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ABN2265M

Sigma-Aldrich

Anti-alpha-Synuclein Antibody, oligomer-specific Syn33

from rabbit

Sinónimos:

oligomeric 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

rabbit

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human

technique(s)

ELISA: suitable
immunofluorescence: suitable
inhibition assay: suitable
western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

ambient

target post-translational modification

unmodified

Gene Information

human ... SNCA(6622)

General description

Alpha-synuclein (UniProt: P37840; also known as Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP) is encoded by the SNCA (also known as NACP, PARK1) gene (Gene ID: 6622) in human. Alpha-synuclein is a membrane-bound protein in dopaminergic neurons that is involved in the regulation of dopamine release and transport. It is also reported to induce fibrillization of microtubule-associated protein tau and reduces neuronal responsiveness to various apoptotic stimuli. Aggregation of alpha-synuclein is known to be a causative factor in the development of Parkinson′s disease (PD), which leads to the degeneration of dopaminergic neurons in the substantia nigra (SN) in the midbrain region. Aggregates of alpha-synuclein are present in Lewy bodies. Alpha-synuclein can be phosphorylated, predominantly on serine residues by casein kinase 1. Phosphorylation of Ser129 is reported to be selective and extensive in synucleinopathy lesions and promotes insoluble fibril formation. Mutations in the SNCA gene produce defective alpha-synuclein that induces conformational changes making it more prone to self-aggregation and deposition in Lewy bodies. Mutant forms of alpha-synuclein impair synaptic vesicle formation, elevate cytoplasmic levels of dopamine, and increases superoxide radicals, which lead to oxidative stress and misfolding of alpha-synuclein.

Specificity

This rabbit polyclonal antibody specifically recognizes aggregated form of alpha-synuclein.

Immunogen

Synuclein oligomers from full length human wild-type alpha-synuclein.

Application

Anti-alpha-Synuclein, oligomer-specific Syn33 Antibody, Cat. No. ABN2265, is a highly specific rabbit polyclonal antibody that targets aggregted alpha-synuclein and has been tested in ELISA, Inhibition, Immunofluorescence, and Western Blotting.
Immunofluorescence Analysis: A representative lot detected alpha-Synuclein, oligomers in brain cortices from Parkinson s disease (PD) and dementia with Lewy bodies (DLB) patients (Sengupta, U., et. al. (2015). Biol Psychiatry. 78(10):672-83).

Western Blotting Analysis: A representative lot detected recombinant alpha-Synuclein, oligomers. (Sengupta, U., et. al. (2015). Biol Psychiatry. 78(10):672-83).

Western Blotting Analysis: A representative lot detected recombinant alpha-Synuclein, oligomer. (Courtesy of Dr. Rakez Kayed′s laboratory at University of Texas Medical Branch, Galveston).

ELISA Analysis: A representative lot detected alpha-Synuclein, oligomers in ELISA application (Sengupta, U., et. al. (2015). Biol Psychiatry. 78(10):672-83).

Inhibition Analysis: A representative lot inhibited cytotoxicity exerted alpha-synuclein oligomers in human neuroblastoma SH-SY5Y cells measured by MTT-based assay (Sengupta, U., et. al. (2015). Biol Psychiatry. 78(10):672-83).

Quality

Evaluated by Western Blotting in Alpha Synuclein aggregate.

Western Blotting Analysis: A 1:500 dilution of this antibody detected alpha-Synuclein in alpha Synuclein aggregates.

Target description

~75 kDa observed; 14.46 kDa calculated (monomers). Uncharacterized bands may be observed in some lysate(s).

Physical form

Format: Purified
Purified rabbit polyclonal antibody in PBS.

Other Notes

Concentration: Please refer to lot specific datasheet.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Roberta Cascella et al.
Nature communications, 12(1), 1814-1814 (2021-03-24)
The self-assembly of α-synuclein (αS) into intraneuronal inclusion bodies is a key characteristic of Parkinson's disease. To define the nature of the species giving rise to neuronal damage, we have investigated the mechanism of action of the main αS populations

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