Anti-LRRK2 (C-terminal region) antibody is suitable for use in western blot (2-4 μg/mL using HEK-293T cells expressing human LRRK2, and using S2 fractions of rat and mouse brain extracts).
Leucine-rich repeat protein kinase 2 (LRRK2) comprises multiple domains, including a leucine-rich repeat (LRR) domain, a Roc (Ras of complex proteins) GTPase domain followed by a C-terminal of ROC (COR) domain, a Ser/Thr kinase domain and a C-terminal Trp-Asp-40 (WD40) domain. The N-terminal region (?900 amino acids) contains ankyrin (ANK) repeats. The LRRK2 homologue LRRK1 shares domain structure similarity with LRRK2.
LRRK2 mRNA is expressed throughout the brain predominantly within regions of the basal ganglia that are associated with Parkinson′s disease. The presence of multiple protein interaction domains suggests that in addition to its kinase and GTPase activities, LRRK2 may serve as a scaffold protein for the assembly of multiprotein signaling complex. R1441C mutation has been shown to disrupt GTPase activity. G2019S and R1441C, both associated with increased kinase activity.
