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AB169521

Anti-LRRK2 (phospho S955) 抗体 [MJF-R11 (75-1)]

Anti-LRRK2 (phospho S955) antibody [MJF-R11 (75-1)]

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(10 Publications)

Rabbit Recombinant Monoclonal LRRK2 phospho S955 antibody. Suitable for WB and reacts with Human samples. Cited in 10 publications.

別名を表示する

PARK8, LRRK2, Leucine-rich repeat serine/threonine-protein kinase 2, Dardarin

1 Images
Western blot - Anti-LRRK2 (phospho S955) antibody [MJF-R11 (75-1)] (AB169521)
  • WB

Collaborator

Western blot - Anti-LRRK2 (phospho S955) antibody [MJF-R11 (75-1)] (AB169521)

Lanes 1 - 2:

Anti-DDDDK tag antibody

Lanes 3 - 4:

Western blot - Anti-LRRK2 (phospho S955) antibody [MJF-R11 (75-1)] (ab169521) at 1/2000 dilution

Lanes 5 - 6:

Western blot - Anti-LRRK2 (phospho S955) antibody [MJF-R11 (75-1)] (ab169521) at 1/10000 dilution

Lanes 1, 3 and 5:

HEK293T cells stably expressed with wild-type DDDDK-LRRK2

Lanes 2, 4 and 6:

HEK293T cells stably expressed with mutant DDDDK-LRRK2

Predicted band size: 286 kDa

false

This image is courtesy of Drs. Dario Alessi and Paul Davies (The University of Dundee)

Key facts

宿主種

Rabbit

クローン性

Monoclonal

クローン番号

MJF-R11 (75-1)

アイソタイプ

IgG

キャリアフリー

No

交差種

Human

アプリケーション

WB

applications

免疫原

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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製品の詳細

This antibody was developed with support of The Michael J. Fox Foundation (MJFF) with the assistance of a consortium of investigators to help accelerate LRRK2 research.

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. Based upon mass spectrometry findings, a number of other residues within LRRK2 have also been found to be phosphorylated as well.

It is of note that phosphorylation of Serine 955 is not thought to be the result of autophosphorylation of the kinase though currently, the physiological relevance of these phospho-sites is not clear. Thus with the generation of this phospho-specific antibody, it is MJFF's hope that investigators may have at hand a critical tool to assist in their research endeavors that might thereby lend further clarity to the field of LRRK2 and its role in PD pathogenesis.

Acknowledgements: The Michael J. Fox Foundation would like to acknowledge the assistance of the following laboratories and individuals, whose input, guidance and assistance in testing all phospho specific LRRK2 antibodies was critical:

• The Laboratory of Dr. Dario Alessi (University of Dundee) - Paul Davies, PhD
• The Laboratory of Dr. Mark Cookson (National Institute on Aging) - Alexandra Beilina, PhD
• The Laboratory of Dr. Johannes Gloeckner (Helmholtz Zentrum Munchen)
• The Laboratory of Dr. Takeshi Iwatsubo (University of Tokyo) - Genta Ito, PhD
• The Laboratory of Dr. Jeremy Nichols (The Parkinson's Institute)
• The Laboratory of Dr. Andrew West (University of Alabama)

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
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 batch production

For more information, read more on recombinant antibodies.

Collaborations
This antibody was developed with support from The Michael J. Fox Foundation.

出荷温度及び保存条件

製品の状態
Liquid
精製方法
Affinity purification Protein A
バッファー組成
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 50% Tissue culture supernatant, 40% Glycerol (glycerin, glycerine), 0.05% BSA
出荷温度
Blue Ice
短期保存期間
1-2 weeks
短期保存温度
+4°C
長期保存温度
-20°C
分注に関する情報
Upon delivery aliquot

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

The protein LRRK2 also known as leucine-rich repeat kinase 2 or dardarin is an enzyme with a molecular weight of approximately 286 kDa. It functions as a kinase meaning it adds phosphate groups to other proteins which affects their activity. LRRK2 is expressed in various tissues but it is highly abundant in the brain especially in regions such as the striatum and cortex. It has a significant role in cellular signaling processes due to its phosphorylation activity.
Biological function summary

LRRK2 interacts with cellular mechanisms by regulating cytoskeletal dynamics autophagy and vesicle trafficking. It is a part of a larger complex that includes other proteins involved in these processes. The kinase activity of LRRK2 plays an essential part in maintaining neuronal health and function. It influences the process of autophagy which is a way cells clean themselves by removing damaged components and recycling them.

Pathways

The action of LRRK2 is central to the mitogen-activated protein kinase (MAPK) and the mammalian target of rapamycin (mTOR) pathways. In these pathways LRRK2 interacts with other proteins such as mTOR and RPS6KB1. It modulates cellular processes like growth proliferation and response to stressors. Its kinase activity affects the phosphorylation state of targets within the pathways hence influencing biological outcomes like survival and apoptosis.

LRRK2 mutations have a significant connection to Parkinson's disease and Crohn's disease. In Parkinson's disease mutated LRRK2 leads to abnormal protein aggregation linking to proteins such as alpha-synuclein. For Crohn's disease LRRK2 influences the immune response and intestinal inflammation. These connections highlight LRRK2's role in the pathogenesis and contribute to understanding these complex disorders.

