Home Primary Antibodies Phospho-MEK1 (Ser298) Antibody [L22P14]

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Phospho-MEK1 (Ser298) Antibody [L22P14]

Cat.No.: F4751

    Application: Reactivity:
    • F4751-wb
      Lane 1: MDA-MB-231, Lane 2: MDA-MB-231 (phosphatase treated), Lane 3: NIH/3T3, Lane 4: NIH/3T3 (phosphatase treated)

    Usage Information

    Dilution
    1:1000
    1:50
    Application
    WB, IP
    Reactivity
    Human, Mouse, Rat
    Source
    Rabbit Monoclonal Antibody
    Storage Buffer
    PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
    Storage (from the date of receipt)
    -20°C (avoid freeze-thaw cycles), 2 years
    Predicted MW
    45 kDa
    Positive Control HeLa cells; MEF cells
    Negative Control MDA-MB-231 cells; NIH/3T3 cells; H-4-II-E cells

    Datasheet & SDS

    Biological Description

    Specificity
    Phospho-MEK1 (Ser298) Antibody [L22P14] detects endogenous levels of total MEK1 protein only when it is phosphorylated at Ser298
    Clone
    L22P14
    Synonym(s)
    MAP2K1; Dual specificity mitogen-activated protein kinase kinase 1; MAP kinase kinase 1; MAPKK 1; MKK1; ERK activator kinase 1; MAPK/ERK kinase 1 (MEK 1); MEK1; PRKMK1
    Background
    Phospho-MEK1 (Ser298) refers to MEK1, a dual-specificity kinase in the MAPK/ERK cascade, phosphorylated at serine 298 by PAK1, which enhances Raf-mediated phosphorylation of its activation loop serines 218/222 to drive signal transduction to ERK1/2 for cell growth, differentiation, and adhesion responses. MEK1 features a typical kinase domain with N- and C-lobes, proline-rich motifs, and key residues, such as Asp217 near the A-loop, that interact with upstream regulators, like B-Raf's Arg662, to facilitate A-loop repositioning and phosphorylation flexibility during activation. Ser298 phosphorylation by PAK1 serves as a critical convergence for integrin and growth factor signaling, localizing phospho-MEK1 to peripheral adhesion sites via FAK/Src dependency, promoting MEK1-ERK complex formation, MAPK activation, and fibronectin-stimulated responses like cell spreading, while mutants lacking this site (S298A) impair ERK phosphorylation and pathway efficiency in NIH/3T3 or other cells. This modification is adhesion-regulated, distinct from serum-independent basal phosphorylation, and supports transformation or differentiation without cross-reactivity to MEK2.
    References
    • https://pubmed.ncbi.nlm.nih.gov/17314031/
    • https://pubmed.ncbi.nlm.nih.gov/12876277/

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