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MABN1818

Sigma-Aldrich

Anti-α-Synuclein Antibody, clone SOY1

clone SOY1, from mouse

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Synonym(s):
Alpha-synuclein, NACP, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Synuclein alpha-140
eCl@ss:
32160702

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

SOY1, monoclonal

species reactivity

mouse, human

species reactivity (predicted by homology)

rat (based on 100% sequence homology)

technique(s)

ELISA: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG2bκ

NCBI accession no.

UniProt accession no.

shipped in

ambient

target post-translational modification

unmodified

Gene Information

human ... SNCA(6622)

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This Item
MABN1817MABN2419MABN826
clone

SOY1, monoclonal

clone

2F12, monoclonal

clone

LS4-1B1, monoclonal

clone

81A, monoclonal

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

purified antibody

Gene Information

human ... SNCA(6622)

Gene Information

human ... SNCA(6622)

Gene Information

human ... SNCA(6622)

Gene Information

human ... SNCA(6622)

species reactivity

mouse, human

species reactivity

rat, human, mouse

species reactivity

human, mouse

species reactivity

mouse, human

isotype

IgG2bκ

isotype

IgG2bκ

isotype

IgG1κ

isotype

IgG2aκ

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General description

Alpha-synuclein (UniProt P37840; also known as NACP, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Synuclein alpha-140) is encoded by the SNCA (also known as NACP, PARK1, PARK4) gene (Gene ID 6622) in human. Pathological aggregates are common features of many neurodegenerative diseases, such as tau neurofibrillary tangles (NFTs) in Alzheimer’s disease (AD) and frontotemporal degeneration, and α-synuclein (α-syn or αS) Lewy bodies (LBs) in Parkinson’s disease (PD) and dementia with LBs (DLB). Alpha-synuclein is a phospholipid-binding protein concentrated in presynaptic terminals where it promotes SNARE complex formation and modulates synaptic functions. Alpha-synuclein is the major component of pathologic inclusions that characterize PD, DLB, and multiple system atrophy (MSA). Research shows that αS exists not only as unfolded monomers, but in large part also as multimers, principally as ~60 kDa tetramers composed of four N-acetylated αS, that assume α-helical conformation and resist aggregation. PD-causing αS missense mutations are found to shift cellular αS from tetramers/multimers to monomers, indicating that decreased α-helical tetramers and increased unfolded monomers initiate pathogenesis. In addition, both casein kinase-1 (CK-1) and CK-2 can catalyze the phosphorylation of αS on Ser129, and Ser129-phosphorylated αS is found in αS inclusions.

Specificity

Clone SOY1 detected both wild-type alpha-synuclein and fPD mutants (Dettmer, U., et al. (2015). Nat. Commun. 6:7314). Clone SOY1 targets a C-terminal half epitope present in all three human spliced iisoforms, NACP140, NACP112, and NACP126, reported by UniProt (P37840). Clone SOY1 also exhibits murine cross-reactivity, albeit at a lower sensitivity than that of human alpha-synuclein.

Immunogen

Purified human erythrocyte alpha-synuclein.

Application

Anti-α-Synuclein, clone SOY1 Antibody, Cat. No. MABN1818, is a highly specific mouse monoclonal antibody that targets -synuclein and has been tested in ELISA, Immunohistochemistry (Paraffin), Immunoprecipitation, and Western Blotting.
Immunohistochemistry Analysis: A 1:250 dilution from a representative lot detected α-synuclein in human cerebellum, cerebral cortex, and pancreas tissue sections.

ELISA Analysis: A 1:74.6 dilution from a representative lot (preconjugated with Sulfo tag) detected recombinant human α-synuclein (0.2-40 ng/mL) captured by clone 2F12 (Cat. No. MABN1817; 200 ng/30 µL/well for coating) in a sandwich ELISA application (Courtesy of Tim Bartels, Ph.D., Brigham and Women′s Hospital, Boston, MA, U.S.A.).

Immunoprecipitation Analysis: 4 µL from a representative lot immunoprecipitated α-synuclein from 50 µg of HEL human erythroleukemia cell lysate (Courtesy of Tim Bartels, Ph.D., Brigham and Women′s Hospital, Boston, MA, U.S.A.).

ELISA Analysis: A representative lot (preconjugated with Sulfo tag) detected both endogenous alpha-synuclein (αS) from human cortical homogenate, as well the exogenously expressed wild type and familial PD (fPD) αS mutants (A30P, E46K, H50Q, G51D, A53T) from sytosolic extracts of transfected M17D human neuroblastoma cells in a sandwich ELISA application utilizing clone 2F12 (Cat. No. MABN1817) as the capture antibody (Dettmer, U., et al. (2015). Nat. Commun. 6:7314).

ELISA Analysis: A representative lot (preconjugated with Sulfo tag) detected both pre-aggregated fibrillar recombinant -synuclein as well as partially purified Lewy bodies (LBs) from a DLB (dementia with LBs) patient with or without prior sample denaturing by boiling with 2% SDS in a sandwich ELISA application utilizing clone 2F12 (Cat. No. MABN1817) as the capture antibody (Dettmer, U., et al. (2015). Nat. Commun. 6:7314).

Quality

Evaluated by Western Blotting in human fetal brain tissue lysate.

Western Blotting Analysis: A 1:125 dilution of this antibody detected α-synuclein in 10 µg of human fetal brain tissue lysate.

Target description

~14.5 kDa observed. 14.46/11.37/13.11 kDa (human isoform NACP140/NACP112/NACP126) calculated.. Uncharacterized bands may be observed in some lysate(s).

Physical form

Format: Purified
Purified mouse IgG2b in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide

Other Notes

Concentration: Please refer to lot specific datasheet.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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John B Sanderson et al.
Brain communications, 2(1), fcaa010-fcaa010 (2020-04-14)
Since researchers identified α-synuclein as the principal component of Lewy bodies and Lewy neurites, studies have suggested that it plays a causative role in the pathogenesis of dementia with Lewy bodies and other 'synucleinopathies'. While α-synuclein dyshomeostasis likely contributes to
Matteo Rovere et al.
FEBS letters, 592(9), 1464-1472 (2018-04-11)
α-Synuclein (αSyn) is a key player in the pathogenesis of Parkinson's disease and other synucleinopathies. Here, we report the existence of a novel soluble α-helical conformer of αSyn, obtained through transient interaction with lipid interfaces, and propose dynamic oligomerization as
Laura de Boni et al.
Acta neuropathologica, 143(4), 453-469 (2022-02-11)
The protein α-synuclein, a key player in Parkinson's disease (PD) and other synucleinopathies, exists in different physiological conformations: cytosolic unfolded aggregation-prone monomers and helical aggregation-resistant multimers. It has been shown that familial PD-associated missense mutations within the α-synuclein gene destabilize

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