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Anti erk p44 p42

Manufactured by Cell Signaling Technology
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The Anti-ERK (p44/p42) product is a primary antibody that recognizes the extracellular signal-regulated kinases (ERK) p44 and p42. It is designed for use in various research applications, such as Western blotting, immunohistochemistry, and immunocytochemistry.

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Lab products found in correlation

Nitrocellulose membrane, by GE Healthcare (3 mentions) Anti phospho erk p p44 p42 tyr202 204, by Cell Signaling Technology (3 mentions) Anti mek, by Cell Signaling Technology (3 mentions) Complete protease inhibitor cocktail, by Roche (3 mentions) Anti phospho mek, by Cell Signaling Technology (2 mentions) Anti phospho mtor, by Cell Signaling Technology (2 mentions) Anti pan akt, by Cell Signaling Technology (2 mentions) Anti mtor, by Cell Signaling Technology (2 mentions) Anti phospho akt, by Cell Signaling Technology (2 mentions) Anti tubulin, by Merck Group (2 mentions) Anti actin, by Merck Group (1 mentions) Anti phospho s6, by Cell Signaling Technology (1 mentions) Anti s6, by Cell Signaling Technology (1 mentions) Anti tbk1, by Cell Signaling Technology (1 mentions) C digit scanner, by LI COR (1 mentions) Anti β actin, by Thermo Fisher Scientific (1 mentions) Nupage bis tris gel, by Thermo Fisher Scientific (1 mentions) Anti phospho smad1 5, by Cell Signaling Technology (1 mentions) Immobilon, by Merck Group (1 mentions) Anti phospho erk p42 p44, by Cell Signaling Technology (1 mentions)

5 protocols using anti erk p44 p42

1

Protein Extraction and Western Blot Analysis

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A total of 0.5 × 106 cells were lysed for 30 minutes in ice-cold MPERM buffer supplemented with 25 mM NaF, 1 mM dithiothreitol, and complete protease inhibitor cocktail from Roche Diagnostics. Cell debris was removed by centrifugation at 10000 rpm for 10 minutes, loading buffer added and treated for 5 min at 95°C. Then, proteins were separated by gel electrophoresis. Separated proteins were blotted onto a nitrocellulose membrane (GE Healthcare) which was blocked with 5% bovine serum albumin in phosphate-buffered saline/Tween (0.05% Tween-20 in phosphate-buffered saline). The following antibodies were used: anti-phospho-ERK (P-p44/p42 (Tyr202/204, #9101, Cell Signaling Technology), anti-ERK (p44/p42, # 4695, Cell Signaling Technology), anti-phospho Akt (Ser473, # 4085, Cell Signaling Technology), anti-panAKT (# 9272, Cell Signaling Technology), anti-phospho MEK (Ser298, #9128, Cell Signaling Technology), anti-MEK (# 8727, Cell Signaling Technology), anti-phospho mTOR (Ser2448, #2971, Cell Signaling Technology),anti-mTOR (# 2972, Cell Signaling Technology), anti-HRAS rabbit (# ab97488, Abcam) and anti–actin (Sigma-Aldrich).
Kiessling M.K., Curioni-Fontecedro A., Samaras P., Atrott K., Cosin-Roger J., Lang S., Scharl M, & Rogler G. (2015). Mutant HRAS as novel target for MEK and mTOR inhibitors. Oncotarget, 6(39), 42183-42196.
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2

Western Blot Analysis of Cellular Signaling

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Western Blots were performed as described previously [9 (link)]. In brief, 0.5x106 cells were lysed for 30 minutes in ice-cold MPERM buffer supplemented with 25mM NaF, 1mM dithiothreitol, and complete protease inhibitor cocktail from Roche Diagnostics. Cell debris was removed by centrifugation and then, proteins were blotted onto a nitrocellulose membrane (GE Healthcare) followed by blocking with 5% bovine serum albumin in phosphate-buffered saline/Tween (0.05% Tween-20 in phosphate-buffered saline). The following antibodies were used: anti-phospho-ERK (P-p44/p42 (Tyr202/204, #9101, Cell Signaling Technology), anti-ERK (p44/p42, # 4695, Cell Signaling Technology), anti-phospho Akt (Ser473, # 4085, Cell Signaling Technology), anti-panAKT (# 9272, Cell Signaling Technology), anti-phospho MEK (Ser298, #9128, Cell Signaling Technology), anti-MEK (# 8727, Cell Signaling Technology), anti-phospho mTOR (Ser2448, #2971, Cell Signaling Technology), anti-mTOR (# 2972, Cell Signaling Technology), anti-phospho S6 (Ser235/236, Cell Signaling Technology), anti-S6 (#2317, Cell Signaling Technology), anti-NRAS rabbit (# ab97488, Abcam) and anti—tubulin (Sigma-Aldrich).
Kiessling M.K., Curioni-Fontecedro A., Samaras P., Lang S., Scharl M., Aguzzi A., Oldrige D.A., Maris J.M, & Rogler G. (2016). Targeting the mTOR Complex by Everolimus in NRAS Mutant Neuroblastoma. PLoS ONE, 11(1), e0147682.
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3

