Anti-LRRK2 (C-terminal region) antibody produced in rabbit

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.

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).

Anti-LRRK2 (C-terminal region) antibody is specific for LRRK2 (approx. 240 kDa) in mice, rats and humans.

LRRK2 is a μLtimeric kinase that also functions as a GTPase. LRRK2 activates a calcium/calmodulin-dependent protein kinase kinase (CaMKK)-β/AMPK signaling pathway and subsequently mediates autophagy. Genetic alterations in LRRK2 cause late-onset Parkinson′s disease . Anti-LRRK2 (C-terminal region) antibody is specific for LRRK2 (approx. 240 kDa) in mice, rats and humans. Staining of the LRRK2 band by immunoblotting is specifically inhibited by the LRRK2 immunizing peptide.

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.

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

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