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Mouse anti p44 42 mapk erk1 2 l34f12

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Mouse anti-p44/42 MAPK (Erk1/2) (L34F12) is a monoclonal antibody that recognizes the p44/42 mitogen-activated protein kinase (MAPK), also known as Erk1/2. This antibody is a useful tool for the detection and analysis of p44/42 MAPK in various experimental systems.

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Lab products found in correlation

Mouse anti gsk3β clone 3d10, by Cell Signaling Technology (2 mentions) Rabbit anti phospho sfk y416 clone 100f9, by Cell Signaling Technology (2 mentions) Rabbit anti fyn clone epr5500, by Merck Group (2 mentions) Odyssey clx scanner, by LI COR (1 mentions) Nupage 4 12 bis tris gradient gel, by Thermo Fisher Scientific (1 mentions) Anti rabbit irdye 800cw, by LI COR (1 mentions) Anti phospho p44 42 mapk, by Cell Signaling Technology (1 mentions) Mouse anti gapdh 1d4, by Novus Biologicals (1 mentions) Nitrocellulose membrane, by Bio-Rad (1 mentions) Ab108387, by Abcam (1 mentions) Rabbit anti phosphogsk3β ser9 d85e12, by Cell Signaling Technology (1 mentions) Mouse anti actin clone c4, by Merck Group (1 mentions) Rabbit anti ha clone c29f4, by Cell Signaling Technology (1 mentions) Mouse anti bα clone 2g9, by Merck Group (1 mentions) Rabbit anti gfp clone d5, by Cell Signaling Technology (1 mentions) Rabbit anti phospho gsk 3β ser9, by Cell Signaling Technology (1 mentions) Clone c4, by Merck Group (1 mentions) Mouse anti ha clone 16b12, by Fortrea (1 mentions)

Close spelling variants of this product

Anti- P44/42 MAPK (ERK1/2) (L34F12) P44/42 MAPK (Erk1/2) (L34F12) Mouse anti-p44/42 MAPK (Erk1/2) Anti-p44/42 MAPK (Erk1/2) P44/42 MAPK (Erk1/2) ERK1/2 p44/42 Anti-p44/42 MAPK P44/42 MAPK ERK1/2 MAPK Mouse anti-ERK1/2

3 protocols using mouse anti p44 42 mapk erk1 2 l34f12

1

Quantitative Western Blot for ERK1/2 Activation

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Samples (20 µL containing 10 µg protein) were loaded per well of a NuPage 4–12% Bis-Tris gradient gels (#NP0336BOX, Thermo Fisher Scientific), and the SDS-Page gel was subsequently transferred to nitrocellulose membranes (#1620115, BioRad) and Western blot was carried out using the following primary rabbit anti-Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP® (Cell signaling, MA, catalog 8544S, 1:1,000), mouse anti-p44/42 MAPK (Erk1/2) (L34F12) (Cell Signaling, catalog 4696S, 1:1,000), mouse anti-GAPDH (1D4) (Novus Biologicals, CA, catalog 221, 1:1,000) and Li-Cor secondary antibodies: anti-mouse IRdye 680LT (Li-Cor, Lincoln, NE, catalog 926–68020, 1:5,000) and anti-rabbit IRDye 800CW (catalog 926–32211, 1:5,000). Prepared samples were scanned using the Li-Cor Odyssey® CLx Scanner (Li-Cor). For statistical analysis, all ERK bands were normalized to GAPDH.
Blaine A.T., Miao Y., Yuan J., Palant S., Liu R.J., Zhang Z.Y, & van Rijn R.M. (2022). Exploration of beta-arrestin isoform signaling pathways in delta opioid receptor agonist-induced convulsions. Frontiers in Pharmacology, 13, 914651.
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2

