Anti phospho mek1 2 ser217 221 antibody

Manufactured by Cell Signaling Technology

The Anti-phospho-MEK1/2(Ser217/221) antibody is a laboratory reagent used to detect and measure the phosphorylation of MEK1/2 proteins at specific serine residues (Ser217/221). This antibody can be used in various analytical techniques, such as Western blotting, to study the activation and regulation of the MEK1/2 signaling pathway.

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Lab products found in correlation

Anti p44 42 mapk erk1 2 antibody, by Cell Signaling Technology (2 mentions) Anti mek1 2 antibody, by Cell Signaling Technology (2 mentions) Odyssey blocking buffer pbs, by LI COR (1 mentions) Odyssey protein molecular weight marker, by LI COR (1 mentions) Odyssey infrared imaging system, by LI COR (1 mentions) Nitrocellulose membrane, by Bio-Rad (1 mentions) Anti craf antibody, by Cell Signaling Technology (1 mentions) Anti ras antibody, by Cell Signaling Technology (1 mentions) Anti phospho p44 42 mapk erk1 2 thr202 tyr204 antibody, by Cell Signaling Technology (1 mentions) Pvdf membrane, by Merck Group (1 mentions) Clarity western ecl substrate, by Bio-Rad (1 mentions) Immobilon western chemiluminescent hrp substrate, by Merck Group (1 mentions) Anti β actin antibody, by Merck Group (1 mentions)

Close spelling variants of this product

Anti-phospho-MEK1/2 (Ser217/221) Phospho-MEK1/2 (Ser217/221) Anti-phospho-MEK1/2 Anti-MEK1/2 antibody Phospho-MEK1/2 Anti-MEK1/2 Phospho-MEK1 MEK1/2 Anti-MEK1

3 protocols using anti phospho mek1 2 ser217 221 antibody

Immunohistochemical Analysis of pMEK1/2

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IHC staining was performed as described previously (19) on formalin-fixed paraffin-embedded (FFPE) tumor sections of the HIPO-HNC cohort with a rabbit anti-phospho-MEK1/2(Ser217/221) antibody (#9121, Cell Signaling Technology). The specificity of the staining was confirmed with a rabbit IgG isotype control antibody (DA1E, Cell Signaling Technology) (data not shown). FFPE tumor sections were provided by the tissue bank of the National Center for Tumor Disease (Institute of Pathology, University Hospital Heidelberg, Heidelberg, Germany).

Feng B., Wang K., Herpel E., Plath M., Weichert W., Freier K., Zaoui K, & Hess J. (2021). Prognostic Gene Signature for Squamous Cell Carcinoma with a Higher Risk for Treatment Failure and Accelerated MEK-ERK Pathway Activity. Cancers, 13(20), 5182.

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Western Blot Analysis of MAPK Pathway

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Tumor lysates prepared for RPPA were also used for Western blot. Briefly, 20μg protein from each sample was used for 10% polyacrylamide gel electrophoresis, followed by transferring onto nitrocellulose membrane (Biorad, Cat. # 162–0115), blocking with Odyssey Blocking Buffer (PBS) (LI-COR, Lincoln, NE, Cat. # 927–40000) at room temperature for 1h, incubating with primary antibodies at room temperature for 1h and Infrared (IR)-labeled secondary antibodies (IRdye800CW goat anti-rabbit IgG, Cat. 92532211) at room temperature for 1h. Membranes were imaged and quantified using Odyssey Infrared Imaging System and its application software Version 3.0.30 (LI-COR). Newblot Nitro Striping Buffer (LI-COR, Cat. #928–40030) was used for antibody striping and subsequent probing with a different antibody. All first antibodies used are from Cell Signaling Technology (CST): anti-Phospho-MEK1/2 (Ser217/221) antibody (Cat. #9121, 1:1000); anti-MEK1/2 antibody (Cat. #9122, 1:1000); anti-Phospho-p44/42MAPK (Erk1/2) (Thr202/Try204) antibody (Cat. # 4377, 1:1000); and anti-p44/42 MAPK (Erk1/2) antibody (Cat. #9102, 1:1000). Odyssey Protein Molecular Weight Marker (LI-COR, Cat. 928–40000) was used as molecular weight reference.

Bu W., Liu Z., Jiang W., Nagi C., Huang S., Edwards D.P., Jo E., Mo Q., Creighton C.J., Hilsenbeck S.G., Leavitt A.D., Lewis M.T., Wong S.T, & Li Y. (2018). Mammary precancerous stem and non-stem cells evolve into cancers of distinct subtypes. Cancer research, 79(1), 61-71.

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Western Blot Analysis of MAPK Signaling Pathway

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Cells were lysed with SDS lysis buffer (0.1 M Tris‐HCl at pH 8.0, 10% glycerol, 1% SDS) and immediately boiled for 10 minutes to obtain clear lysates. Protein concentrations were measured using the BCA method (Pierce). Lysates containing equal amounts of proteins were separated by SDS‐PAGE and transferred to PVDF membranes (Merck) for Western blot analysis using the appropriate antibodies. Immunoreactive proteins were visualized using the Immobilon Western chemiluminescent HRP substrate (Merck) or Clarity Western ECL substrate (Bio‐Rad); light emission intensity was quantified using an LAS‐3000 lumino‐image analyzer equipped with Image Gauge v2.3 software. The antibodies used in this study were: anti‐BRAF antibody (14814; Cell Signaling Technology), anti‐CRAF antibody (53745; Cell Signaling Technology), anti‐MEK1/2 antibody (8727; Cell Signaling Technology), anti‐phospho‐MEK1/2 (Ser217/221) antibody (9121; Cell Signaling Technology), anti‐p44/42 MAPK (ERK1/2) antibody (4695; Cell Signaling Technology), anti‐phospho‐p44/42 MAPK (ERK1/2) (Thr202/Tyr204) antibody (4377; Cell Signaling Technology), anti‐RAS antibody (8955; Cell Signaling Technology), anti‐CRBN antibody (71810; Cell Signaling Technology), and anti‐β‐actin antibody (A5316; Merck).

Ohoka N., Suzuki M., Uchida T., Tsukumo Y., Yoshida M., Inoue T., Ohki H, & Naito M. (2022). Development of a potent small‐molecule degrader against oncogenic BRAFV600E protein that evades paradoxical MAPK activation. Cancer Science, 113(8), 2828-2838.

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