P erk 1 2

Manufactured by Bio-Rad

Sourced in United States

The P-Erk)-1/2 is a laboratory instrument designed for the detection and quantification of phosphorylated Erk1/2 proteins. It provides a reliable and efficient method for analyzing cellular signaling pathways.

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Lab products found in correlation

Erk 1 2, by Bio-Rad (1 mentions) Mouse and rabbit horseradish peroxidase conjugated igg, by Bio-Rad (1 mentions) P akt, by Bio-Rad (1 mentions) β actin, by Merck Group (1 mentions) Supersignal west femto maximum sensitivity substrate, by Thermo Fisher Scientific (1 mentions) Bradford assay, by Bio-Rad (1 mentions) Gel logic 1500 imaging system, by Kodak (1 mentions) Smad1 5 8, by Santa Cruz Biotechnology (1 mentions) Enhanced chemiluminescent substrate, by Thermo Fisher Scientific (1 mentions) Horseradish peroxidase conjugated igg antibodies, by Bio-Rad (1 mentions) Sds page, by Bio-Rad (1 mentions)

2 protocols using p erk 1 2

Protein Expression Profiling by Immunoblot

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Total MMEC protein lysates were quantified with the Bradford assay (Bio-Rad, Hercules, CA, USA) and subjected to immunoblot with primary and secondary antibodies to the following: cMet (cod.#8198), phospho (p)-cMet (cod.#3077), VEGFR2 (cod.#9698), p-VEGFR2 (cod.#3770), p-extracellular signal regulated kinase (p-Erk)-1/2 (cod.#4370), Erk-1/2 (cod.#9102), p-Protein kinase B (p-AKT) (cod.#4060), AKT (cod.#9272), p-Phosphoinositide-specific phospholipase C (p-PLC)γ1 (cod.#8713), PLCγ1(cod.#5690), p-P38 mitogen-activated protein kinases (p-p38) (cod.#4511), p38 (cod. #8690) (Cell Signaling Technology, Danvers, MA, USA); beta-actin (Sigma-Aldrich) (cod. A1978); and mouse and rabbit horseradish peroxidase–conjugated IgG (Bio-Rad). Immunoreactive bands were visualized by enhanced chemiluminescence (SuperSignal West Femto Maximum Sensitivity Substrate, Thermo Scientific, Waltham, MA, USA) and the Gel Logic 1500 Imaging System (Eastman Kodak Co.), quantified with the Kodak Molecular Imaging Software, and expressed as arbitrary optical density (OD).

Rao L., De Veirman K., Giannico D., Saltarella I., Desantis V., Frassanito M.A., Solimando A.G., Ribatti D., Prete M., Harstrick A., Fiedler U., De Raeve H., Racanelli V., Vanderkerken K, & Vacca A. (2018). Targeting angiogenesis in multiple myeloma by the VEGF and HGF blocking DARPin® protein MP0250: a preclinical study. Oncotarget, 9(17), 13366-13381.

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Quantifying Signaling Pathway Dynamics

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Lysates for western blot analysis were prepared from scaffolds at 0, 3, 7, 14, and 21 days of culture using Phosphosafe lysis buffer (Novagen, Madison, WI). Equal amounts of protein lysates were subjected to 4–20% SDS-PAGE (Bio-Rad, Hercules, CA). Western analysis was carried out with antibodies against phosphorylated-Smad1/5 (p-Smad1/5), total Smad1/5/8, phosphorylated-ERK1/2 (p-ERK1/2), total ERK1/2, phosphorylated-Smad2/3 (p-Smad2/3), total Smad2/3, phosphorylated-p38 (p-p38), total p38, and β-actin followed by 1:4000 dilutions of horseradish peroxidase-conjugated IgG antibodies (Bio-Rad, Hercules, CA) and an enhanced chemiluminescent substrate (Thermo Scientific, Rockford, IL). All primary phospho and full length antibodies were obtained from Cell Signaling Technologies (Beverly, MA) except Smad1/5/8, which was obtained from Santa Cruz Biotechnology (Santa Cruz, CA). Imaging was carried out using ImageJ (NIH, Bethesda, MD).

Ren X., Weisgerber D.W., Bischoff D., Lewis M.S., Reid R.R., He T.C., Yamaguchi D.T., Miller T.A., Harley B.A, & Lee J.C. (2016). Nanoparticulate Mineralized Collagen Scaffolds and BMP-9 Induce a Long Term Bone Cartilage Construct in Human Mesenchymal Stem Cells. Advanced healthcare materials, 5(14), 1821-1830.

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