Molecular Mechanisms of Tau Hyperphosphorylation

Cited 1 time
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Unless indicated, all chemicals were purchased from Sigma/Merck Millipore. Antibodies used for immunoblotting included: mouse anti‐demethylated PP2Ac (clone 1D6, Merck Millipore); mouse anti‐PP2Acα/β (clone 46, BD Transduction); rabbit anti‐phospho‐p44/42 mitogen activated protein kinase (MAPK) (#9101, Cell Signaling Technology); mouse anti‐p44/42 MAPK (ERK1/2) (L34F12, Cell Signaling Technology); rabbit anti‐phospho‐GSK3β (Ser9) (D85E12, Cell Signaling Technology); mouse anti‐GSK3β (clone 3D10, Cell Signaling Technology); rabbit anti‐Tau (T‐1308‐1, rPeptide); mouse anti‐pS202‐Tau (CP13) [41 (link)] and anti‐pSer396/Ser404 (PHF‐1) tau (kindly donated by Peter Davies); mouse anti‐pS422‐tau (44‐764G, ThermoFisher); mouse anti‐human Tau‐13 (ab19030, Abcam); rabbit anti‐Fyn (clone EPR5500, Merck Millipore); mouse anti‐Fyn clone 25 (BD Transduction Laboratories); rabbit anti‐phospho‐SFK (Y416) (clone 100F9, Cell Signaling Technology); mouse anti‐actin (clone C4, Merck Millipore); and mouse anti‐glyceraldehyde 3‐phosphate dehydrogenase (clone 6C5, Merck Millipore). Mouse anti‐Fyn (clone 15, Santa Cruz), rabbit anti‐pS202‐Tau (ab108387, Abcam) and PHF‐1 antibodies were used for immunostaining.
van Hummel A., Taleski G., Sontag J., Feiten A.F., Ke Y.D., Ittner L.M, & Sontag E. (2023). Methyl donor supplementation reduces phospho‐Tau, Fyn and demethylated protein phosphatase 2A levels and mitigates learning and motor deficits in a mouse model of tauopathy. Neuropathology and Applied Neurobiology, 49(4), e12931.
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3

Antibody-Based Analysis of Protein Signaling

Cited 1 time
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Unless indicated, all chemicals were purchased from Sigma/Merck Millipore. Antibodies used in this study included mouse anti-HA (clone 16B12, Covance); rabbit anti-HA (clone C29F4, Cell Signaling Technology); rabbit anti-GFP (clone D5.1, Cell Signaling Technology); mouse anti-Bα (clone 2G9, Merck Millipore); mouse anti-PP2Acα/β (BD Transduction); goat anti-pY307 PP2Ac (Santa Cruz Biotechnology, Inc; denoted SC); rabbit anti-phospho-SFK (Y416) (clone 100F9, Cell Signaling Technology); rabbit anti-phospho-p44/42 MAPK (clone D13.14.4E, Cell Signaling Technology); mouse anti-p44/42 MAPK (ERK1/2) (L34F12, Cell Signaling Technology); rabbit anti-phospho-GSK-3β (Ser 9) (Cell Signaling Technology) and mouse anti-GSK3β (clone 3D10, Cell Signaling Technology); rabbit anti-Src (clone 32G6, Cell Signaling Technology); mouse anti-Src (clone GD11, Merck Millipore); rabbit anti-Fyn (clone EPR5500, Merck Millipore); mouse anti-Fyn (BD Transduction and Cell Signaling Technology); mouse and rabbit anti-p-Tyr (P-Tyr-100 and P-Tyr-1000, Cell Signaling Technology); rabbit anti-Tau (rPeptide), mouse anti-pSer202 Tau (CP13) (59 (link)) (a gift from Peter Davies). Mouse (clone C4, Merck Millipore) or rabbit (Cytoskeleton) anti-actin, and mouse (clone 236-10501, Life Technologies Australia Pty Ltd) or rabbit (Epitomics) anti-α-tubulin antibodies were used for protein normalization.
Sontag J.M., Schuhmacher D., Taleski G., Jordan A., Khan S., Hoffman A., Gomez R.J., Mazalouskas M.D., Hanks S.K., Spiller B.W., Sontag E, & Wadzinski B.E. (2022). A new paradigm for regulation of protein phosphatase 2A function via Src and Fyn kinase–mediated tyrosine phosphorylation. The Journal of Biological Chemistry, 298(8), 102248.
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