Immunoblot versus rat brain low-speed pellet (LSP), mouse brain membranes (MBM) and wild-type (WT) and LRRK2 KO mouse samples probed with N138/6 (left) and K89/41 (right) TC supe. Mouse brain samples provided by Xiaojie Li, Ted Dawson and Valina Dawson (Johns Hopkins University).
Anti-Dardarin/LRRK2, N-Terminus Antibody
LRRK2 (also known as PARK8) encodes a protein with 5 putative functional domains: an N-terminal leucine-rich repeat (LRR) domain, a Roc (Ras of complex protein) domain that shares sequence homology to the Ras-related GTPase superfamily, a COR (C-terminal of Roc) domain, a mitogen-activated protein kinase kinase kinase (MAPKKK) domain, and a C-terminal WD40 repeat domain. Mutation in this gene is one of the most common causes of inherited Parkinson disease (Gandhi et al., 2008). LRRK2 was originally identified as a putative disease-causing transcript (DKFZp434H2111) within a 2.6-Mb region encompassing a locus for Parkinson disease-8 (PARK8). Northern blot analysis detected a 9-kb mRNA transcript in all tissues tested, including brain. The authors named the protein product dardarin, derived from the Basque word dardara, meaning tremor. LRRK2/dardarin is also known to positively regulate autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway and together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner. LRRK2/PARK8 is also known to regulate neuronal process morphology in the intact central nervous system (CNS) and play a role in synaptic vesicle trafficking.
Fusion protein amino acids 1-500 (N-terminus) of human LRRK2 (also known as Leucine-rich repeat serine/threonine-protein kinase 2, Dardarin and PARK8, accession number Q5S007); Mouse: 83% identity (418/502 amino acids identical)
Human, Mouse, Rat
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