Western Blot Analysis of Signaling Pathways

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A total of 5 × 105 cells were lysed for 30 min in ice-cold MPERM buffer supplemented with 25 mM NaF, 1 mM dithiothreitol, and complete protease inhibitor cocktail from Roche Diagnostics. Equal amounts of protein were separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Then, separated proteins were blotted onto a nitrocellulose membrane (GE Healthcare) followed by blocking with 5 % bovine serum albumin in phosphate-buffered saline/Tween (0.05 % Tween-20 in phosphate-buffered saline). The following antibodies were used: anti-phospho-ERK (P-p44/p42 (Tyr202/204, #9101, Cell Signaling Technology), anti-ERK (p44/p42, # 4695, Cell Signaling Technology), anti-phospho MEK (Ser298, #9128, Cell Signaling Technology), anti-MEK (# 8727, Cell Signaling Technology), anti-TBK1 (Cell Signaling Technology), and anti–tubulin (Sigma-Aldrich).
Kiessling M.K., Schuierer S., Stertz S., Beibel M., Bergling S., Knehr J., Carbone W., de Vallière C., Tchinda J., Bouwmeester T., Seuwen K., Rogler G, & Roma G. (2016). Identification of oncogenic driver mutations by genome-wide CRISPR-Cas9 dropout screening. BMC Genomics, 17(1), 723.
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4

Analyzing Signaling Pathways in C2C12 and BRITER Cells

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Whole cell extracts were collected from C2C12 or BRITER cells in complete lysis buffer (20 mM Tris, 150 mM NaCl, 50 mM NaF, 1% NP40 substitute, HALT protease inhibitor cocktail (ThermoScientific). Proteins were resolved by electrophoresis on pre-cast 10% NuPage Bis-Tris gels (Invitrogen) and transferred to PVDF membranes (Bio-Rad). Membranes were blocked in 5% BSA-TBS-0.5% Tween-20 for 15 minutes, then incubated at 4° overnight with primary antibodies. Antibodies used were: rabbit anti-phospho-p38 MAPK (cat. no. 9211), anti-p38 MAPK XP (8690), anti-phospho-SMAD1/5 (9516), anti-SMAD1 XP (6944), anti-phospho-SMAD2/3 (8828), anti-SMAD2/3 XP (8685), anti-phospho-JNK (4668), anti-SAPK/JNK (9252), anti-phospho-Akt XP (4060), pan anti-Akt (4691), anti-phospho ERK p42/p44 (4377), anti-ERK p42/p44 (9102), anti-phospho-MKK3/6 (12280), anti-MKK3 (8535), anti-phospho-TAK1 (4531), anti-TAK1 (5206), anti-HA (3274), and anti-FLAG (14793); all from Cell Signaling); and mouse anti-p38α (cat. no. 33-1300), anti-p38β (33-8700; both ThermoFisher) and anti-β-actin (Sigma A1978). Proteins were visualized with HRP-conjugated secondary antibodies (Bio-Rad) with WestPico (ThermoFisher) or Immobilon (Millipore) chemiluminescence reagents. Images were obtained and analyzed for relative densitometric relationships on a LI-COR C-DiGit scanner using Image Studio software.
Cook B., Rafiq R., Lee H., Banks K.M., El-Debs M., Chiaravalli J., Glickman J.F., Das B.C., Chen S, & Evans T. (2019). Discovery of a small molecule promoting mouse and human osteoblast differentiation via activation of p38 MAPK-beta. Cell chemical biology, 26(7), 926-935.e6.
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5

Western Blot Antibody Profiling for Signal Transduction

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Antibodies used were the following: anti-ACC (1:500; C83B10, Cell Signaling Technology, 3676), anti–β-actin (1:1000; LI-COR Biosciences, 926-42210), anti-NFκB p65 (1:500; Cell Signaling Technology, 8242), anti–phospho-NFκB p65 (S536) (1:500; Cell Signaling Technology, 3033), anti-ERK p42/p44 (1:1000; Cell Signaling Technology, 4696), anti–phospho-ERK p42/p44 (T202/Y204) (1:1000; Cell Signaling Technology, 4377), anti–glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (1:1000; Cell Signaling Technology, 5174), anti–phospho-STAT6 (Y641) (1:1000; Cell Signaling Technology, 9361), anti-STAT6 (1:1000; Cell Signaling Technology, 9362), anti-vinculin (1:1000; Cell Signaling Technology, 13901), anti-FASN (1:1000; Cell Signaling Technology, 3180), anti-arginase (1:500; Santa Cruz Biotechnology, sc-18351), anti–acetyl-H3 (K27) (1:500; Active Motif, 39133), anti-H3 (1:5000; Abcam, ab1791), rodent OXPHOS antibody cocktail (1:250; Abcam, ab110413), and anti-GLUT1 (1:1000; Novus Biologicals, NB110-39113).
Yeudall S., Upchurch C.M., Seegren P.V., Pavelec C.M., Greulich J., Lemke M.C., Harris T.E., Desai B.N., Hoehn K.L, & Leitinger N. (2022). Macrophage acetyl-CoA carboxylase regulates acute inflammation through control of glucose and lipid metabolism. Science Advances, 8(47), eabq1984.
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