Key features and details
- Produced recombinantly (animal-free) for high batch-to-batch consistency and long term security of supply
- Rabbit monoclonal [UDD1 15(3)] to LRRK2 (phospho S910)
- Suitable for: WB
- Reacts with: Human
Product nameAnti-LRRK2 (phospho S910) antibody [UDD1 15(3)]
See all LRRK2 primary antibodies
DescriptionRabbit monoclonal [UDD1 15(3)] to LRRK2 (phospho S910)
Tested applicationsSuitable for: WBmore details
Unsuitable for: Flow Cyt,ICC/IF,IHC-P or IP
Species reactivityReacts with: Human
Synthetic phosphopeptide corresponding to a region surrounding Serine 910 of Human LRRK2 (UniProt Q5S007).
- GFP-LRRK2 lysate and Lymphoblastoid lysate
This antibody was developed with the support of The Michael J. Fox Foundation (MJFF) and in partnership with Dr. Dario Alessi (MRC Protein Phosphorylation Unit, University of Dundee) to help accelerate LRRK2 research. Dr. Alessi has characterized several unique and high quality LRRK2 rabbit monoclonal antibodies, generated by Abcam, to be made widely available for PD research community.
LRRK2 (Leucine-rich repeat kinase 2, dardarin) is a multi-domain protein belonging to the ROCO family of proteins that contains a kinase and GTPase domain among its many protein interaction domains. LRRK2 is mutated in a significant number of Parkinson's disease (PD) patients. Mutations in this gene account for 4% of PD, and are observed in 1% of sporadic PD patients. The most common mutation replaces glycine 2019 with a serine that results in increased LRRK2 kinase activity. This indicates that inhibitors of LRRK2 kinase activity might be of therapeutic benefit for the treatment of Parkinson’s disease and has stimulated much activity in this field of research.
Recent work has revealed that LRRK2 interacts with14-3-3 phospho-binding adaptor isoforms that is mediated by phosphorylation of Ser910 and Ser935 located prior to the leucine rich repeat domain mediates. Interestingly, 14-3-3 binding has been linked to Parkinson’s disease as Ser910 as well as Ser935 and interaction with the 14-3-3 is inhibited by five of the six validated LRRK2 pathogenic mutations (R1441C, R1441G, R1441H, Y1699C and I2020T). The Dundee-MJFF LRRK2 PhosphoSer935 antibody will be of great utility in further understanding the link between 14-3-3 binding to LRRK2 and Parkinson’s disease as well as assessing the efficacy of LRRK2 inhibitors that are being developed.
It should be noted the Dundee-MJFF antibody is highly selective and sensitive and can readily be used to monitor LRRK2 Ser910 phosphorylation in immunoblot analysis of 2-20 microgram amounts of whole cell extract. The Dundee-MJFF LRRK2 PhosphoSer910 recognizes human but not mouse endogenous LRRK2.
Mouse: We have preliminary internal testing data to indicate this antibody may not react with these species. Please contact us for more information.
This product is a recombinant monoclonal antibody, which offers several advantages including:
- - High batch-to-batch consistency and reproducibility
- - Improved sensitivity and specificity
- - Long-term security of supply
- - Animal-free production
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
We are constantly working hard to ensure we provide our customers with best in class antibodies. As a result of this work we are pleased to now offer this antibody in purified format. We are in the process of updating our datasheets. The purified format is designated 'PUR' on our product labels. If you have any questions regarding this update, please contact our Scientific Support team.
Storage instructionsShipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Storage bufferPreservative: 0.01% Sodium azide
Constituents: 59% PBS, 40% Glycerol, 0.5% BSA
Concentration information loading...
PurityProtein A purified
Clone numberUDD1 15(3)
Our Abpromise guarantee covers the use of ab133449 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/1000 - 1/5000. Detects a band of approximately 286 kDa (predicted molecular weight: 286 kDa).|
FunctionPositively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes. 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. Regulates neuronal process morphology in the intact central nervous system (CNS). Plays a role in synaptic vesicle trafficking. Phosphorylates PRDX3. Has GTPase activity. May play a role in the phosphorylation of proteins central to Parkinson disease.
Tissue specificityExpressed in the brain. Expressed in pyramidal neurons in all cortical laminae of the visual cortex, in neurons of the substantia nigra pars compacta and caudate putamen (at protein level). Expressed throughout the adult brain, but at a lower level than in heart and liver. Also expressed in placenta, lung, skeletal muscle, kidney and pancreas. In the brain, expressed in the cerebellum, cerebral cortex, medulla, spinal cord occipital pole, frontal lobe, temporal lobe and putamen. Expression is particularly high in brain dopaminoceptive areas.
