NB300-268
antibody from Novus Biologicals
Targeting: LRRK2
DKFZp434H2111, FLJ45829, PARK8, RIPK7, ROCO2
Antibody data
- Antibody Data
- Antigen structure
- References [38]
- Comments [0]
- Validations
- Western blot [4]
- Immunoprecipitation [1]
- Immunohistochemistry [5]
- Flow cytometry [2]
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Validation data
Reference
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- Product number
- NB300-268 - Provider product page
- Provider
- Novus Biologicals
- Proper citation
- Novus Cat#NB300-268, RRID:AB_10126471
- Product name
- Rabbit Polyclonal LRRK2 Antibody
- Antibody type
- Polyclonal
- Description
- Immunogen affinity purified.
- Reactivity
- Human, Mouse, Bovine
- Host
- Rabbit
- Isotype
- IgG
- Vial size
- 0.1 ml
- Concentration
- 1 mg/ml
- Storage
- Store at 4C. Do not freeze.
Submitted references Generation of two LRRK2 homozygous knockout human induced pluripotent stem cell lines using CRISPR/Cas9.
LRRK2 kinase plays a critical role in manganese-induced inflammation and apoptosis in microglia.
LRRK2 impairs PINK1/Parkin-dependent mitophagy via its kinase activity: pathologic insights into Parkinson's disease.
Miro1 Marks Parkinson's Disease Subset and Miro1 Reducer Rescues Neuron Loss in Parkinson's Models.
Isolated nigral degeneration without pathological protein aggregation in autopsied brains with LRRK2 p.R1441H homozygous and heterozygous mutations.
LRRK2 G2019S Induces Anxiety/Depression-like Behavior before the Onset of Motor Dysfunction with 5-HT(1A) Receptor Upregulation in Mice.
LRRK2 contributes to monocyte dysregulation in Parkinson's disease.
Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1.
Thiol peroxidases ameliorate LRRK2 mutant-induced mitochondrial and dopaminergic neuronal degeneration in Drosophila.
MAP1B rescues LRRK2 mutant-mediated cytotoxicity.
Differential effects of familial parkinson mutations in LRRK2 revealed by a systematic analysis of autophosphorylation.
Sequences located within the N-terminus of the PD-linked LRRK2 lead to increased aggregation and attenuation of 6-hydroxydopamine-induced cell death.
Distinct mechanisms of axonal globule formation in mice expressing human wild type α-synuclein or dementia with Lewy bodies-linked P123H β-synuclein.
LRRK2 kinase inhibition prevents pathological microglial phagocytosis in response to HIV-1 Tat protein.
Re-examination of the dimerization state of leucine-rich repeat kinase 2: predominance of the monomeric form.
The kinase LRRK2 is a regulator of the transcription factor NFAT that modulates the severity of inflammatory bowel disease.
Parkinson's disease-linked LRRK2 is expressed in circulating and tissue immune cells and upregulated following recognition of microbial structures.
LRRK2-mediated neurodegeneration and dysfunction of dopaminergic neurons in a Caenorhabditis elegans model of Parkinson's disease.
Deletion of the WD40 domain of LRRK2 in Zebrafish causes Parkinsonism-like loss of neurons and locomotive defect.
Identification of the autophosphorylation sites of LRRK2.
Leucine-Rich Repeat Kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease.
LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model.
Tauopathies with parkinsonism: clinical spectrum, neuropathologic basis, biological markers, and treatment options.
LRRK2 and neurodegeneration.
Leucine-rich repeat kinase 2 expression leads to aggresome formation that is not associated with alpha-synuclein inclusions.
LRRK2 modulates vulnerability to mitochondrial dysfunction in Caenorhabditis elegans.
Lrrk2 interaction with alpha-synuclein in diffuse Lewy body disease.
LRRK2 is a component of granular alpha-synuclein pathology in the brainstem of Parkinson's disease.
Screening for the LRRK2 G2019S and codon-1441 mutations in a pathological series of parkinsonian syndromes and frontotemporal lobar degeneration.
Lrrk2 and chronic inflammation are linked to pallido-ponto-nigral degeneration caused by the N279K tau mutation.
