Anti-LRRK2/Dardarin, C-Terminus (N241A/34) Recombinant Chicken Chimeric mAb

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.

Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.

This recombinant antibody is a chimeric antibody created by replacing the mouse heavy and light constant regions of clone N241A/34 with chicken IgY heavy and light constant regions. As such this antibody retains the same binding performance as the original clone N241A/34 but can be detected using standard anti-chicken secondary antibodies allowing flexibility for multiplexing applications. This antibody is expressed recombinantly in mammalian cells and then affinity purified from the cell culture media.

Each new lot of antibody is quality control tested by Western blot on rat whole brain lysate and confirmed to stain the expected molecular weight band.