Involvement in diseaseParkinson disease 8
Sequence similaritiesBelongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
Contains 12 LRR (leucine-rich) repeats.
Contains 1 protein kinase domain.
Contains 1 Roc domain.
Contains 7 WD repeats.
DomainThe seven-bladed WD repeat region is critical for synaptic vesicle trafficking and mediates interaction with multiple vesicle-associated presynaptic proteins.
The Roc domain mediates homodimerization and regulates kinase activity.
Cellular localizationMembrane. Cytoplasm. Perikaryon. Mitochondrion. Golgi apparatus. Cell projection, axon. Cell projection, dendrite. Endoplasmic reticulum. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane. Endosome. Lysosome. Mitochondrion outer membrane. Mitochondrion inner membrane. Mitochondrion matrix. Predominantly associated with intracytoplasmic vesicular and membranous structures (By similarity). Localized in the cytoplasm and associated with cellular membrane structures. Predominantly associated with the mitochondrial outer membrane of the mitochondria. Colocalized with RAB29 along tubular structures emerging from Golgi apparatus. Localizes in intracytoplasmic punctate structures of neuronal perikarya and dendritic and axonal processes.
- Information by UniProt
- augmented in rheumatoid arthritis 17 antibody
- AURA17 antibody
- Dardarin antibody
All lanes : Anti-LRRK2 (phospho S910) antibody [UDD1 15(3)] (ab133449) at 1/1000 dilution
Lane 1 : GFP tagged WT LRRK2 lysate at 5 µg
Lane 2 : GFP LRRK2 S910A lysate at 5 µg
Lane 3 : GFP LRRK2 S935A lysate at 5 µg
Lanes 4-5 : Lymphoblastoid lysate at 30 µg
Lanes 6-7 : Lymphoblastoid lysate from
LRRK2 IN1 treated cells at 30 µg
All lanes : HRP conjugated goat anti-rabbit antibody at 1/2000 dilution
Predicted band size: 286 kDa
ab133449 has been referenced in 10 publications.
- Schmidt SH et al. The dynamic switch mechanism that leads to activation of LRRK2 is embedded in the DFG? motif in the kinase domain. Proc Natl Acad Sci U S A 116:14979-14988 (2019). PubMed: 31292254
- Purlyte E et al. Rab29 activation of the Parkinson's disease-associated LRRK2 kinase. EMBO J 37:1-18 (2018). PubMed: 29212815
- Bae EJ et al. LRRK2 kinase regulates a-synuclein propagation via RAB35 phosphorylation. Nat Commun 9:3465 (2018). PubMed: 30150626
- Chen Z et al. LRRK2 interacts with ATM and regulates Mdm2-p53 cell proliferation axis in response to genotoxic stress. Hum Mol Genet 26:4494-4505 (2017). PubMed: 28973420
- Perera G et al. Inhibitor treatment of peripheral mononuclear cells from Parkinson's disease patients further validates LRRK2 dephosphorylation as a pharmacodynamic biomarker. Sci Rep 6:31391 (2016). PubMed: 27503089
- Kuss M et al. Interferon-? induces leucine-rich repeat kinase LRRK2 via extracellular signal-regulated kinase ERK5 in macrophages. J Neurochem 129:980-7 (2014). PubMed: 24479685
- Ito G et al. Lack of correlation between the kinase activity of LRRK2 harboring kinase-modifying mutations and its phosphorylation at Ser910, 935, and Ser955. PLoS One 9:e97988 (2014). WB ; Human . PubMed: 24836358
- Dusonchet J et al. A Parkinson's disease gene regulatory network identifies the signaling protein RGS2 as a modulator of LRRK2 activity and neuronal toxicity. Hum Mol Genet N/A:N/A (2014). Human . PubMed: 24794857
- Mamais A et al. Arsenite stress down-regulates phosphorylation and 14-3-3 binding of leucine-rich repeat kinase 2 (LRRK2), promoting self-association and cellular redistribution. J Biol Chem 289:21386-400 (2014). WB ; Human . PubMed: 24942733
- Chia R et al. Phosphorylation of LRRK2 by casein kinase 1a regulates trans-Golgi clustering via differential interaction with ARHGEF7. Nat Commun 5:5827 (2014). WB . PubMed: 25500533