LRRK2 Protein, Human (sf9, GST, G2019S)

LRRK2 Protein, Human (sf9, GST, G2019S) is the recombinant human-derived LRRK2, expressed by sf9 insect cells , with GST labeled tag.

LRRK2 is a serine/threonine-protein kinase that phosphorylates a broad range of proteins involved in neuronal plasticity, innate immunity, autophagy, and vesicle trafficking. It serves as a key regulator of RAB GTPases by controlling their GTP/GDP exchange and interaction partners through phosphorylation. LRRK2 phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB29, RAB35, and RAB43. By phosphorylating RAB8A at Thr-72, it modulates RAB3IP-catalyzed GDP/GTP exchange and inhibits RAB8A binding to GDI1/GDI2. Additionally, LRRK2 promotes primary ciliogenesis via phosphorylation of RAB8A and RAB10, enhancing SHH signaling in the brain. Together with RAB29, it facilitates retromer-dependent retrograde trafficking between lysosomes and the Golgi apparatus. LRRK2 regulates neuronal morphology, synaptic vesicle trafficking, and endoplasmic reticulum exit site (ERES) organization. It positively regulates autophagy through calcium-dependent activation of the CaMKK/AMPK pathway and phosphorylates PRDX3 and APP (promoting AICD production and nuclear translocation). In innate immunity, LRRK2 enhances RIPK2 activation downstream of NOD1/NOD2. Independently of its kinase activity, it inhibits MAPT proteasomal degradation, promoting oligomerization and secretion. Its Roc domain exhibits GTPase activity, modulating LRRK2 kinase function. Recruited by RAB29/RAB7L1 to overloaded lysosomes, LRRK2 stabilizes RAB8A and RAB10 via phosphorylation, facilitating lysosomal content release and suppressing lysosomal enlargement.

Human

Sf9 insect cells

GST

Q5S007 (H970-E2527, G2019S)

120892

Partial

Approximately 210 kDa,based on SDS-PAGE under reducing conditions.

Greater than 70% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.