Leucine-rich repeat kinase 2 associates with lipid rafts.
Localization of Parkinson's disease-associated LRRK2 in normal and pathological human brain.
Mutations in LRRK2/dardarin associated with Parkinson disease are more toxic than equivalent mutations in the homologous kinase LRRK1.
A comparative analysis of leucine-rich repeat kinase 2 (Lrrk2) expression in mouse brain and Lewy body disease.
GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease.
LRRK2 expression in normal and pathologic human brain and in human cell lines.
LRRK2 protein is a component of Lewy bodies.
LRRK2 in Parkinson's disease and dementia with Lewy bodies.
Chen S, Luo Z, Ward C, Ibañez DP, Liu H, Zhong X, Sharma NK, Qin B, Fan W, Wang D
Stem cell research 2020 May;45:101804
Stem cell research 2020 May;45:101804
LRRK2 kinase plays a critical role in manganese-induced inflammation and apoptosis in microglia.
Kim J, Pajarillo E, Rizor A, Son DS, Lee J, Aschner M, Lee E
PloS one 2019;14(1):e0210248
PloS one 2019;14(1):e0210248
LRRK2 impairs PINK1/Parkin-dependent mitophagy via its kinase activity: pathologic insights into Parkinson's disease.
Bonello F, Hassoun SM, Mouton-Liger F, Shin YS, Muscat A, Tesson C, Lesage S, Beart PM, Brice A, Krupp J, Corvol JC, Corti O
Human molecular genetics 2019 May 15;28(10):1645-1660
Human molecular genetics 2019 May 15;28(10):1645-1660
Miro1 Marks Parkinson's Disease Subset and Miro1 Reducer Rescues Neuron Loss in Parkinson's Models.
Hsieh CH, Li L, Vanhauwaert R, Nguyen KT, Davis MD, Bu G, Wszolek ZK, Wang X
Cell metabolism 2019 Dec 3;30(6):1131-1140.e7
Cell metabolism 2019 Dec 3;30(6):1131-1140.e7
Isolated nigral degeneration without pathological protein aggregation in autopsied brains with LRRK2 p.R1441H homozygous and heterozygous mutations.
Takanashi M, Funayama M, Matsuura E, Yoshino H, Li Y, Tsuyama S, Takashima H, Nishioka K, Hattori N
Acta neuropathologica communications 2018 Oct 17;6(1):105
Acta neuropathologica communications 2018 Oct 17;6(1):105
LRRK2 G2019S Induces Anxiety/Depression-like Behavior before the Onset of Motor Dysfunction with 5-HT(1A) Receptor Upregulation in Mice.
Lim J, Bang Y, Choi JH, Han A, Kwon MS, Liu KH, Choi HJ
The Journal of neuroscience : the official journal of the Society for Neuroscience 2018 Feb 14;38(7):1611-1621
The Journal of neuroscience : the official journal of the Society for Neuroscience 2018 Feb 14;38(7):1611-1621
LRRK2 contributes to monocyte dysregulation in Parkinson's disease.
Bliederhaeuser C, Zondler L, Grozdanov V, Ruf WP, Brenner D, Melrose HL, Bauer P, Ludolph AC, Gillardon F, Kassubek J, Weishaupt JH, Danzer KM
Acta neuropathologica communications 2016 Nov 24;4(1):123
Acta neuropathologica communications 2016 Nov 24;4(1):123
Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1.
Nucifora FC Jr, Nucifora LG, Ng CH, Arbez N, Guo Y, Roby E, Shani V, Engelender S, Wei D, Wang XF, Li T, Moore DJ, Pletnikova O, Troncoso JC, Sawa A, Dawson TM, Smith W, Lim KL, Ross CA
Nature communications 2016 Jun 7;7:11792
Nature communications 2016 Jun 7;7:11792
Thiol peroxidases ameliorate LRRK2 mutant-induced mitochondrial and dopaminergic neuronal degeneration in Drosophila.
