Recombinant human PRAK/MK5 protein is a Human Full Length protein, in the 1 to 471 aa range, expressed in Baculovirus infected Sf9, with >80% purity and suitable for SDS-PAGE, WB, FuncS.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement.
PRAK, MAPKAPK5, MAP kinase-activated protein kinase 5, MAPK-activated protein kinase 5, MAPKAP kinase 5, MAPKAP-K5, MAPKAPK-5, MK-5, MK5, p38-regulated/activated protein kinase
Recombinant human PRAK/MK5 protein is a Human Full Length protein, in the 1 to 471 aa range, expressed in Baculovirus infected Sf9, with >80% purity and suitable for SDS-PAGE, WB, FuncS.
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF
Purity was determined to be >80% by densitometry. Affinity purified.
Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement.
Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.
Phosphorylated on Thr-182 ERK3/MAPK6 or ERK4/MAPK4; which is the regulatory phosphorylation site and is located on the T-loop/loop 12, leading to activation. Phosphorylation at Thr-182 by p38-alpha/MAPK14, p38-beta/MAPK11 is subject to debate. Phosphorylated at Ser-115 by PKA/PRKACA, leading to localization to the cytoplasm. Autophosphorylated (By similarity).
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Hsp27 peptide ab204861 (Hsp27 peptide) can be utilized as a substrate for assessing kinase activity
This product was previously labelled as PRAK
PRAK also known as MK5 is a serine/threonine protein kinase with a molecular weight of approximately 54 kDa. It is expressed in various tissues like the heart brain liver and skeletal muscle. PRAK belongs to the mitogen-activated protein kinase (MAPK) signaling pathway and gets activated by phosphorylation. Mechanically PRAK interacts with and phosphorylates other proteins which affects their activity and function playing an important role in regulating cellular processes such as stress response and the cell cycle.
PRAK/MK5 is a critical component in the regulation of cellular responses to stress stimuli. It is a participant in the activation loop of the MAPK p38 signaling pathway where it serves to influence the phosphorylation state and activity of downstream effectors. PRAK is not typically known to be part of a large complex but it interacts directly with other kinases to amplify or dampen the stress response signal. This allows cells to adapt to varied stress conditions by modulating gene expression apoptosis and other cell fate decisions.
PRAK/MK5 plays essential roles within the p38 MAPK and ERK signaling pathways. It closely associates with p38 MAPK which phosphorylates and activates PRAK enabling it to further disseminate the signal. In these pathways PRAK interplays with proteins such as MAPKAPK-2 and HSP27 facilitating diverse cellular activities like inflammation and differentiation. These signaling networks allow PRAK to serve as a link between external stimuli and internal cellular outcomes.
PRAK/MK5 influences cancer and cardiovascular diseases. Its activity connects closely with tumor suppression wherein it regulates actions involving proteins like p53 and HSP27 impacting cell cycle arrest and apoptosis. In cardiovascular contexts altered PRAK function can relate to heart disease since it regulates stress-induced cardiac responses. Understanding PRAK's interplay with these proteins sheds light on its potential as a therapeutic target for treating diseases related to stress signaling dysfunction.
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SDS-PAGE analysis of ab125743.
Sample Kinase Assay showing the specific activity of ab125743 to be 172 nmol/min/mg.
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