Anti-LRRK2/Dardarin, N-Terminus Antibody (N138/6)

28 Citations

Our Anti-Dardarin/LRRK2, N-terminus mouse monoclonal primary antibody from NeuroMab is produced in-house from hybridoma clone N138/6. It is KO validated, detects human, mouse, and rat Dardarin/LRRK2, N-terminus, and is purified by Protein A chromatography. It is great for use in ICC, WB.

Immunoblot versus rat brain low-speed pellet (LSP), mouse brain membranes (MBM) and wild-type (WT) and LRRK2 KO mouse samples probed with N138/6 (left) and K89/41 (right) TC supe. Mouse brain samples provided by Xiaojie Li, Ted Dawson and Valina Dawson (Johns Hopkins University).
Immunoblot versus rat brain low-speed pellet (LSP), mouse brain membranes (MBM) and wild-type (WT) and LRRK2 KO mouse samples probed with N138/6 (left) and K89/41 (right) TC supe. Mouse brain samples provided by Xiaojie Li, Ted Dawson and Valina Dawson (Johns Hopkins University).
Roll over image to zoom in Click on image to zoom
Immunoblot versus rat brain low-speed pellet (LSP), mouse brain membranes (MBM) and wild-type (WT) and LRRK2 KO mouse samples probed with N138/6 (left) and K89/41 (right) TC supe. Mouse brain samples provided by Xiaojie Li, Ted Dawson and Valina Dawson (Johns Hopkins University).

Human, Mouse, Rat
ICC, IHC, IP, WB
Mouse
490
550
594
650
Carrier-Free

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Data Sheet
KO Validated KO Validated

SKU: 75-188

Volume: 100 µL
Price:
$329.00
Ships: 1-2 business days

Product Details

Dardarin/LRRK2, N-terminus
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.
Purified by Protein A chromatography
1 mg/mL
Monoclonal
N138/6
IgG1
ICC, IHC, IP, WB
Mouse
LRRK2 PARK8
>200 kDa
Fusion protein amino acids 1-500 (N-terminus) of human LRRK2 (accession number Q5S007) produced recombinantly in E. Coli
Human, Mouse, Rat
AB_2234791
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.
Liquid
Produced by in vitro bioreactor culture of hybridoma line followed by Protein A affinity chromatography. Purified mAbs are >90% specific antibody.
10 mM Tris, 50 mM Sodium Chloride, 0.065% Sodium Azide pH 7.116
WB: 1:1000
IHC: 1:500
ICC: 1:500
IP: 10 ug
Unconjugated
No cross-reactivity reported
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.
These antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans.
United States
24 months from date of receipt
Shipped on ice packs
Leucine-rich repeat serine/threonine-protein kinase 2 (EC 2.7.11.1) (Dardarin)
Q5S007