Angeles DC, Ho P, Chua LL, Wang C, Yap YW, Ng C, Zhou Zd, Lim KL, Wszolek ZK, Wang HY, Tan EK
Human molecular genetics 2014 Jun 15;23(12):3157-65
Human molecular genetics 2014 Jun 15;23(12):3157-65
MAP1B rescues LRRK2 mutant-mediated cytotoxicity.
Chan SL, Chua LL, Angeles DC, Tan EK
Molecular brain 2014 Apr 22;7:29
Molecular brain 2014 Apr 22;7:29
Differential effects of familial parkinson mutations in LRRK2 revealed by a systematic analysis of autophosphorylation.
Kamikawaji S, Ito G, Sano T, Iwatsubo T
Biochemistry 2013 Sep 3;52(35):6052-62
Biochemistry 2013 Sep 3;52(35):6052-62
Sequences located within the N-terminus of the PD-linked LRRK2 lead to increased aggregation and attenuation of 6-hydroxydopamine-induced cell death.
Pandey N, Fahey MT, Jong YJ, O'Malley KL
PloS one 2012;7(9):e45149
PloS one 2012;7(9):e45149
Distinct mechanisms of axonal globule formation in mice expressing human wild type α-synuclein or dementia with Lewy bodies-linked P123H β-synuclein.
Sekigawa A, Fujita M, Sekiyama K, Takamatsu Y, Hatano T, Rockenstein E, La Spada AR, Masliah E, Hashimoto M
Molecular brain 2012 Sep 26;5:34
Molecular brain 2012 Sep 26;5:34
LRRK2 kinase inhibition prevents pathological microglial phagocytosis in response to HIV-1 Tat protein.
Marker DF, Puccini JM, Mockus TE, Barbieri J, Lu SM, Gelbard HA
Journal of neuroinflammation 2012 Nov 29;9:261
Journal of neuroinflammation 2012 Nov 29;9:261
Re-examination of the dimerization state of leucine-rich repeat kinase 2: predominance of the monomeric form.
Ito G, Iwatsubo T
The Biochemical journal 2012 Feb 1;441(3):987-94
The Biochemical journal 2012 Feb 1;441(3):987-94
The kinase LRRK2 is a regulator of the transcription factor NFAT that modulates the severity of inflammatory bowel disease.
Liu Z, Lee J, Krummey S, Lu W, Cai H, Lenardo MJ
Nature immunology 2011 Oct 9;12(11):1063-70
Nature immunology 2011 Oct 9;12(11):1063-70
Parkinson's disease-linked LRRK2 is expressed in circulating and tissue immune cells and upregulated following recognition of microbial structures.
Hakimi M, Selvanantham T, Swinton E, Padmore RF, Tong Y, Kabbach G, Venderova K, Girardin SE, Bulman DE, Scherzer CR, LaVoie MJ, Gris D, Park DS, Angel JB, Shen J, Philpott DJ, Schlossmacher MG
Journal of neural transmission (Vienna, Austria : 1996) 2011 May;118(5):795-808
Journal of neural transmission (Vienna, Austria : 1996) 2011 May;118(5):795-808
LRRK2-mediated neurodegeneration and dysfunction of dopaminergic neurons in a Caenorhabditis elegans model of Parkinson's disease.
Yao C, El Khoury R, Wang W, Byrd TA, Pehek EA, Thacker C, Zhu X, Smith MA, Wilson-Delfosse AL, Chen SG
Neurobiology of disease 2010 Oct;40(1):73-81
Neurobiology of disease 2010 Oct;40(1):73-81
Deletion of the WD40 domain of LRRK2 in Zebrafish causes Parkinsonism-like loss of neurons and locomotive defect.
Sheng D, Qu D, Kwok KH, Ng SS, Lim AY, Aw SS, Lee CW, Sung WK, Tan EK, Lufkin T, Jesuthasan S, Sinnakaruppan M, Liu J
PLoS genetics 2010 Apr 22;6(4):e1000914
PLoS genetics 2010 Apr 22;6(4):e1000914
Identification of the autophosphorylation sites of LRRK2.
Kamikawaji S, Ito G, Iwatsubo T
Biochemistry 2009 Nov 24;48(46):10963-75
Biochemistry 2009 Nov 24;48(46):10963-75
Leucine-Rich Repeat Kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease.
