Recombinant Mouse Map Kinase-Activated Protein Kinase 2 (MAPKAPK2) Protein (His&Myc)

Name: Recombinant Mouse Map Kinase-Activated Protein Kinase 2 (MAPKAPK2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06363P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Map Kinase-Activated Protein Kinase 2 (MAPKAPK2) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P49138
Target Symbol	MAPKAPK2
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MLSGSPGQTPPAPFPSPPPPAPAQPPPPFPQFHVKSGLQIRKNAITDDYKVTSQVLGLGINGKVLRIFDKRTQQKFALKMLQDCPKARREVELHWRASQCPHIVHIVDVYENLYAGRKCLLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLHTSRVLKEDKERWEDVKEEMTSALATMRVDYEQIKIKKIEDASNPLLLKRRKKARAVEDAALAH
Expression Range	1-386aa
Protein Length	Full Length
Mol. Weight	51.5 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. 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. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress following ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites. Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3.
Subcellular Location	Cytoplasm. Nucleus. Note=Phosphorylation and subsequent activation releases the autoinhibitory helix, resulting in the export from the nucleus into the cytoplasm.
Protein Families	Protein kinase superfamily, CAMK Ser/Thr protein kinase family
Database References	KEGG: mmu:17164 STRING: 10090.ENSMUSP00000016672 UniGene: PMID: 29197088 MK2 promotes polarization of tumor-associated macrophages into protumorigenic, proangiogenic M2-like macrophages. PMID: 29666270 Phosphorylation of inhibitory PAS domain protein (IPAS) at Ser184 by MAPK-activated protein kinase 2 (MK2 or MAPKAPK2) enhances the proapoptotic function of IPAS. PMID: 29054108 MK2-mediated RIPK1 phosphorylation is an important molecular mechanism limiting the sensitivity of the cells to the cytotoxic effects of TNF. PMID: 28920952 p38MAPK/MK2 phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction. PMID: 28920954 MK2-mediated phosphorylation of RIPK1 serves as a checkpoint within the TNF signaling pathway that integrates cell survival and cytokine production. PMID: 28506461 this study shows that the loss of MK2 in mast cells decreases the IL-33-induced leukocyte recruitment and the resulting skin inflammation PMID: 27694493 MK2 signaling differentially regulated CCL3 and CCL4. PMID: 27795356 MK2-activating peptide (MK2-AP) blocks the effects of anthrax lethal toxin on endothelial barriers in cultured cells and reduces pulmonary vascular leak in rats. PMID: 26066827 MK2 regulates postnatal arteriogenesis by controlling vascular recruitment of monocytes/macrophages in dual manner: regulation of endothelial MCP-1 expression in response to hemodynamic and inflammatory forces as well as MCP-1 dependent monocyte migration PMID: 26431421 these data suggest there is a sexual dimorphism in MK2 signaling of osteoclast progenitor cell subpopulations. PMID: 25946081 Loss of MK2 effectively blocks bone resorption and prevents the development of postmenopausal bone loss. PMID: 23169443 This study showed that cmpd28, a Mapkapk2/3 inhibitor, represents a potentially new approach to type 2 diabetes therapy. PMID: 26068544 Deficiency of MK2 prevents adverse remodelling and promotes endothelial healing of the arterial wall after injury. PMID: 25120198 high-fat diet-fed MK2-/- mice display decreased glucose tolerance and increased insulin resistance compared to controls. Decreased adipose tissue expression of GLUT4 might contribute to this phenotype. PMID: 25233471 Show a low dose of tumor necrosis factor (TNF) causes hyperacute mortality via an oxidative stress driven mechanism in MK2-deficient mice. In addition, MK2-deficient mice were found to be more sensitive to cecal ligation and puncture-induced sepsis. PMID: 25185746 a key role of MK2 and FasR in the regulation and limitation of the immune response in the CNS PMID: 24964076 These data suggest that MK2 is a key downstream effector of p38 that can modulate pemphigus vulgaris autoantibody pathogenicity. PMID: 23657501 Ube2j1 is phosphorylated in response to lipopolysaccharides in macrophages and contributes to MK2-dependent TNFalpha biosynthesis by an unknown mechanism. PMID: 24020373 MK2 mediated the cellular inflammatory responses within the intestinal muscularis in a mouse model of postoperative ileus. PMID: 23764316 MK2 activity was required for damage response, accumulation of ssDNA, and decreased survival when cells were treated with the nucleoside analogue gemcitabine or when the checkpoint kinase Chk1 was antagonized. PMID: 24082115 MAPKAPK-2 regulates SERCA2a expression and fiber type composition to modulate skeletal muscle and cardiomyocyte function. PMID: 23608535 Protein