Rabbit anti p44 42 mapk erk1 2

Manufactured by Cell Signaling Technology

Sourced in United States

Rabbit anti-p44/42 MAPK (Erk1/2) is a primary antibody that specifically recognizes the p44/42 mitogen-activated protein kinase (MAPK), also known as extracellular signal-regulated kinases 1 and 2 (Erk1/2).

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Lab products found in correlation

Rabbit anti phospho p44 42 mapk erk1 2 thr202 tyr204, by Cell Signaling Technology (7 mentions) Rabbit anti akt, by Cell Signaling Technology (5 mentions) Rabbit anti phospho p44 42 mapk p erk1 2, by Cell Signaling Technology (4 mentions) Rabbit anti phospho akt ser473, by Cell Signaling Technology (4 mentions) Mouse anti e cadherin, by BD (3 mentions) Mouse anti akt, by Cell Signaling Technology (2 mentions) Mouse anti actin, by Merck Group (2 mentions) Pvdf membrane, by Merck Group (2 mentions) Protease and phosphatase inhibitor, by Merck Group (2 mentions) Irdye 800cw donkey anti mouse, by LI COR (2 mentions) Odyssey clx imaging system, by LI COR (2 mentions) M per, by Thermo Fisher Scientific (2 mentions) Irdye 680rd goat anti rabbit, by LI COR (2 mentions) Mouse anti β actin, by LI COR (2 mentions) Nupage bis tris sds page, by Thermo Fisher Scientific (2 mentions) Mouse anti gfap, by Merck Group (1 mentions) Rabbit anti glur1, by Merck Group (1 mentions) Mouse monoclonal anti actin, by Merck Group (1 mentions) Mouse anti glur2, by Merck Group (1 mentions) Rabbit anti cdk5, by Santa Cruz Biotechnology (1 mentions)

Close spelling variants of this product

ERK1/2 (1487 citations) Anti-ERK1/2 (692 citations) P44/42 MAPK (Erk1/2) (135 citations) Rabbit anti-ERK1/2 (92 citations) P44/42 MAPK (90 citations) Anti-p44/42 MAPK (Erk1/2) (80 citations) Anti-p44/42 MAPK (36 citations) Rabbit anti-p44/42 MAPK (16 citations) Rabbit anti-Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (15 citations) Rabbit anti-Phospho-p44/42 MAPK (Erk1/2) (8 citations)

23 protocols using rabbit anti p44 42 mapk erk1 2

Western Blot Analyses of Synaptic Proteins

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For Western blot analyses, the following primary antibodies were used: mouse anti-PSD-95 (1:250; BD transduction), rabbit anti-CDK5 (1:500; Santa Cruz biotechnology, Dallas TX), mouse anti-Akt (1:1000, Cell signal technology, Danvers, MA), rabbit anti-p44/42 MAPK (Erk1/2) (1:1000; Cell signal technology), mouse anti-GFAP (1:500, Sigma Aldrich, Oakville, Ontario), mouse anti-syntaxin (1:10 000, Sigma Aldrich), rabbit anti-GluR1 (1:2000, Millipore, Billrica, MA), mouse anti-GluR2 (1:2000, Millipore), mouse anti-NR1 (1:2000), rabbit anti-D2R (1:500, Millipore) and mouse anti-actin (1:10 000; Millipore). Secondary antibodies IRDye 680 Goat Anti-Rabbit IgG (1:10 000; Mandel Scientific, Guelf, Ontario) or IRDye 800 Goat Anti-Mouse (1:10 000; Mandel Scientific) were then used.
For immunochemistry analysis, mouse monoclonal anti-neuronal nuclei (NeuN) (1:250; Millipore) and mouse monoclonal anti-actin (1:5000; Millipore) were used as primary antibodies. Revelation of labeling using the Odyssey imager was performed using IRDye 800 Goat Anti-mouse IgG (1:1000) and IRDye 680 Goat Anti-mouse IgG (1:1000) secondary antibodies.

Etiévant A., Manta S., Latapy C., Magno L.A., Fecteau S, & Beaulieu J.M. (2015). Repetitive transcranial magnetic stimulation induces long-lasting changes in protein expression and histone acetylation. Scientific Reports, 5, 16873.

