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MABN1818

Sigma-Aldrich

Anti-α-Synuclein (SNCA) Antibody

mouse monoclonal, SOY1

Sinónimos:

Alpha-synuclein, NACP, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Synuclein alpha-140

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200 μL
$414.00

$414.00


Fecha estimada de envío24 de abril de 2025

Está disponible un anticuerpo recombinante y sin conservantes para su diana. Pruebe ZRB1134

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200 μL
$414.00

About This Item

Código UNSPSC:
12352203
eCl@ss:
32160702

$414.00


Fecha estimada de envío24 de abril de 2025

Está disponible un anticuerpo recombinante y sin conservantes para su diana. Pruebe ZRB1134

Solicitar un pedido a granel

Nombre del producto

Anti-α-Synuclein Antibody, clone SOY1, clone SOY1, from mouse

origen biológico

mouse

Nivel de calidad

forma del anticuerpo

purified immunoglobulin

tipo de anticuerpo

primary antibodies

clon

SOY1, monoclonal

reactividad de especies

mouse, human

reactividad de especies (predicha por homología)

rat (based on 100% sequence homology)

técnicas

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

isotipo

IgG2bκ

Nº de acceso NCBI

Nº de acceso UniProt

Condiciones de envío

ambient

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... SNCA(6622)

Descripción general

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.

Especificidad

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.

Inmunógeno

Purified human erythrocyte alpha-synuclein.

Aplicación

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).

Calidad

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.

Descripción de destino

~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).

Forma física

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

Otras notas

Concentration: Please refer to lot specific datasheet.

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Opcional

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°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
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
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

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