Volume: Purified: 100 µL; Purified Trial: 20 µL; TC Supernatant: 5 mL

Concentration: Purified: 1 mg/mL; TC Supernatant: Lot Specific

Clonality: Monoclonal

Form: Purified and TC Supernatant Available (select your preferred form, size and quantity before clicking "Add to Cart")

Host Species: Mouse

Immunogen: Fusion protein amino acids 970-2527 (C-terminus) of human LRRK2 (also known as Leucine-rich repeat serine/threonine-protein kinase 2, Dardarin and PARK8, accession number Q5SS00)
Mouse: 89% identity (1393/1557 amino acids identical)
Rat:89% identity (1392/1557 amino acids identical) 30% identity with LRRK1This NeuroMab antibody is considered "Restricted" and is therefore not available for commercial re-distribution on a for-profit basis.

Target Description: 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.

Gene ID: LRRK2 PARK8

Antibody Registry ID (RRID): AB_10675136

Physical State: Liquid

Validation and Application Notes

Molecular Weight: >200 kDa

NOTE

Aves Labs products are intended for use as research laboratory reagents. They are not intended for use as diagnostic or therapeutic reagents in humans.

↑ back to top

Citations

• West AB, Cowell RM, Daher JP, Moehle MS, Hinkle KM, Melrose HL, Standaert DG, Volpicelli-Daley LA. (2014), 'Differential LRRK2 expression in the cortex, striatum, and substantia nigra in transgenic and nontransgenic rodents..' J Comp Neurol.. 10.1002/cne.23583.
• Dzamko N, Gysbers AM, Bandopadhyay R, Bolliger MF, Uchino A, Zhao Y, Takao M, Wauters S, van de Berg WD, Takahashi-Fujigasaki J, Nichols RJ, Holton JL, Murayama S, Halliday GM. (2017), 'LRRK2 levels and phosphorylation in Parkinson's disease brain and cases with restricted Lewy bodies..' Mov Disord.. 10.1002/mds.26892.
• Schwab AJ, Ebert AD. (2015), 'Neurite Aggregation and Calcium Dysfunction in iPSC-Derived Sensory Neurons with Parkinson's Disease-Related LRRK2 G2019S Mutation..' Stem Cell Reports.. 10.1016/j.stemcr.2015.11.004.
• Choi I, Kim B, Byun JW, Baik SH, Huh YH, Kim JH, Mook-Jung I, Song WK, Shin JH, Seo H, Suh YH, Jou I, Park SM, Kang HC, Joe EH,. (2015), 'LRRK2 G2019S mutation attenuates microglial motility by inhibiting focal adhesion kinase..' Nat Commun.. 10.1038/ncomms9255.
• Zhao J, Molitor TP, Langston JW, Nichols RJ. (2015), 'LRRK2 dephosphorylation increases its ubiquitination.' Biochem J.. 10.1042/BJ20141305.
• Boddu R, Hull TD, Bolisetty S, Hu X, Moehle MS, Daher JP, Kamal AI, Joseph R, George JF, Agarwal A, Curtis LM, West AB. (2015), 'Leucine-rich repeat kinase 2 deficiency is protective in rhabdomyolysis-induced kidney injury..' Hum Mol Genet.. 10.1093/hmg/ddv147.
• Davies P, Hinkle KM, Sukar NN, Sepulveda B, Mesias R, Serrano G, Alessi DR, Beach TG, Benson DL, White CL, Cowell RM, Das SS, West AB, Melrose HL. (2013), 'Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies..' Biochem J.. 10.1042/BJ20121742.