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Immunoblotting Antibodies and Reagents

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Antibodies for Western blot were as follows: mouse anti-EGFR and mouse anti-HER4 (Abcam, Cambridge, UK), rabbit anti-HER3, mouse anti-p85 PI3K, rabbit anti-phospho EGFR (Try1068), rabbit anti-HER2, rabbit anti-cyclinD1, mouse anti-CDK4, rabbit anti-phospho p44/42 MAPK (p- Erk1/2), rabbit anti-p44/42 MAPK (Erk1/2), rabbit anti-Akt (Cell signaling technology, Danvers, MA), rabbit anti-phospho HER2 and rabbit anti-phospho Akt (Ser473) (Sigma-Aldrich, MO, USA). Recombinant human EGF was purchased from R&D systems, MN, USA. Varlitinib was supplied by ASLAN Pharmaceuticals, Singapore. BKM-120 was purchased from Active Biochem, NJ, USA. These were dissolved as stock in 100% dimethyl sulfoxide (DMSO) and stored at −80°C until use.

Dokduang H., Jamnongkarn W., Promraksa B., Suksawat M., Padthaisong S., Thanee M., Phetcharaburanin J., Namwat N., Sangkhamanon S., Titapun A., Khuntikeo N., Klanrit P, & Loilome W. (2020). In vitro and in vivo Anti-Tumor Effects of Pan-HER Inhibitor Varlitinib on Cholangiocarcinoma Cell Lines. Drug Design, Development and Therapy, 14, 2319-2334.

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Rat Primary Schwann Cell Activation

Cited 1 time

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Rat primary SCs were purchased from a commercial vendor (cat #
R-1700, ScienceCell Research Labs, CA, USA) and cultured according to the
manufacturer’s instructions in 100 mm culture plates at 70%
confluency. Cells were serum-starved (0.1% fetal bovine serum containing
medium) for 18 h, and the day after, platelet derived growth factor (PDGF, 50
ng/ml, cat # P8953, Sigma, MO, USA) was added to cells for 15 min. Cells
were washed once with 1× Dulbecco’s phosphate balanced saline
(PBS, cat# 10010-23, Gibco, MA, USA) solution, and soluble proteins were
prepared for immunoprecipitation analysis as previously described (Bargagna-Mohan et al. 2015 (link)). Blots were
probed with the following antibodies: rabbit anti-p38SerVim (1:400, cat
# sc-16673, SantaCruz Biotechnology, CA, USA, RRID:AB_2216097), rabbit
anti-phospho-p44/42 MAPK (p-ERK1/2; 1:2000, cat # 4370, Cell Signaling
Technology, MA, USA, RRID:AB_2315112), and rabbit anti-p44/42 MAPK (ERK1/2,
1:2000, cat # 4695, Cell Signaling Technology, MA, USA, RRID:AB_390779),
as loading control.

Bargagna-Mohan P., Ishii A., Lei L., Sheehy D., Pandit S., Chan G., Bansal R, & Mohan R. (2017). Sustained Activation of ERK1/2 MAPK in Schwann Cells Causes Corneal Neurofibroma. Journal of neuroscience research, 95(9), 1712-1729.

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Quantifying MEK-ERK Signaling Pathway

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Mitogen-activated protein kinase kinase (MEK) is upstream of ERK. At 30 min after treatment with the MEK inhibitor PD98059 (10 μM; Cell Signaling Technology, Inc., Danvers, MA, USA), the level of phospho-ERK (p-ERK) was detected by WB.
Samples of 10 μg total protein were separated in SDS-PAGE gel. The proteins were then transferred onto a polyvinylidene fluoride (PVDF) membrane. The PVDF membrane was blocked for 2 h at room temperature and then incubated with primary antibodies [rabbit anti-phospho-p44/42 MAPK (ERK1/2; Thr202/Tyr204; 1:1,000; Cell Signaling Technology, Inc.), rabbit anti-p44/42 MAPK (ERK1/2; 1:1,000; Cell Signaling Technology, Inc.) or rabbit anti-GAPDH antibody (1:5,000; Abcam)] overnight with gentle agitation at 4°C. The following day, the membrane was incubated with secondary antibodies [horseradish peroxidase-conjugated goat anti-rabbit IgG, (1:5,000; CoWin Biotech Co., Ltd., Beijing, China)] for 3 h at room temperature. Protein detection was performed using enhanced chemiluminescence.

