T., Shimoyama T., Ota Y., Nakano K., Ishida T., Okada S, & Watanabe T. (2015). Coordinated loss of microRNA group causes defenseless signaling in malignant lymphoma. Scientific Reports, 5, 17868.

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Western Blot Analysis of Cellular Proteins

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Cells were washed twice with PBS before harvesting and lysed in lysis buffer (500 mM NaCl, 1% NP40, 1% sodium deoxycholate, 0.1% SDS, 50 mM Tris, pH 7.0). Total protein concentrations were determined with BCA kit (ThermoFisher). The lysate was mixed with sample buffer and boiled at 100 °C for 10 min. Ten microgram of total protein was loaded and separated by SDS-PAGE gel, and then transferred to nitrocellulose membranes (Millipore, Massachusetts, USA). After blocking, the membranes were incubated overnight at 4 °C with antibodies specific to different proteins, and then with secondary antibodies conjugated with horseradish peroxidase. Immunoreactivity was visualized by enhanced chemiluminescence (GE Healthcare, Illinois, USA). Proteins were detected using the following antibodies: Flag (Sigma, F1804, Missouri, USA), NCL (Proteintech, 10556-1-AP, Illinois, USA), ILF3 (Abcam, ab225626 Cambridge, UK), RPL7A (Santa Cruz, sc-79043, Texas, USA), RPL10A (Santa Cruz, sc-100827), RPL19 (Santa Cruz, sc-100830), RPL36A (Santa Cruz, sc-100831), and GAPDH (Sigma, g8795).

Tan R., Du W., Liu Y., Cong X., Bai M., Jiang C., Li Z., Tan M., Ma D.K., Huang Q., Jiang W, & Dang Y. (2020). Nucleolus localization of SpyCas9 affects its stability and interferes with host protein translation in mammalian cells. Genes & Diseases, 9(3), 731-740.

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Antibody Profiling of Cell Signaling

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Antibodies against the following proteins were used in this study: TMBIM6/BI-1 (1:100, ab51905), and RPL19 (1:1000, ab128648) (all from Abcam, Cambridge, UK); RICTOR (1:2000, A300-459A) (Bethyl Laboratories, Montgomery, TX, USA); AKT (1:1000, #9272), GST (1:1000, #2622), mTOR (1:1000, #2972), mTOR (1:1000, #4517), NDRG1 (1:1000, #9408), phospho-Ser473-AKT (1:1000, #9271), phospho-Ser939-TSC2 (1:1000, #3615), phospho-Thr308-AKT (1:1000, #4056), TSC2 (1:1000, #4308), phospho-Thr346-NDRG1 (1:1000, #3217), SIN1 (1:1000, #12860), p70 S6 Kinase (1:100, #9202), RICTOR (1:1000, #2114), RICTOR (Sepharose bead conjugate, #5379), and RAPTOR (1:1000, #2280) (all from Cell Signaling Technology, Danvers, MA, USA); HA (1:2000, 11867423001) (Roche Diagnostics, Basel, Switzerland); actin (1:1000, sc-47778), Ki-67 (1:100, sc-15402), phospho-Thr450-AKT (1:1000, sc-293094), RPL19 (1:1000, sc-100830), and RPS16 (1:1000, sc-102087), (all from Santa Cruz Biotechnology, Santa Cruz, CA, USA). Secondary antibodies (1:10,000) for immunoblotting (Jackson ImmunoResearch, West Grove, PA, USA) and immunoprecipitation (1:5000, sc-2006) (Santa Cruz Biotechnology) were also used. Insulin (I3769), EGF (E9644), and IGF1 (I3769) were from Sigma-Aldrich. BAPTA-AM (B6769), BAPTA (B1212), and EGTA-AM (E1219) were from Thermo Fisher Scientific (Waltham, MA, USA).

Kim H.K., Bhattarai K.R., Junjappa R.P., Ahn J.H., Pagire S.H., Yoo H.J., Han J., Lee D., Kim K.W., Kim H.R, & Chae H.J. (2020). TMBIM6/BI-1 contributes to cancer progression through assembly with mTORC2 and AKT activation. Nature Communications, 11, 4012.

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