• Henry AG, Aghamohammadzadeh S, Samaroo H, Chen Y, Mou K, Needle E, Hirst WD. (2015), 'Pathogenic LRRK2 mutations, through increased kinase activity, produce enlarged lysosomes with reduced degradative capacity and increase ATP13A2 expression..' Hum Mol Genet.. 10.1093/hmg/ddv314.
• Fuji RN, Flagella M, Baca M, Baptista MA, Brodbeck J, Chan BK, Fiske BK, Honigberg L, Jubb AM, Katavolos P, Lee DW, Lewin-Koh SC, Lin T, Liu X, Liu S, Lyssikatos JP, O'Mahony J, Reichelt M, Roose-Girma M, Sheng Z, Sherer T, Smith A, Solon M, Sweeney ZK, Tarrant J, Urkowitz A, Warming S, Yaylaoglu M, Zhang S, Zhu H, Estrada AA, Watts RJ. (2015), 'Effect of selective LRRK2 kinase inhibition on nonhuman primate lung..' Sci Transl Med.. 10.1126/scitranslmed.aaa3634.
• Liu Z, Galemmo RA Jr, Fraser KB, Moehle MS, Sen S, Volpicelli-Daley LA, DeLucas LJ, Ross LJ, Valiyaveettil J, Moukha-Chafiq O, Pathak AK, Ananthan S, Kezar H, White EL, Gupta V, Maddry JA, Suto MJ, West AB. (2014), 'Unique functional and structural properties of the LRRK2 protein ATP-binding pocket..' J Biol Chem.. 10.1074/jbc.M114.602318.
• Lee JW, Tapias V, Di Maio R, Greenamyre JT, Cannon JR. (2015), 'Behavioral, neurochemical, and pathologic alterations in bacterial artificial chromosome transgenic G2019S leucine-rich repeated kinase 2 rats..' Neurobiol Aging.. 10.1016/j.neurobiolaging.2014.07.011.
• Gómez-Suaga P, Rivero-Ríos P, Fdez E, Blanca Ramírez M, Ferrer I, Aiastui A, López De Munain A, Hilfiker S. (2014), 'LRRK2 delays degradative receptor trafficking by impeding late endosomal budding through decreasing Rab7 activity..' Hum Mol Genet.. 10.1093/hmg/ddu395.
• Daher JP, Volpicelli-Daley LA, Blackburn JP, Moehle MS, West AB. (2014), 'Abrogation of α-synuclein-mediated dopaminergic neurodegeneration in LRRK2-deficient rats..' Proc Natl Acad Sci U S A.. 10.1073/pnas.1403215111.
• Schapansky J, Nardozzi JD, Felizia F, LaVoie MJ. (2014), 'Membrane recruitment of endogenous LRRK2 precedes its potent regulation of autophagy..' Hum Mol Genet.. 10.1093/hmg/ddu138.
• Dorval V, Mandemakers W, Jolivette F, Coudert L, Mazroui R, De Strooper B, Hébert SS. (2014), 'Gene and MicroRNA transcriptome analysis of Parkinson's related LRRK2 mouse models..' PLoS One.. 10.1371/journal.pone.0085510.
• Stafa K, Tsika E, Moser R, Musso A, Glauser L, Jones A, Biskup S, Xiong Y, Bandopadhyay R, Dawson VL, Dawson TM, Moore DJ. (2014), 'Functional interaction of Parkinson's disease-associated LRRK2 with members of the dynamin GTPase superfamily..' Hum Mol Genet.. 10.1093/hmg/ddt600.
• Yao C, Johnson WM, Gao Y, Wang W, Zhang J, Deak M, Alessi DR, Zhu X, Mieyal JJ, Roder H, Wilson-Delfosse AL, Chen SG. (2013), 'Kinase inhibitors arrest neurodegeneration in cell and C. elegans models of LRRK2 toxicity..' Hum Mol Genet.. 10.1093/hmg/dds431.
• Gómez-Suaga P, Luzón-Toro B, Churamani D, Zhang L, Bloor-Young D, Patel S, Woodman PG, Churchill GC, Hilfiker S. (2012), 'Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP..' Hum Mol Genet.. 10.1093/hmg/ddr481.

↑ back to top