LIU F., XUAN A., CHEN Y., ZHANG J., XU L., YAN Q, & LONG D. (2014). Combined effect of nerve growth factor and brain-derived neurotrophic factor on neuronal differentiation of neural stem cells and the potential molecular mechanisms. Molecular Medicine Reports, 10(4), 1739-1745.

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Analyzing Nasal Embryo MAPK Signaling

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Nasal portions (from nose point to eye) of each embryo (E10.5 or E17.5) were lysed in NP40 lysis buffer (20mM pH 8.0 Tris-HCl, 137mM NaCl, 1% NP40, 10% Glycerol, 1mM Na3VO4) using a Bio-Gen Pro200 homogenizer (Pro Scientific, Oxford, CT, USA). Resulted lysates were run on 10% Mini-Protean TGX gels (Bio-Rad, Richmond, CA, USA) and transferred to PVDF membrane (Millipore, IPVH00010). Following antibodies were used for immunodetection: rabbit anti-phospho-SMAD1/5/9 (pSmad1/5/9) (#13820, Cell Signaling), rabbit anti-phospho-p38 MAPK (#4631, Cell Signaling), rabbit anti-p38 MAPK (#9212, Cell Signaling), mouse anti-Vinculin antibody (V4505, Sigma-Aldrich), rabbit anti-phospho-p44/42 MAPK (pERK1/2) (#9101, Cell Signaling), rabbit anti-p44/42 MAPK (ERK1/2) (#9102, Cell Signaling). HPR substrate ECL (Millipore, WBKL S0500) was used to detect a bound antibody against pSmad1/5/9, pERK1/2, pERK1/2, pp38, p38 and Vinculin.

Liu X., Hayano S., Pan H., Inagaki M., Ninomiya-Tsuji J., Sun H, & Mishina Y. (2018). Compound mutations in Bmpr1a and Tak1 synergize facial deformities via increased cell death. Genesis (New York, N.Y. : 2000), 56(3), e23093.

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Western Blot Analysis of Signaling Pathways

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Cells were lysed in RIPA buffer (Cell Signaling; Danvers, MA, USA) supplemented with protease and phosphatase inhibitors (Sigma-Aldrich). Total protein extracts were run on SDS-PAGE and blotted onto nitrocellulose. Blots were probed overnight. The following antibodies were purchased from Cell Signaling: Rabbit anti-phospho-IGF-1 receptor β (Tyr1131) (#3021, 1:200); rabbit anti-IGF-1 receptor β (#3018, 1:250); rabbit anti-phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (#9101, 1:1000); rabbit anti-p44/42 MAPK (Erk1/2) (#9102, 1:1000); rabbit anti-phospho-Akt XP (Ser473) (#9018, 1:1000); rabbit anti-AKT (#9272, 1:1000); rabbit anti-phospho-EGFR (Tyr1148) (#4404, 1:200); and mouse anti-EGFR (#2239, 1:200). Mouse anti-β-actin was purchased from Sigma-Aldrich (AC-15, 1:15,000). All primary antibodies were diluted in 5% BSA/TBS-T. Goat anti-mouse secondary IRDye 800 antibody (#926-32210, 1:10,000) was purchased from Li-Cor Biosciences (Lincoln, NE, USA). Goat anti-rabbit alexa-fluor 680 secondary antibody (#1027681, 1:10,000) was purchased from Invitrogen (Grand Island, NY, USA). Protein bands were detected using the Odyssey Imaging System (Li-Cor Biosciences, Lincoln, NE, USA).

Overholser J., Ambegaokar K.H., Eze S.M., Sanabria-Figueroa E., Nahta R., Bekaii-Saab T, & Kaumaya P.T. (2015). Anti-Tumor Effects of Peptide Therapeutic and Peptide Vaccine Antibody Co-targeting HER-1 and HER-2 in Esophageal Cancer (EC) and HER-1 and IGF-1R in Triple-Negative Breast Cancer (TNBC). Vaccines, 3(3), 519-543.