Venderova K, Kabbach G, Abdel-Messih E, Zhang Y, Parks RJ, Imai Y, Gehrke S, Ngsee J, Lavoie MJ, Slack RS, Rao Y, Zhang Z, Lu B, Haque ME, Park DS
Human molecular genetics 2009 Nov 15;18(22):4390-404
Human molecular genetics 2009 Nov 15;18(22):4390-404
LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model.
Alegre-Abarrategui J, Christian H, Lufino MM, Mutihac R, Venda LL, Ansorge O, Wade-Martins R
Human molecular genetics 2009 Nov 1;18(21):4022-34
Human molecular genetics 2009 Nov 1;18(21):4022-34
Tauopathies with parkinsonism: clinical spectrum, neuropathologic basis, biological markers, and treatment options.
Ludolph AC, Kassubek J, Landwehrmeyer BG, Mandelkow E, Mandelkow EM, Burn DJ, Caparros-Lefebvre D, Frey KA, de Yebenes JG, Gasser T, Heutink P, Höglinger G, Jamrozik Z, Jellinger KA, Kazantsev A, Kretzschmar H, Lang AE, Litvan I, Lucas JJ, McGeer PL, Melquist S, Oertel W, Otto M, Paviour D, Reum T, Saint-Raymond A, Steele JC, Tolnay M, Tumani H, van Swieten JC, Vanier MT, Vonsattel JP, Wagner S, Wszolek ZK, Reisensburg Working Group for Tauopathies With Parkinsonism.
European journal of neurology 2009 Mar;16(3):297-309
European journal of neurology 2009 Mar;16(3):297-309
LRRK2 and neurodegeneration.
Santpere G, Ferrer I
Acta neuropathologica 2009 Mar;117(3):227-46
Acta neuropathologica 2009 Mar;117(3):227-46
Leucine-rich repeat kinase 2 expression leads to aggresome formation that is not associated with alpha-synuclein inclusions.
Waxman EA, Covy JP, Bukh I, Li X, Dawson TM, Giasson BI
Journal of neuropathology and experimental neurology 2009 Jul;68(7):785-96
Journal of neuropathology and experimental neurology 2009 Jul;68(7):785-96
LRRK2 modulates vulnerability to mitochondrial dysfunction in Caenorhabditis elegans.
Saha S, Guillily MD, Ferree A, Lanceta J, Chan D, Ghosh J, Hsu CH, Segal L, Raghavan K, Matsumoto K, Hisamoto N, Kuwahara T, Iwatsubo T, Moore L, Goldstein L, Cookson M, Wolozin B
The Journal of neuroscience : the official journal of the Society for Neuroscience 2009 Jul 22;29(29):9210-8
The Journal of neuroscience : the official journal of the Society for Neuroscience 2009 Jul 22;29(29):9210-8
Lrrk2 interaction with alpha-synuclein in diffuse Lewy body disease.
Qing H, Zhang Y, Deng Y, McGeer EG, McGeer PL
Biochemical and biophysical research communications 2009 Dec 25;390(4):1229-34
Biochemical and biophysical research communications 2009 Dec 25;390(4):1229-34
LRRK2 is a component of granular alpha-synuclein pathology in the brainstem of Parkinson's disease.
Alegre-Abarrategui J, Ansorge O, Esiri M, Wade-Martins R
Neuropathology and applied neurobiology 2008 Jun;34(3):272-83
Neuropathology and applied neurobiology 2008 Jun;34(3):272-83
Screening for the LRRK2 G2019S and codon-1441 mutations in a pathological series of parkinsonian syndromes and frontotemporal lobar degeneration.
Gaig C, Ezquerra M, Martí MJ, Valldeoriola F, Muñoz E, Lladó A, Rey MJ, Cardozo A, Molinuevo JL, Tolosa E
Journal of the neurological sciences 2008 Jul 15;270(1-2):94-8
Journal of the neurological sciences 2008 Jul 15;270(1-2):94-8
Lrrk2 and chronic inflammation are linked to pallido-ponto-nigral degeneration caused by the N279K tau mutation.