Product Specific References for Applications and Species

Immunocytochemistry: Mouse
PMID Dilution Publication
25201882not listedCho, H.J., et al. 2014. Leucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow ER-Golgi export.. The EMBO Journal, 2314-2331.
244640401:200Parisiadou, L., et al. 2014. LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity.. Nature Neuroscience, 367-376.
Immunohistochemistry: Mouse
PMID Dilution Publication
235607501:1000Davies, P., et al. 2013. Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies.. Biochemical Journal, 101-13.
Immunohistochemistry: Rat
PMID Dilution Publication
235607501:1000Davies, P., et al. 2013. Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies.. Biochemical Journal, 101-13.
Immunoprecipitation: Human
PMID Dilution Publication
272735691:1000Nucifora, F.C. Jr., et al. 2016. Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1.. Nature Communications, 11792.
22423108not listedXiong, Y., et al. 2012. ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2.. Journal of Neuroscience, 3877-3886.
PLA: Human
PMID Dilution Publication
38313055not listedAbe, T., et al. 2024. Lysosomal stress drives the release of pathogenic α-synuclein from macrophage lineage cells via the LRRK2-Rab10 pathway. iScience, 108893.
Immunoprecipitation: Mouse
PMID Dilution Publication
329190312ulKuwahara, T., et al. 2020. Roles of lysosomotropic agents on LRRK2 activation and Rab10 phosphorylation. Neurobiology of Disease, 105081.
272735691:1000Nucifora, F.C. Jr., et al. 2016. Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1.. Nature Communications, 11792.
2201298510ugGómez-Suaga, P., et al. 2012. Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP.. Human Molecular Genetics, 511-525.
220044532.5ugDoggett, E.A., et al. 2012. Phosphorylation of LRRK2 serines 955 and 973 is disrupted by Parkinson''s disease mutations and LRRK2 pharmacological inhibition.. Journal of Neurochemistry, 37-45.
Western Blot: Human
PMID Dilution Publication
272735691:1000Nucifora, F.C. Jr., et al. 2016. Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1.. Nature Communications, 11792.
24947832not listedReyniers, L., et al. 2014. Differential protein-protein interactions of LRRK1 and LRRK2 indicate roles in distinct cellular signaling pathways.. Journal of Neurochemistry, 239-250.
24917786not listedVancraenenbroeck, R., et al. 2014. In silico, in vitro and cellular analysis with a kinome-wide inhibitor panel correlates cellular LRRK2 dephosphorylation to inhibitor activity on LRRK2.. Frontiers in Molecular Neuroscience, 51.
23916833not listedManzoni, C., et al. 2013. Inhibition of LRRK2 kinase activity stimulates macroautophagy.. Biochimica et Biophysica Acta, 2900-2910.
Western Blot: Mouse
PMID Dilution Publication
37366237not listedLiu, Q., et al. 2023. Regulation of LRRK2 mRNA Stability by ATIC and its Substrate AICAR Through ARE-mediated mRNA Decay in Parkinson's Disease. The EMBO Journal, e113410.
34759048not listedKim, J.W., et al. 2021. Dysregulated mRNA Translation in the G2019S LRRK2 and LRRK2 Knock-Out Mouse Brains. eNeuro, .
30592011not listedDe Wit, T., et al. 2019. Inhibition of LRRK2 or casein kinase 1 results in LRRK2 protein destabilization. Molecular Neurobiology, 5273-5286.
28321439not listedXiong, Y., et al. 2017. Overexpression of Parkinson's Disease-Associated Mutation LRRK2 G2019S in Mouse Forebrain Induces Behavioral Deficits and α-Synuclein Pathology. eNeuro, .
281039011:1000Berwick, D.C., et al. 2017. Pathogenic LRRK2 variants are gain-of-function mutations that enhance LRRK2-mediated repression of β-catenin signaling.. Molecular Neurodegeneration, 9.
273786961:1000Ma, B., et al. 2016. LRRK2 modulates microglial activity through regulation of chemokine (C-X3-C) receptor 1 -mediated signalling pathways. Human Molecular Genetics, 3515-3523.
272735691:1000Nucifora, F.C. Jr., et al. 2016. Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1.. Nature Communications, 11792.
244640401:1000Parisiadou, L., et al. 2014. LRRK2 regulates synaptogenesis and dopamine receptor activation through modulation of PKA activity.. Nature Neuroscience, 367-376.
235607501:1000Davies, P., et al. 2013. Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies.. Biochemical Journal, 101-13.
23125283not listedCho, H.J., et al. 2013. MicroRNA-205 regulates the expression of Parkinson''s disease-related leucine-rich repeat kinase 2 protein.. Human Molecular Genetics, 608-622.
22899650not listedBerwick, D.C., et al. 2012. LRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6.. Human Molecular Genetics, 4966-4979.
20016100not listedAndres-Mateos, E., et al. 2009. Unexpected lack of hypersensitivity in LRRK2 knock-out mice to MPTP (1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine).. Journal of Neuroscience, 15846-15850.
Western Blot: Rat
PMID Dilution Publication
235607501:1000Davies, P., et al. 2013. Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies.. Biochemical Journal, 101-13.

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