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Western Blot Analysis of MAPK Signaling

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Protein lysates were prepared in MPER (ThermoScientific, Waltham, MA, USA) containing protease (Roche, Indianapolis, IN, USA) and phosphatase (Sigma-Aldrich, St. Louis, MO, USA) inhibitors. Lysates were resolved by 4-12% NuPage Bis-Tris SDS-PAGE (Invitrogen) and transferred to nitrocellulose. Antibodies: Rabbit anti-p44/42 MAPK (Erk1/2) (1:1,000, #4695 Cell Signaling Technology, Danvers, MA, USA), Rabbit anti-Phospho-p44/42 MAPK (Erk1/2), Thr202/Tyr204 (1:2,000, #4370, Cell Signaling Technology), Mouse anti-β-actin (1:3,000, #926-42212, LI-COR, Lincoln, NE, USA), IRDye 680RD Goat anti-Rabbit (1:15,000, 925-68071, LI-COR) and IRDye 800CW Donkey anti-Mouse (1:15,000, 92532212, LI-COR). Blots were developed using the LI-COR Odyssey CLx Imaging System.

Morris S.M., Mhyre A.J., Carmack S.S., Myers C.H., Burns C., Ye W., Ferrer M., Olson J.M, & Klinghoffer R.A. (2018). A modified gene trap approach for improved high-throughput cancer drug discovery. Oncogene, 37(31), 4226-4238.

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Western Blotting of EMT Markers

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Western blotting was performed as described previously using whole cell lysates [14 (link)]. Cells were harvested to prepare cell lysates two weeks after initiating of mutant KRAS^V12 induction. Primary antibodies used were mouse anti-E-cadherin (Cat#610181, BD Biosciences), mouse anti-Vimentin Cat#550513, BD Biosciences), mouse anti-p53 (Cat#sc-126, Santa Cruz, USA), mouse anti-p21 Waf/Cip/CDKN1A (Cat#sc-6246, Santa Cruz), mouse anti-KRAS (Cat#sc-30, Santa Cruz), rabbit anti-AKT (pan) (Cat#4691, Cell Signaling Technology), rabbit anti-phospho-AKT (ser 473) (Cat#4060, Cell Signaling Technology), rabbit anti-p44/42MAPK(Erk1/2) (Cat#9102, Cell Signaling Technology), rabbit anti-phospho-p44/42MAPK(Erk1/2) (Cat#4370, Cell Signaling Technology), mouse anti-Actin (Cat#A2228, Sigma-Aldrich), mouse anti-Vinculin (Cat#SC-73614, Santa Cruz), rabbit anti-α-tubulin (Cat# PM054-7, MBL Life Science, USA), and rabbit anti-phospho-p53 (Ser 15) (Cat#9284, Cell Signaling Technology) antibodies. Actin, Vinculin, or α-tubulin protein levels were used as a control for the adequacy of equal protein loading. Anti-rabbit or anti-mouse (GE Healthcare, Buckinghamshire, England) antibodies were used at 1:2000 dilution as secondary antibodies.

Bisgaard H, & Møller H. (1999). Changes in risk of hospital readmission among asthmatic children in Denmark, 1978-93. BMJ : British Medical Journal, 319(7204), 229-230.

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Western Blot Analysis of MAPK Signaling

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Western Blot Analysis of Signaling Proteins

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Proteins were separated on 10% SDS-PAGE and transferred to nitrocellulose membrane (Bio-Rad, Hercules, California, USA). Then the membrane was blocked with 5% non-fat milk and incubated with rabbit anti-VLDLR antibody (1:400; Abgent), rabbit anti-SP3 antibody (Abgent, San Diego, California, USA) (1:400), mouse anti-GAPDH antibody (1:3000; Sigma-Aldrich), mouse anti-c-Myc antibody (1:500; Santa Cruz Biotechnology, Santa Cruz, California, USA), rabbit anti-p44/42 MAPK (Erk1/2) (1:1000; Cell Signaling Technology [CST], Danvers, Massachusetts, USA), rabbit anti-phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) antibody (1:1000; CST), mouse anti-SAPK/JNK (56G8) antibody (1:1000; CST), rabbit anti-phospho-SAPK/JNK (Thr183/Tyr185) (81E11) antibody (1:1000; CST), rabbit anti-p38 MAPK (D13E1) antibody (1:1000; CST), or rabbit anti-phospho-p38 MAPK (Thr180/Tyr182) (12F8) antibody (1:1000; CST). The proteins were detected with enhanced chemiluminescence reagents (Thermo Scientific, Waltham, Massachusetts, USA).

Zhou H., Guo W., Zhao Y., Wang Y., Zha R., Ding J., Liang L., Yang G., Chen Z., Ma B, & Yin B. (2014). MicroRNA-135a acts as a putative tumor suppressor by directly targeting very low density lipoprotein receptor in human gallbladder cancer. Cancer Science, 105(8), 956-965.

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