Miklossy J, Qing H, Guo JP, Yu S, Wszolek ZK, Calne D, McGeer EG, McGeer PL
Acta neuropathologica 2007 Sep;114(3):243-54
Acta neuropathologica 2007 Sep;114(3):243-54
Leucine-rich repeat kinase 2 associates with lipid rafts.
Hatano T, Kubo S, Imai S, Maeda M, Ishikawa K, Mizuno Y, Hattori N
Human molecular genetics 2007 Mar 15;16(6):678-90
Human molecular genetics 2007 Mar 15;16(6):678-90
Localization of Parkinson's disease-associated LRRK2 in normal and pathological human brain.
Higashi S, Biskup S, West AB, Trinkaus D, Dawson VL, Faull RL, Waldvogel HJ, Arai H, Dawson TM, Moore DJ, Emson PC
Brain research 2007 Jun 25;1155:208-19
Brain research 2007 Jun 25;1155:208-19
Mutations in LRRK2/dardarin associated with Parkinson disease are more toxic than equivalent mutations in the homologous kinase LRRK1.
Greggio E, Lewis PA, van der Brug MP, Ahmad R, Kaganovich A, Ding J, Beilina A, Baker AK, Cookson MR
Journal of neurochemistry 2007 Jul;102(1):93-102
Journal of neurochemistry 2007 Jul;102(1):93-102
A comparative analysis of leucine-rich repeat kinase 2 (Lrrk2) expression in mouse brain and Lewy body disease.
Melrose HL, Kent CB, Taylor JP, Dachsel JC, Hinkle KM, Lincoln SJ, Mok SS, Culvenor JG, Masters CL, Tyndall GM, Bass DI, Ahmed Z, Andorfer CA, Ross OA, Wszolek ZK, Delldonne A, Dickson DW, Farrer MJ
Neuroscience 2007 Jul 29;147(4):1047-58
Neuroscience 2007 Jul 29;147(4):1047-58
GTP binding is essential to the protein kinase activity of LRRK2, a causative gene product for familial Parkinson's disease.
Ito G, Okai T, Fujino G, Takeda K, Ichijo H, Katada T, Iwatsubo T
Biochemistry 2007 Feb 6;46(5):1380-8
Biochemistry 2007 Feb 6;46(5):1380-8
LRRK2 expression in normal and pathologic human brain and in human cell lines.
Miklossy J, Arai T, Guo JP, Klegeris A, Yu S, McGeer EG, McGeer PL
Journal of neuropathology and experimental neurology 2006 Oct;65(10):953-63
Journal of neuropathology and experimental neurology 2006 Oct;65(10):953-63
LRRK2 protein is a component of Lewy bodies.
Zhu X, Siedlak SL, Smith MA, Perry G, Chen SG
Annals of neurology 2006 Nov;60(5):617-8; author reply 618-9
Annals of neurology 2006 Nov;60(5):617-8; author reply 618-9
LRRK2 in Parkinson's disease and dementia with Lewy bodies.
Zhu X, Babar A, Siedlak SL, Yang Q, Ito G, Iwatsubo T, Smith MA, Perry G, Chen SG
Molecular neurodegeneration 2006 Nov 30;1:17
Molecular neurodegeneration 2006 Nov 30;1:17
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Supportive validation
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Western Blot: LRRK2 Antibody [NB300-268] - Detection of LRRK2 in HeLa whole cell lysate (RIPA) using NB300-268. 1:5000 dilution, 1 minute ECL detection.
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Western Blot: LRRK2 Antibody [NB300-268] - Detection of LRRK2 in 50 ug of crude bovine brain membrane.
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Western Blot: LRRK2 Antibody [NB300-268] - Western blotting of LRRK2. Recombinant LRRK2 (arrowhead) from transfected (+) HEK 293T and M17 cells was specifically recognized by all four LRRK2 antibodies (Ab1, Ab2, Ab3, and Ab4) used in this study. LRRK2 was not recognized in non-transfected cells (-). Image collected and cropped by CiteAb from the following publication (http://molecularneurodegeneration.biomedcentral.com/articles/10.1186/1750-1326-1-17), licensed under a CC-BY licence.
