Anti-MEK2/MAP2K2 Antibody Picoband®

Dual specificity mitogen-activated protein kinase kinase 2 (MAP2K2), also called PRKMK2 or MEK2, is an enzyme that in humans is encoded by the MAP2K2 gene. The protein encoded by this gene is a dual specificity protein kinase that belongs to the MAP kinase kinase family. MAP2K2 is mapped to 19p13.3. This kinase is known to play a critical role in mitogen growth factor signal transduction, and the inhibition or degradation of this kinase is found to be involved in the pathogenesis of Yersinia and anthrax. Recombinant MEK2 and MEK1 both could activate human ERK1 in vitro, and they further characterized biochemically the 2 MAP2Ks. MAP2K2 has been shown to interact with MAPK3 and ARAF.

Alzheimer's Disease, Cancer, Cancer Metabolism, Cardiovascular, Energy Transfer Pathways, Fatty Acid Oxidation, Fatty Acids, Integration Of Energy, Integration Of Energy Metabolism, Lipid and Lipoprotein Metabolism, Lipids/Lipoproteins, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Metabolism Processes, Neurodegenerative Disease, Neurology Process, Neuroscience, Pathways and Processes, Protein Phosphorylation, Redox Metabolism, Response To Hypoxia, Ser/Thr Kinases, Signal Transduction

Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by inly activating myosin. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.

At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing.