MABN389
Anti-Aggregated a-Synuclein Antibody, clone 5G4
clone 5G4, from mouse, purified by affinity chromatography
Synonym(s):
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
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.
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
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.).
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.
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.
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.
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Description
Pricing
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Ursula Unterberger et al.
Clinical neuropathology, 33(5), 329-334 (2014-08-19)
With the aim to evaluate the significance and reliability of detecting disease-specific α-synuclein in the cerebrospinal fluid (CSF) we developed an ELISA and bead-assay. We used a commercial antibody (5G4) that does not bind to the physiological monomeric form of
In vivo markers of Parkinson's disease and dementia with Lewy bodies: current value of the 5G4 ?-synuclein antibody.
Maetzler, W; Pilotto, A; Apel, A; Deuschle, C; Kuebart, G; Heinzel, S; Liepelt-Scarfone et al.
Acta neuropathologica null
Intracellular processing of disease-associated ?-synuclein in the human brain suggests prion-like cell-to-cell spread.
Kovacs, GG; Breydo, L; Green, R; Kis, V; Puska, G; Lorincz, P; Perju-Dumbrava, L; Giera et al.
Neurobiology of Disease null
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
Hugo Vicente Miranda et al.
Brain : a journal of neurology, 140(5), 1399-1419 (2017-04-12)
α-Synuclein misfolding and aggregation is a hallmark in Parkinson's disease and in several other neurodegenerative diseases known as synucleinopathies. The toxic properties of α-synuclein are conserved from yeast to man, but the precise underpinnings of the cellular pathologies associated are
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