Phospho-LRRK2 (Ser935) Antibody (YA9811)
(Synonyms: AURA17; Dardarin; ; Leucine rich repeat kinase 2; LRRK 2; LRRK2; LRRK2_HUMAN; PARK 8; PARK8; RIPK7; ROCO 2; ROCO2)
Based on 1 Customer Validation
Phospho-LRRK2 (Ser935) Antibody (YA9811) is a Rabbit-derived and non-conjugated IgG Recombinant, Monoclonal antibody, targeting to Phospho-LRRK2 (Ser935).
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, ICC/IF, FC
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Reactivity :
Human, Mouse
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Formulation:
Supplied in TBS (pH7.4), 0.05% BSA, 40% Glycerol, 0.05% Sodium Azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
FC
FC: Flow Cytometry
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|---|---|---|---|
| Dilution Ratio | 1:1000 | 1:1000 | 1:1000 |
Product Details
Phospho-LRRK2 (Ser935) Antibody (YA9811) is a Rabbit-derived and non-conjugated IgG Recombinant, Monoclonal antibody, targeting to Phospho-LRRK2 (Ser935).
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Host Rabbit
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Species ReactivityHuman, Mouse
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Observed Molecular WeightObserved band size: 286 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 286 kDa
Synthetic phosphopeptide corresponding to residues surrounding Ser935 of human LRRK2 protein.
Endogenous
affinity purified
Non-conjugated
Phosphorylated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in TBS (pH7.4), 0.05% BSA, 40% Glycerol, 0.05% Sodium Azide.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
LRRK2 is a Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, innate immunity, autophagy, and vesicle trafficking. Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation. Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB29, RAB35, and RAB43. Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A. Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A. Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain. 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. Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization. Positively 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. Phosphorylates PRDX3. By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis. Acts as a positive regulator of innate immunity by mediating phosphorylation of RIPK2 downstream of NOD1 and NOD2, thereby enhancing RIPK2 activation. Independent of its kinase activity, inhibits the proteasomal degradation of MAPT, thus promoting MAPT oligomerization and secretion. In addition, has GTPase activity via its Roc domain which regulates LRRK2 kinase activity. Recruited by RAB29/RAB7L1 to overloaded lysosomes where it phosphorylates and stabilizes RAB8A and RAB10 which promote lysosomal content release and suppress lysosomal enlargement through the EHBP1 and EHBP1L1 effector proteins[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20].
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Subcellular Localization
Cytoplasmic vesicle; Perikaryon; Golgi apparatus membrane; Cell projection, axon; Cell projection, dendrite; Endoplasmic reticulum membrane; Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Endosome; Lysosome; Mitochondrion outer membrane; Cytoplasm, cytoskeleton; Cytoplasmic vesicle, phagosome
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Expression
Tissue_Specificity: 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 in neutrophils (at protein level). Expressed in the brain. 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. -
Isoforms & Post-Translational Modification
Phospho-LRRK2 has an amino acid length of 2527, molecular weight is 286103 Da.
Autophosphorylated at Ser-1292; autophosphorylation is stimulated by RAB29. Phosphorylation of Ser-910 and either Ser-935 or Ser-1444 facilitates interaction with YWHAG. Phosphorylation of Ser-910 and/or Ser-935 facilitates interaction with SFN. -
Subunit
Homodimer.
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SwissProt ID
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Synonyms
AURA17; Dardarin; ; Leucine rich repeat kinase 2; LRRK 2; LRRK2; LRRK2_HUMAN; PARK 8; PARK8; RIPK7; ROCO 2; ROCO2
Documentation
References
[1]. MacLeod D, et al. The familial Parkinsonism gene LRRK2 regulates neurite process morphology. Neuron. 2006 Nov 22;52(4):587-93. [Content Brief]
[2]. Zach S, et al. Signal transduction protein array analysis links LRRK2 to Ste20 kinases and PKC zeta that modulate neuronal plasticity. PLoS One. 2010 Oct 7;5(10):e13191. [Content Brief]
[3]. Angeles DC, et al. Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death. Hum Mutat. 2011 Dec;32(12):1390-7. [Content Brief]
[4]. Gómez-Suaga P, et al. Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP. Hum Mol Genet. 2012 Feb 1;21(3):511-25. [Content Brief]
[5]. MacLeod DA, et al. RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson's disease risk. Neuron. 2013 Feb 6;77(3):425-39. [Content Brief]
[6]. Piccoli G, et al. Leucine-rich repeat kinase 2 binds to neuronal vesicles through protein interactions mediated by its C-terminal WD40 domain. Mol Cell Biol. 2014 Jun;34(12):2147-61. [Content Brief]
[7]. Cho HJ, et al. Leucine-rich repeat kinase 2 regulates Sec16A at ER exit sites to allow ER-Golgi export. EMBO J. 2014 Oct 16;33(20):2314-31. [Content Brief]
[8]. Guerreiro PS, et al. LRRK2 Promotes Tau Accumulation, Aggregation and Release. Mol Neurobiol. 2016 Jul;53(5):3124-3135. [Content Brief]
[9]. Steger M, et al. Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases. Elife. 2016 Jan 29;5:. [Content Brief]
[10]. Yan R, et al. LRRK2 enhances Nod1/2-mediated inflammatory cytokine production by promoting Rip2 phosphorylation. Protein Cell. 2017 Jan;8(1):55-66. [Content Brief]
[11]. Chen ZC, et al. Phosphorylation of amyloid precursor protein by mutant LRRK2 promotes AICD activity and neurotoxicity in Parkinson's disease. Sci Signal. 2017 Jul 18;10(488):. [Content Brief]
[12]. Steger M, et al. Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis. Elife. 2017 Nov 10;6:. [Content Brief]
[13]. Fan Y, et al. Interrogating Parkinson's disease LRRK2 kinase pathway activity by assessing Rab10 phosphorylation in human neutrophils. Biochem J. 2018 Jan 2;475(1):23-44. [Content Brief]
[14]. Purlyte E, et al. Rab29 activation of the Parkinson's disease-associated LRRK2 kinase. EMBO J. 2018 Jan 4;37(1):1-18. [Content Brief]
[15]. Dhekne HS, et al. A pathway for Parkinson's Disease LRRK2 kinase to block primary cilia and Sonic hedgehog signaling in the brain. Elife. 2018 Nov 6;7:. [Content Brief]
[16]. Zhang P, et al. Crystal structure of the WD40 domain dimer of LRRK2. Proc Natl Acad Sci U S A. 2019 Jan 29;116(5):1579-1584. [Content Brief]
[17]. Zhu H, et al. Rab29-dependent asymmetrical activation of leucine-rich repeat kinase 2. Science. 2023 Dec 22;382(6677):1404-1411. [Content Brief]
[18]. Deng J, et al. Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase. Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1499-504. [Content Brief]
[19]. Eguchi T, et al. LRRK2 and its substrate Rab GTPases are sequentially targeted onto stressed lysosomes and maintain their homeostasis. Proc Natl Acad Sci U S A. 2018 Sep 25;115(39):E9115-E9124. [Content Brief]
[20]. Eguchi T, et al. The V-ATPase-ATG16L1 axis recruits LRRK2 to facilitate the lysosomal stress response. J Cell Biol. 2024 Mar 4;223(3):. [Content Brief]
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