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  • DNA Ligase from T4-infected Escherichia coli
    TS3319

    PLX7904, also known as PB04, is a potent and selective paradox-breaker RAF inhibitor. It is able to efficiently inhibit activation of ERK1/2 in mutant BRAF melanoma cells but does not hyperactivate ERK1/2 in mutant RAS-expressing cells.

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  • DNA Ligase from T4-infected Escherichia coli
    TS3340

    CEP-32496 is a highly potent inhibitor of BRAF(V600E/WT) and c-Raf with Kd of 14 nM/36 nM and 39 nM, also potent to Abl-1, c-Kit, Ret, PDGFRβ and VEGFR2, respectively insignificant affinity for MEK-1, MEK-2, ERK-1 and ERK-2.

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  • DNA Ligase from T4-infected Escherichia coli
    TS3386

    BMS-582949 is a potent and selective p38 mitogen-activated protein kinase (p38 MAPK) inhibitor with IC50 of 13nM,inhibiting both p38 kinase activity and activation of p38.

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  • DNA Ligase from T4-infected Escherichia coli
    TS3387

    Pamapimod is a novel, selective inhibitor of p38 mitogen-activated protein kinase. It inhibits p38α and p38β enzymatic activity with IC50 values of 0.014±0.002 and 0.48± 0.04 microM, respectively with no activity against p38delta or p38gamma isoforms.

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  • DNA Ligase from T4-infected Escherichia coli
    TS3430

    BI-78D3 is a competitive JNK inhibitor with IC50 of 280 nM that displays > 100 fold selectivity over p38α and no activity at mTOR and PI-3K.

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  • DNA Ligase from T4-infected Escherichia coli
    TS3459

    eFT-508 is a potent and selective MNK1/2 inhibitor with IC50s of 2.4 nM and 1 nM, respectively. It potentially results in decreased tumor cell proliferation and tumor growth.

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  • DNA Ligase from T4-infected Escherichia coli
    TS3499

    APS-2-79 is a MAPK antagonist that modulating KSR-dependent MAPK signalling by antagonizing RAF heterodimerization as well as the conformational changes required for phosphorylation and activation of KSR-bound MEK. IC50=120 ± 23 nM.

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  • DNA Ligase from T4-infected Escherichia coli
    TS3551

    Tanzisertib is kinetically competitive with ATP in the JNK-dependent phosphorylation of the protein substrate c-Jun and potent against all isoforms of JNK (Ki(JNK1) = 44 ± 3 nM, IC50(JNK1) = 61 nM, Ki(JNK2) = 6.2 ± 0.6 nM, IC50(JNK2) = 5 nM, IC50(JNK3) = 5 nM) and selective against MAP kinases ERK1 and p38a with IC50 of 0.48 and 3.4 μM respectively.

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