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MABN633

Sigma-Aldrich

Anti-a-Synuclein, clone 10D2 Antibody

clone 10D2, from mouse, purified by affinity chromatography

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

biological source

mouse

Quality Level

antibody form

affinity purified immunoglobulin

antibody product type

primary antibodies

clone

10D2, 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

wet ice

target post-translational modification

unmodified

Gene Information

human ... SNCA(6622)

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MABN1817MABN2419MABN826
biological source

mouse

biological source

mouse

biological source

mouse

biological source

mouse

clone

10D2, monoclonal

clone

2F12, monoclonal

clone

LS4-1B1, monoclonal

clone

81A, monoclonal

species reactivity

human

species reactivity

rat, human, mouse

species reactivity

human, mouse

species reactivity

mouse, human

antibody form

affinity purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

purified antibody

shipped in

wet ice

shipped in

ambient

shipped in

-

shipped in

dry ice

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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.
This antibody can be used as a sandwich ELISA pair with Cat. No. MABN389, Anti-Aggregated a-Synuclein, clone 5G4.

Immunogen

Recombinant protein corresponding to human Synuclein.

Application

Anti-a-Synuclein, clone 10D2 Antibody is an antibody against a-Synuclein for use in western blotting, IHC & ELISA.
Immunohistochemistry Analysis: A representative lot detected aggregated a-Synuclein in human brain tissues.

ELISA Analysis: A representative lot from an independent laboratory detected aggregated a-Synuclein in a sandwich ELISA with Cat. No. MABN389, Anti-Aggregated a-Synuclein, clone 5G4 (Kovacs, G. G., et al. (2012). Acta Neuropathol. 123(1):37-50.).

Quality

Evaluated by Western Blotting in human brain tissue lysate.

Western Blotting Analysis: 1.5 µg/mL of this antibody detected a-Synuclein in 10 µg of human brain tissue lysate.

Target description

~15 kDa observed

Linkage

Replaces: 04-1053

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Benedict Tanudjojo et al.
Nature communications, 12(1), 3817-3817 (2021-06-23)
α-Synuclein is critical in the pathogenesis of Parkinson's disease and related disorders, yet it remains unclear how its aggregation causes degeneration of human dopaminergic neurons. In this study, we induced α-synuclein aggregation in human iPSC-derived dopaminergic neurons using fibrils generated

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