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We validate the specificity of these antibodies to MAPKAPK2 by testing them on tissues known to express MAPKAPK2 positively and negatively. Browse below to find the MAPKAPK2 antibody that suites your experiment. We have 15 of these antibodies and many publications and validation images.
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Facts about MAP kinase-activated protein kinase 2.
Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36.
|protein kinase superfamily|
EC 2.7.11; EC 184.108.40.206; MAP kinase-activated protein kinase 2; MAPK-activated protein kinase 2; MAPKAP kinase 2; MAPKAPK2; MAPKAPK-2; mitogen-activated protein kinase-activated protein kinase 2; MK2; Rps6kc1
|Sequence:||1; NC_000001.11 (206684905..206734283)|
Expressed in all tissues examined.
Cytoplasm. Nucleus. Phosphorylation and subsequent activation releases the autoinhibitory helix, resulting in the export from the nucleus into the cytoplasm.
The MAPKAPK2 marker regulates a wide range of biological events. It is a substrate to p38MAPK. It also modulates the function and activity of RBPs. It regulates tumor progression and growth in the intestine. MAPKAPK2 also plays a critical role in cancer progression. It regulates RBPs and modulates p38MAPK activity.
The MAPKAPK2 enzyme isoform family includes four distinct forms: p38a. p38b. p38d. P38a is the founding member of the family and shares 74% homology with p38b. P38g and the p38d have different tissue expression patterns. P38b is found mainly in the brain and skeletal muscles, while p38b is found primarily in the kidneys, lungs and heart.
MAP2K and ERK signaling pathways rely primarily on downstream components. These components integrate signals from different pathways and confer specificity. ERK phosphorylates RSK-1 to respond to photic stimulation of SCN, while p38 works in a circadian rhythm. These CCGs are rhythmic because of the ASL-1 transcription factor.
The nonphosphorylated p38-MK2 compound shares a global, quaternary structure that is shared with the parallel and the phosphorylated forms. It also shares regulatory sites on substrate kinase. Both forms are high in conservation in metazoans. This suggests they may have coevolved to develop their respective signaling functions.
The p38MAPK pathway regulates genes which contain adenine/uridine repetitives (AREs). MK2 is involved in signaling events, inflammatory cytokines expression, and other important cellular processes. In addition, it regulates transcript stability. MK2 inhibition inhibits prostate cancer cell invasion. Bladder cancer invasion is also dependent on MK2-driven MMP-2/9 transcripts.
The N terminal lobe of MAPK's substrate contains the catalytic locations. Their binding affinity is sub-micromolar for the double-phosphorylated and nonphosphorylated forms. By comparison, the binding affinity for ERK2-RSK1 complex is only 100 nM. MAPKAPKs could interact with other MAPKs, such as p38MAPK that are not phosphorylated.
The nucleus is formed by an antiparallel conformer by the phosphoamino-amino acid/p38 AL complex. P38 is phosphorylated only by the AL (Thr-573), and MK2 depends on AL-phosphatation and two other auxiliary sites in the phosphorylated status. However, these sites are not permitted to phosphorylate P38 active site by the antiparallel heterodimer.
PoA inhibitors can be found in the pp38-MK2 compound. The p38 nucleotide binding pouch contains the PoA inhibitors. The PoA inhibitor inhibits the formation of an AL phosphorylation-competent complex. These findings provide molecular foundation for the development of specific p38 inhibiters. Table 1 shows the structure solution.
MAPKAPK2/6 and p38 MKK3/6 bind with p38. In this way, they have similar docking grooves. They form binary structures that are both productive and unproductive. These complexes can be quickly dissociated, which allows for efficient turnovers of enzymatic reactions. Nevertheless, pp-p38 MKK2 contains additional CSPs.
MAPKAPK2 RNA binding protein (RBP). These proteins are key to cellular function as they play key roles in the formation and maintenance of ribonucleoprotein-protein complexes. They play important roles in post-transcriptional RNA regulation, mRNA translation and export, and mRNA location and processing. RBPs also play a role in translation.
The role of RBPs in regulating gene expression is well-known. They regulate transcription through interaction with protein kinases that inhibit or reassign their function. RBPs in mammals encode over 1000 proteins, including many AREs. They play an important role in gene regulation.
MAPKAPK2 regulates activity of the p38MAPK Cascade, which controls recruitment of kinases for target mRNAs. PKB, p38, and MK2 phosphorylation sites are shown by color in the schematics. These proteins are essential components of tumor development. They regulate the expression and function in tumor development.
MAPKAPK2 is a regulator of RBPs and could be a therapeutic target for cancer. MK2 is a p38MAPK inhibitor, and inhibition of it is associated is increased cancer risk. Multiple cellular processes are controlled through the MAPKAPK2 pathway including gene expression and inflammation. These intricate interactions can influence gene stability and expression. In the end, post-transcriptional gene regulation is an important step in controlling the cellular cascades.
In addition to its role in tumorigenesis, MAPKAPK2 is also implicated in the development of lung cancer. An increased risk of developing lung cancer from MAPKAPK2 mutations in lung cancer is linked to MAPKAPK2 mutations. These findings suggest MAPKAPK2 might be a biomarker to detect lung cancer. This discovery has implications for the future of cancer treatment. For now, however, there is very little evidence linking MAPKAPK2 tumorigenesis.
It is known for a long period that RBPs associate and regulate the expression of target transcripts' 3'-UTR. MK2, the master regulator of RBPs, regulates all these activities. MK2 plays a key role in regulating RBPs. It is also important for tumor treatment. These findings show that RBPs can regulate many cellular processes.
MAPKAPK2 is a key regulator for tumor growth and progression in intestine. Its overexpression in cancer cells is associated with poor prognosis, and it could provide a promising therapeutic target. MAPKAPK2 is a protein that regulates transcriptional control of human p53-regulated genes. MK2 can not only control tumor growth but also acts as an anti-tumor and promising alternative to inhibition of p38MAPK.
MK2 inhibition inhibits colon carcinoma tumor growth by decreasing tumor multiplycity. It also reduces tumor size and angiogenesis. Additionally, MK2 regulates the functions of Hsp27, another downstream mediator. This is a crucial factor in colon carcinoma progression. Mice that are MK2-deficient have decreased tumor growth. MK2 downstream signaling regulates cell survival and differentiation.
MK2 targets AU -rich elements in tumor cell cells and controls the production of interleukin-6. Trometraprolin and Tumor necrosis Factor. These proteins are produced from tumor cells and are crucial in their growth. This pathway is not fully understood in humans. Further study is needed in order to understand how MK2 regulates the progression of tumors in the intestine.
The lncRNAs were extensively studied over the past decade. Many studies have shown that lncRNAs regulate GI cancer by interfacing with key genes and proteins. It may also be used as a diagnostic marker for GI Cancer. MCA1 has a regulatory role and could be a promising therapeutic drug for GI cancer. There are several reasons MCA1 is gaining more attention.
MMP-2 regulation is not only controlled by MMP activity but also by the pathway p38MAPK. Invasion is inhibited by inhibition of MMP-2 activity. Furthermore, inhibiting MMP-2 mRNA stability in prostate cancer cells has been shown to reduce the activity of MMP-2. Chronic inflammation may play a role as a trigger for the development of gastrointestinal tumours.
Although many cellular processes are controlled by the p38MAPK pathway, it is especially important for controlling the cell cycle and triggering certain responses. MK2, also known as mitogen-activated kinase 2, is one of the downstream substrates. It is involved in the post-translational regulation and cytokines. This has been implicated in tumor progression and growth. MK2 suppression reduces MK2 production.