製品プロトコール

For this product, it's our understanding that no specific protocols are required. You can visit:

ターゲットの情報

The protein expressed by the gene LRRK2 is a serine/threonine-protein kinase that phosphorylates a wide range of proteins involved in neuronal plasticity, autophagy, and vesicle trafficking. It serves as a key regulator of RAB GTPases by affecting the GTP/GDP exchange and interaction partners of RABs through phosphorylation, targeting proteins like RAB3A, RAB3B, and others. LRRK2 manages the GDP/GTP exchange for RAB8A by phosphorylating 'Thr-72', inhibiting RAB8A's interaction with GDI1/GDI2, and influencing primary ciliogenesis to enhance SHH signaling in the brain. It works with RAB29 in retromer-dependent recycling of proteins between lysosomes and the Golgi. The protein is involved in shaping neuronal morphology in the CNS, synaptic vesicle trafficking, and recruiting SEC16A to assist in ER to Golgi transport. It enhances autophagy via the CaMKK/AMPK pathway and relates to nicotinic acid adenine dinucleotide phosphate receptors and lysosomal activity. LRRK2 phosphorylates PRDX3 and APP, influencing neuron apoptosis. Independently, it inhibits MAPT degradation, fostering MAPT oligomerization. Additionally, LRRK2 possesses GTPase activity that regulates its kinase activity. This supplementary information is collated from multiple sources and compiled automatically.
See full target information LRRK2 phospho S955

文献 (10)

Recent publications for all applications. Explore the full list and refine your search

NPJ Parkinson's disease 9:21 PubMed36750568

2023

Alterations in the LRRK2-Rab pathway in urinary extracellular vesicles as Parkinson's disease and pharmacodynamic biomarkers.

Applications

Unspecified application

Species

Unspecified reactive species

Jean-Marc Taymans,Eugénie Mutez,William Sibran,Laurine Vandewynckel,Claire Deldycke,Séverine Bleuse,Antoine Marchand,Alessia Sarchione,Coline Leghay,Alexandre Kreisler,Clémence Simonin,James Koprich,Guillaume Baille,Luc Defebvre,Kathy Dujardin,Alain Destée,Marie-Christine Chartier-Harlin

The Biochemical journal 479:1759-1783 PubMed35950872

2022

Impact of 100 LRRK2 variants linked to Parkinson's disease on kinase activity and microtubule binding.

Applications

Unspecified application

Species

Unspecified reactive species

Alexia F Kalogeropulou,Elena Purlyte,Francesca Tonelli,Sven M Lange,Melanie Wightman,Alan R Prescott,Shalini Padmanabhan,Esther Sammler,Dario R Alessi

The Biochemical journal 478:3555-3573 PubMed34515301

2021

Impact of Type II LRRK2 inhibitors on signaling and mitophagy.

Applications

Unspecified application

Species

Unspecified reactive species

Anna Tasegian,Francois Singh,Ian G Ganley,Alastair D Reith,Dario R Alessi

Scientific reports 10:17293 PubMed33057100

2020

Mitochondrial DNA damage as a potential biomarker of LRRK2 kinase activity in LRRK2 Parkinson's disease.

Applications

Unspecified application

Species

Unspecified reactive species

C P Gonzalez-Hunt,E A Thacker,C M Toste,S Boularand,S Deprets,L Dubois,L H Sanders

Proceedings of the National Academy of Sciences of 116:14979-14988 PubMed31292254

2019

The dynamic switch mechanism that leads to activation of LRRK2 is embedded in the DFGψ motif in the kinase domain.

Applications

Unspecified application

Species

Unspecified reactive species

Sven H Schmidt,Matthias J Knape,Daniela Boassa,Natascha Mumdey,Alexandr P Kornev,Mark H Ellisman,Susan S Taylor,Friedrich W Herberg

Disease markers 2018:5068701 PubMed30305853

2018

The Protein Expression of PDL1 Is Highly Correlated with Those of eIF2 and ATF4 in Lung Cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Liang-Che Chang,Tzu-Ping Chen,Wei-Ke Kuo,Chung-Ching Hua

Nature communications 9:3465 PubMed30150626

2018

LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation.

Applications

Unspecified application

Species

Unspecified reactive species

Eun-Jin Bae,Dong-Kyu Kim,Changyoun Kim,Michael Mante,Anthony Adame,Edward Rockenstein,Ayse Ulusoy,Michael Klinkenberg,Ga Ram Jeong,Jae Ryul Bae,Cheolsoon Lee,He-Jin Lee,Byung-Dae Lee,Donato A Di Monte,Eliezer Masliah,Seung-Jae Lee

The EMBO journal 37:1-18 PubMed29212815

2017

Rab29 activation of the Parkinson's disease-associated LRRK2 kinase.

Applications

Unspecified application

Species

Unspecified reactive species

Elena Purlyte,Herschel S Dhekne,Adil R Sarhan,Rachel Gomez,Pawel Lis,Melanie Wightman,Terina N Martinez,Francesca Tonelli,Suzanne R Pfeffer,Dario R Alessi

Scientific reports 6:31391 PubMed27503089

2016

Inhibitor treatment of peripheral mononuclear cells from Parkinson's disease patients further validates LRRK2 dephosphorylation as a pharmacodynamic biomarker.

Applications

WB

Species

Unspecified reactive species

G Perera,M Ranola,D B Rowe,G M Halliday,N Dzamko

PloS one 9:e97988 PubMed24836358

2014

Lack of correlation between the kinase activity of LRRK2 harboring kinase-modifying mutations and its phosphorylation at Ser910, 935, and Ser955.

Applications

WB

Species

Unspecified reactive species

Genta Ito,Tetta Fujimoto,Shogo Kamikawaji,Tomoki Kuwahara,Takeshi Iwatsubo
View all publications

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