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MABN389

Sigma-Aldrich

Anti-Aggregated a-Synuclein Antibody, clone 5G4

clone 5G4, from mouse, purified by affinity chromatography

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Synonym(s):
Aggregated a-synuclein, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

affinity purified immunoglobulin

antibody product type

primary antibodies

clone

5G4, monoclonal

purified by

affinity chromatography

species reactivity

human

technique(s)

ELISA: suitable
immunohistochemistry: suitable
western blot: suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... SNCA(6622)

General description

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.

Immunogen

KLH-conjugated linear peptide corresponding to human Aggregated a-Synuclein.

Application

Research Category
Neuroscience
Research Sub Category
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.).

Quality

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.

Target description

~15 kDa observed. Uncharacterized band(s) may be observed in some cell lysates.

Physical form

Affinity purified
Purified mouse monoclonal IgG1κ in buffer containing PBS without preservatives.

Storage and Stability

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.

Disclaimer

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.

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Tomasz Brudek et al.
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
Leping Sun et al.
Brain and behavior, 9(8), e01352-e01352 (2019-07-10)
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
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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