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- Novus Biologicals (provider)
- Main image
- Experimental details
- Western Blot: LRRK2 Antibody [NB300-268] - LRRK2 N-terminal sequences show increased aggregation. Western blots of cell lysates of SH-SY5Y cells transfected with indicated LRRK2 construct showed equal expression of the LRRK2 protein with anti-HA (top panel) or anti-C-terminal- (bottom panel) LRRK2 antibody. Equal lysate loading is indicated by Beta-actin loading control. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0045149) licensed under a CC-BY licence.
Supportive validation
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- Novus Biologicals (provider)
- Main image
- Experimental details
- Immunoprecipitation: LRRK2 Antibody [NB300-268] - IP of LRRK2 from SH-SY5Y cell lysate followed by an autophosphorylation assay using NB300-268. Lane 1 Rabbit IgG, Lanes 2 and 3 NB300-268.
Supportive validation
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- Novus Biologicals (provider)
- Main image
- Experimental details
- Immunohistochemistry-Frozen: LRRK2 Antibody [NB300-268] - Staining as described in PMID 24312256. Image from verified customer review.
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- Novus Biologicals (provider)
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- Experimental details
- Immunohistochemistry-Paraffin: LRRK2 Antibody [NB300-268] - Staining of human brain, Putamen, Neurons and Glia using a 60X magnification.
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- Novus Biologicals (provider)
- Main image
- Experimental details
- Immunohistochemistry-Paraffin: LRRK2 Antibody [NB300-268] - LRRK2 accumulates in globules in alphaS tg mice. Triple immunofluorescence for alphaS, LRRK2 and Rab5B for basal ganglia in alphaS tg mice. LRRK2 and Rab5B were colocalized in axon terminal (arrow), but were not colocalized in the alphaS-globule (arrowhead) Scale bar = 10 um for all panels. Image collected and cropped by CiteAb from the following publication (http://molecularbrain.biomedcentral.com/articles/10.1186/1756-6606-5-34), licensed under a CC-BY licence.
- Submitted by
- Novus Biologicals (provider)
- Main image
- Experimental details
- Immunohistochemistry-Paraffin: LRRK2 Antibody [NB300-268] - Immunocytochemistry of LRRK2 in PD using antibodies (Ab1, Ab4) raised against sequences corresponding to various regions shown on the schematic diagram of LRRK2 (red bars) were used on brainstem sections of PD. Scale bars: 10 um (top); E-L = 100 um (bottom). Image collected and cropped by CiteAb from the following publication (http://molecularneurodegeneration.biomedcentral.com/articles/10.1186/1750-1326-1-17), licensed under a CC-BY licence.
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- Novus Biologicals (provider)
- Main image
- Experimental details
- Immunohistochemistry-Paraffin: LRRK2 Antibody [NB300-268] - Specificity of immunostaining for LRRK2. Specificity of the antibodies used for immunocytochemistry was determined by performing adsorptions with the corresponding peptide sequences. Immunochemical localization of LBs (arrows) by Ab1 against LRRK2900-100 (left) was blocked using respective peptide antigens (right). Adjacent sections with LB within pigmented neurons from the substantia nigra of a case of PD were used. Scale bar: 20 um. Image collected and cropped by CiteAb from the following publication (http://molecularneurodegeneration.biomedcentral.com/articles/10.1186/1750-1326-1-17), licensed under a CC-BY licence.
Supportive validation
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- Novus Biologicals (provider)
- Main image
- Experimental details
- Flow Cytometry: LRRK2 Antibody [NB300-268] - Analysis using the Alexa Fluor 647 conjugate of NB300-268. Staining of LRRK2 in normal human peripheral blood cells (anticoagulated Lithium-Heparin) using anti-LRRK2 antibody conjugated with AF647. The primary antibody was used at a dilution of 1:200 and incubated for 20 min at room temperature. Image from verified customer review.
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- Main image
- Experimental details
- Flow Cytometry: LRRK2 Antibody [NB300-268] - An intracellular stain was performed on U2OS cells with LRRK Antibody NB300-268AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.