Product Description
LRRK2 (Leucine-rich repeat kinase 2), also known as PARK8 or dardarin, is a member of the serine/threonine protein kinase family (ROCO subfamily) that plays a pivotal role in neuronal homeostasis, vesicle trafficking, autophagy, mitochondrial function, and immune signaling, as well as in lysosomal pathway regulation and cytoskeletal dynamics. LRRK2 is activated by various stimuli including oxidative stress, inflammatory signals (e.g., LPS), and Rab GTPase binding, leading to downstream phosphorylation of multiple Rab proteins (including Rab8A, Rab10, and Rab29), thereby modulating membrane trafficking, neurite outgrowth, and autophagic clearance. Beyond its role in normal central nervous system and peripheral immune function, dysregulation of LRRK2 signaling—primarily through gain-of-function mutations (most notably G2019S in the kinase domain) or increased kinase activity—is closely associated with Parkinson's disease (both familial and sporadic), as well as with inflammatory bowel disease (Crohn's disease), leprosy, and multiple cancers (including certain leukemias and renal carcinomas), making it a highly validated target for neuroprotective therapy (particularly for Parkinson's disease) and drug discovery.
Screeningbio’s LRRK2 Kinase Assay Kit provides a robust, sensitive, and high-throughput platform for quantifying LRRK2 kinase activity and evaluating the potency of tyrosine kinase inhibitors (TKIs).
This kit utilizes the ADP-Glo Kinase Assay platform, a luminescent technology that measures the amount of ADP produced during the kinase reaction.
The assay is performed in two distinct steps:
Kinase Reaction: LRRK2 catalyzes the transfer of a phosphate group from ATP to a specific substrate, resulting in the production of phosphorylated substrate and ADP.
ADP-Glo™ Reagent Addition: After the kinase reaction, the ADP-Glo™ Reagent is added to terminate the reaction and deplete any remaining unreacted ATP.
Kinase Detection: The Kinase Detection Reagent is added to simultaneously convert the produced ADP back into ATP, which is then used by luciferase to generate a luminescent signal.
The light intensity produced is directly proportional to the ADP concentration and, consequently, to the enzymatic activity of the LRRK2 kinase.
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