Our lab has not characterized the specificity of this antibody, but according to the literature, this antibody is known to be oligomer-specific. The following citation containing this information may be of interest for reference: In Vivo Protein Complementation Demonstrates Presynaptic α-Synuclein Oligomerization and Age-Dependent Accumulation of 8-16-mer Oligomer Species, Journal: Cell Rep. 2019 Nov 26;29(9):2862-2874.e9, DOI: 10.1016/j.celrep.2019.10.089, PMID: 31775051
MABN389
Anti-α-Synuclein (SNCA) Antibody
mouse monoclonal, 5G4
Sinónimos:
Aggregated a-synuclein, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP
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About This Item
Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
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Nombre del producto
Anti-Aggregated a-Synuclein Antibody, clone 5G4, clone 5G4, from mouse, purified by affinity chromatography
origen biológico
mouse
Nivel de calidad
forma del anticuerpo
affinity purified immunoglobulin
tipo de anticuerpo
primary antibodies
clon
5G4, monoclonal
purificado por
affinity chromatography
reactividad de especies
human
técnicas
ELISA: suitable
immunohistochemistry: suitable
western blot: suitable
isotipo
IgG1κ
Nº de acceso NCBI
Nº de acceso UniProt
Condiciones de envío
dry ice
modificación del objetivo postraduccional
unmodified
Información sobre el gen
human ... SNCA(6622)
Descripción general
α-Synuclein, also known as Non-A beta component of AD amyloid or Non-A4 component of amyloid, or NACP, and encoded by the gene SNCA/NACP/PARK1, is a protein originally identified as non-Abeta component protein (NACP) in the amyloid enriched fraction isolated from Alzheimer’s brain tissue. α-Synuclein is expressed in neural tissue and non-neural tissues too. In neurons, α-Synuclein is localized to the nucleus, presynaptic termini and mitochondria of certain brain regions. α-Synuclein is a molecular chaperone that binds various proteins and compounds including synaptobrevin-2 protein and membrane phospholipids and is involved in vesicle trafficking and membrane transport within neurons. Natural, non-mutated α-Synuclein has autoproteolytic activity and naturally forms stable alpha helical tetramers. However, mutated α-Synuclein can aggregate to form insoluble pathological complexes such as Lewy Bodies inside neurons. Lewy Bodies also contain ubiquitin and it is thought that they are evidence of disrupted proteasome function with regards to α-synuclein but research is still continuing.
Pepscan epitope mapping experiments showed that the epitope of 5G4 seems to be hidden inside full-length a-synuclein in aqueous solution, and this fact could depend on a specific conformation of the molecule. Thus, after conformational change, like b-sheet building, the binding structure of 5G4 may be accessible in biological samples.
This antibody can be used as a sandwich ELISA pair with Cat. No. MABN633, Anti-a-Synuclein, clone 10D2.
Pepscan epitope mapping experiments showed that the epitope of 5G4 seems to be hidden inside full-length a-synuclein in aqueous solution, and this fact could depend on a specific conformation of the molecule. Thus, after conformational change, like b-sheet building, the binding structure of 5G4 may be accessible in biological samples.
This antibody can be used as a sandwich ELISA pair with Cat. No. MABN633, Anti-a-Synuclein, clone 10D2.
Inmunógeno
KLH-conjugated linear peptide corresponding to human Aggregated a-Synuclein.
Aplicación
Research Category
Neuroscience
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Neurodegenerative Diseases
This Anti-Aggregated a-Synuclein Antibody, clone 5G4 is validated for use in western blotting, IHC & ELISA for the detection of Aggregated a-Synuclein.
Western Blotting Analysis: 2 µg/mL from a representative lot detected Aggregated a-Synuclein in human brain tissue lysate.
ELISA Analysis: A representative lot from an independent laboratory detected Aggregated a-Synuclein in a sandwich ELISA with Cat. No. MABN633, Anti-a-Synuclein, clone 5G4 (Kovacs, G. G., et al. (2012). Acta Neuropathol. 123(1):37-50.).
ELISA Analysis: A representative lot from an independent laboratory detected Aggregated a-Synuclein in a sandwich ELISA with Cat. No. MABN633, Anti-a-Synuclein, clone 5G4 (Kovacs, G. G., et al. (2012). Acta Neuropathol. 123(1):37-50.).
Calidad
Evaluated by Immunohistochemistry in brain tissue from a Parkinson′s disease patient.
Immunohistochemistry Analysis: A representative lot detected Aggregated a-Synuclein in brain tissue from a Parkinson′s disease patient.
Immunohistochemistry Analysis: A representative lot detected Aggregated a-Synuclein in brain tissue from a Parkinson′s disease patient.
Descripción de destino
~15 kDa observed. Uncharacterized band(s) may be observed in some cell lysates.
Forma física
Affinity purified
Purified mouse monoclonal IgG1κ in buffer containing PBS without preservatives.
Almacenamiento y estabilidad
Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Cláusula de descargo de responsabilidad
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Opcional
Referencia del producto
Descripción
Precios
Código de clase de almacenamiento
12 - Non Combustible Liquids
Clase de riesgo para el agua (WGK)
WGK 2
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Rizwanul Haque et al.
Oncotarget, 11(6), 634-649 (2020-02-29)
Insulin-signalling is an important pathway in multiple cellular functions and organismal ageing across the taxa. A strong association of insulin-signalling with Parkinson's disease (PD) has been proposed but the exact nature of molecular events and genetic associations are yet to
Dalila G Ordonez et al.
Neuron, 97(1), 108-124 (2017-12-19)
Genetics and neuropathology strongly link α-synuclein aggregation and neurotoxicity to the pathogenesis of Parkinson's disease and related α-synucleinopathies. Here we describe a new Drosophila model of α-synucleinopathy based on widespread expression of wild-type human α-synuclein, which shows robust neurodegeneration, early-onset
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Journal of neurochemistry, 136(1), 172-185 (2015-10-16)
Together with Parkinson's disease (PD) and dementia with Lewy bodies, multiple system atrophy (MSA) is a member of a diverse group of neurodegenerative disorders termed α-synucleinopathies. Previously, it has been shown that α-synuclein, parkin, and synphilin-1 display disease-specific transcription patterns
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Chaperone-mediated autophagy (CMA) is an autophagy-lysosome pathway (ALP) that is different from the other two lysosomal pathways, namely, macroautophagy and microautophagy, and can selectively degrade cytosolic proteins in lysosomes without vesicle formation. CMA activity declines in neurodegenerative diseases such as
Julia Marschallinger et al.
Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics, 17(3), 1061-1074 (2020-02-20)
Dementia with Lewy bodies (DLB) represents a huge medical need as it accounts for up to 30% of all dementia cases, and there is no cure available. The underyling spectrum of pathology is complex and creates a challenge for targeted
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