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S5566

Sigma-Aldrich

Anti-α-Synuclein antibody, Mouse monoclonal

clone Syn211, purified from hybridoma cell culture

Synonym(s):

Anti-SNCA

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

Syn211, monoclonal

form

buffered aqueous solution

mol wt

antigen 19 kDa

species reactivity

zebra finch, human

should not react with

rat, mouse

packaging

antibody small pack of 25 μL

concentration

~1 mg/mL

technique(s)

immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: 0.25 μg/mL using recombinant human α·-synuclein.

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SNCA(6622)

General description

The SNCA (synuclein α) gene codes for a 140-amino acid protein α-synuclein, that is mapped to human chromosome 4q21-23.
The SNCA (synuclein α) gene is mapped to human chromosome 4q22.1. The gene encodes a small synaptic protein called α-synuclein.

Immunogen

recombinant human α synuclein.

Application

Anti-α-Synuclein antibody, Mouse monoclonal has been used in western blotting and ELISA.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Flow cytometry/Cell sorting (1 paper)
Immunocytochemistry (1 paper)

Biochem/physiol Actions

Accumulation of α-synuclein in oligodendrocytes results in the loss of myelin and causes neurodegeneration, leading to multiple system atrophy. Synuclein-α is known to induce oligodendrocyte maturation. The encoded protein is considered to be an important aggregate of Lewy bodies, contributing to the pathogenesis of Parkinson disease.
Synuclein-α is known to induce oligodendrocyte maturation. Accumulation of α-synuclein in oligodendrocytes results in the loss of myelin and causes neurodegeneration, leading to multiple system atrophy. Mutations in the SNCA gene results in Parkinson′s disease.

Physical form

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 1 % bovine serum albumin and 15 mM sodium azide.

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Regional deficiencies in chaperone-mediated autophagy underlie α-synuclein aggregation and neurodegeneration
Malkus KA, et al.
Neurobiology of Disease, 46(3), 732-744 (2012)
Kavita Prasad et al.
Brain pathology (Zurich, Switzerland), 22(6), 811-825 (2012-03-29)
The role of Lewy bodies, Lewy neurites and α-synuclein (αSYN) in the pathophysiology and diagnosis of Parkinson's disease (PD) is unclear. We used postmortem human tissue, a panel of antibodies (Abs) and confocal microscopy to examine the three-dimensional neurochemical anatomy
Sabrina Büttner et al.
The EMBO journal, 32(23), 3041-3054 (2013-10-17)
Malfunctioning of the protein α-synuclein is critically involved in the demise of dopaminergic neurons relevant to Parkinson's disease. Nonetheless, the precise mechanisms explaining this pathogenic neuronal cell death remain elusive. Endonuclease G (EndoG) is a mitochondrially localized nuclease that triggers
α-synuclein in blood and brain from familial Parkinson disease with SNCA locus triplication.
Miller DW, et al.
Neurology, 62(10), 1835-1838 (2004)
Interactions of Pathological Hallmark Proteins
Olah J, et al.
The Journal of Biological Chemistry, 286(39), 34088-34100 (2011)

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