MW 379.5 Da, Purity >98%. Potent and selective LRRK2 inhibitor. Inhibits LRRK2 in cell-free (IC50 = 0.76 nM), cell-based (IC50 = 1.4 nM) and radioligand-binding (IC50 = 3.4 nM) assays. Greater than 295-fold selective against a panel of receptors, channels and over 300 kinases. Oral dosing results in reduced Ser935 phosphorylation of LRRK2 in animal models.
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AURA17, Dardarin, LRRK2_HUMAN, Leucine rich repeat kinase 2, Leucine-rich repeat serine/threonine-protein kinase 2, PARK 8, RIPK7, ROCO 2, augmented in rheumatoid arthritis 17, leucine rich repeat serine threonine protein kinase 2
MW 379.5 Da, Purity >98%. Potent and selective LRRK2 inhibitor. Inhibits LRRK2 in cell-free (IC50 = 0.76 nM), cell-based (IC50 = 1.4 nM) and radioligand-binding (IC50 = 3.4 nM) assays. Greater than 295-fold selective against a panel of receptors, channels and over 300 kinases. Oral dosing results in reduced Ser935 phosphorylation of LRRK2 in animal models.
Soluble in DMSO to 100 mM.
Potent and selective LRRK2 inhibitor. Inhibits LRRK2 in cell-free (IC50 = 0.76 nM), cell-based (IC50 = 1.4 nM) and radioligand-binding (IC50 = 3.4 nM) assays. Greater than 295-fold selective against a panel of receptors, channels and over 300 kinases. Oral dosing results in reduced Ser935 phosphorylation of LRRK2 in animal models.
The protein LRRK2 also known as leucine-rich repeat kinase 2 or dardarin is an enzyme with a molecular weight of approximately 286 kDa. It functions as a kinase meaning it adds phosphate groups to other proteins which affects their activity. LRRK2 is expressed in various tissues but it is highly abundant in the brain especially in regions such as the striatum and cortex. It has a significant role in cellular signaling processes due to its phosphorylation activity.
LRRK2 interacts with cellular mechanisms by regulating cytoskeletal dynamics autophagy and vesicle trafficking. It is a part of a larger complex that includes other proteins involved in these processes. The kinase activity of LRRK2 plays an essential part in maintaining neuronal health and function. It influences the process of autophagy which is a way cells clean themselves by removing damaged components and recycling them.
The action of LRRK2 is central to the mitogen-activated protein kinase (MAPK) and the mammalian target of rapamycin (mTOR) pathways. In these pathways LRRK2 interacts with other proteins such as mTOR and RPS6KB1. It modulates cellular processes like growth proliferation and response to stressors. Its kinase activity affects the phosphorylation state of targets within the pathways hence influencing biological outcomes like survival and apoptosis.
LRRK2 mutations have a significant connection to Parkinson's disease and Crohn's disease. In Parkinson's disease mutated LRRK2 leads to abnormal protein aggregation linking to proteins such as alpha-synuclein. For Crohn's disease LRRK2 influences the immune response and intestinal inflammation. These connections highlight LRRK2's role in the pathogenesis and contribute to understanding these complex disorders.
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