kinases MK2 and MK3 play critical roles in a mouse model of glomerulonephritis. PMID: 23372691 activation of PP2A or inactivation of the p38MAPK-MAPKAPK2-Hsp27 has a role in survival of cancer stem cells under hypoxia and serum depletion via decrease in PP2A activity PMID: 23185379 MAPK-activated protein kinase-2 limits endothelial inflammation via the PIAS1 S522 phosphorylation-mediated increase in PIAS1 transrepression and SUMO ligase activity. PMID: 23202365 Report a novel CB(2)-activated and MK2-dependent pathway that modulates cytokine expression and reduces pancreatic injury and affiliated complications in cerulein-induced pancreatitis. PMID: 23139224 There is an important role for p38 MAPK/MK-2 signaling in podocyte injury. PMID: 21613416 MK2 regulates LPS-induced IFNbeta expression and downstream STAT3 activation as it restrains MK3 from mediating negative regulatory effects PMID: 21586572 This study showed that long PDE4 isoforms provide a novel node for cross-talk between the cAMP and p38 MAPK signalling systems at the level of MK2. PMID: 21323643 Data show that MK2 plays a critical role in angiotensin II signaling, leading to hypertension, oxidative stress via activation of p47phox and inhibition of antioxidants, and vascular inflammation and proliferation. PMID: 21173344 p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate epithelial keratins. PMID: 20724476 lack of MK2 can reduce tissue damage after spinal cord injury and improve locomotor recovery. PMID: 20943915 Data show that nuclear export of p38 requires its dephosphorylation, and it is exported in a MK2-dependent manner. PMID: 20506250 MK2 phosphorylation reduces the ability of TTP to promote deadenylation by inhibiting the recruitment of CAF1 deadenylase in a mechanism that does not involve sequestration of TTP by 14-3-3. PMID: 20595389 data suggest that MK2 may be essential for functional meiotic bipolar spindle formation, chromosome segregation and proper kinetochore-microtubule attachments PMID: 20596525 MK2 participates in the multifactorial regulation of early inflammatory responses in acute pancreatitis, independently of the regulation of stress proteins like HSP25 and HSP60 and most likely due to its effect on cytokine regulation. PMID: 20501446 MK2 has an important role in mediating some aspects of p38-induced cardiac hypertrophy/heart failure. Demonstrate a role for MK2 in the regulation of COX-2 protein expression. PMID: 20339119 critical role for mapkapk2 gene expression in macrophages participating in the process of cutaneous wound healing PMID: 19609314 MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including Ser178 PMID: 14688255 MAPKAPK2 has a role in the uropod localization of PTEN during FMLP-induced neutrophil chemotaxis PMID: 15033451 MK2, similar to p38mitogen-activated protein kinase, is involved in transmitting the death signal to the ischemic myocardium PMID: 15623425 Mouse cells deficient for MK2 show reduced Mdm2 phosphorylation and elevated levels of p53 protein. PMID: 15688025 In MC3T3 E1 and newborn mouse calvarial osteoblastic cultures the OGP-(10-14) mitogenic signaling is critically dependent on de novo synthesis of mitogen-activated protein kinase-activated protein kinase 2 (Mapkapk2) mRNA and protein. PMID: 16150701 Deletion of the MK2 gene in DBA/1LacJ mice confers protection against collagen-induced arthritis. The MK2 heterozygous mutants display an intermediate level of protection when compared with homozygous mutant and wild-type littermates. PMID: 16849504 S28463 and CpG DNA-induced MK2 signalling regulates TNF mRNA primarily at the translational level, whereas lipopolysaccharides-induced MK2 signalling regulates both the stability and translational efficiency of TNF mRNA. PMID: 17485113 Appears to mediate myofibroblast differentiation; inhibiting that differentiation might contribute to fibrosis rather than protect against it. PMID: 17600313 MK2 does not directly participate in neuronal cell death, but indirectly contributes to neurodegeneration by the production of neurotoxic substances, such as nitric oxide or tumor necrosis factor alpha, from activated glia cells. PMID: 18298661 Data suggest a possible role of mitogen-activated protein kinase-activated protein kinase (MK)2 in the cellular response after neuronal depolarization, in particular in excitotoxicity. PMID: 18702688 p38 MAPK-induced myocardial ischemic injury is not modulated by MK2. PMID: 19214782 Thus, MK2 emerges as a regulator of haematopoietic stem cell homeostasis, which could act through chromatin remodelling by the PcG complex. PMID: 19369945

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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