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Merck
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Key Documents

AB5334P

Sigma-Aldrich

Anti-Synuclein α Antibody

Chemicon®, from sheep

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

sheep

Quality Level

antibody form

affinity purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

rat, human

manufacturer/tradename

Chemicon®

technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... SNCA(6622)

Specificity

Recognizes alpha synuclein.

Immunogen

Synthetic peptide corresponding amino acids 116-131 of human alpha synuclein.

Application

Detect Synuclein using this Anti-Synuclein Antibody, α validated for use in WB, IH(P).
Immunohistochemistry: 0.5-1 μg/mL on frozen or paraffin sections.

Western blot: 0.5-1 μg/mL

Optimal working dilutions must be determined by the end user.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases

Linkage

Replaces: 04-1053

Physical form

Affinity purified immunoglobulin in PBS containing 0.02% sodium azide. Lyophilized. Reconstitute with 50 μL of sterile distilled water. Centrifuge to remove any residue. Glycerol (1:1) can be added for additional stability.

Storage and Stability

Maintain lyophilized material at -70°C (dry) for up to 12 months. After reconstitution maintain at -20°C in undiluted aliquots for up to 6 months. Avoid repeated freeze/thaw cycles.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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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Optional

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Lojze M Smid et al.
Journal of Alzheimer's disease : JAD, 36(2), 261-274 (2013-04-10)
This work is aimed at correlating pre-mortem [18F]FDDNP positron emission tomography (PET) scan results in a patient with dementia with Lewy bodies (DLB), with cortical neuropathology distribution determined postmortem in three physical dimensions in whole brain coronal sections. Analysis of
Ivani Brys et al.
The European journal of neuroscience, 46(3), 1906-1917 (2017-04-04)
Parkinson's disease (PD) is a neurodegenerative disorder characterised by progressive motor symptoms resulting from chronic loss of dopaminergic neurons in the nigrostriatal pathway. The over expression of the protein alpha-synuclein in the substantia nigra has been used to induce progressive
Hazel L Roberts et al.
PloS one, 12(2), e0171925-e0171925 (2017-02-12)
α-Synuclein misfolding and aggregation is often accompanied by β-amyloid deposition in some neurodegenerative diseases. We hypothesised that α-synuclein promotes β-amyloid production from APP. β-Amyloid levels and APP amyloidogenic processing were investigated in neuronal cell lines stably overexpressing wildtype and mutant
Christopher Sinadinos et al.
Aging cell, 13(5), 935-945 (2014-07-26)
Glycogen is a branched polymer of glucose and the carbohydrate energy store for animal cells. In the brain, it is essentially found in glial cells, although it is also present in minute amounts in neurons. In humans, loss-of-function mutations in
Jennifer S McDowall et al.
Molecular and cellular neurosciences, 85, 1-11 (2017-08-16)
The normal cellular role of α-synuclein is of potential importance in understanding diseases in which an aggregated form of the protein has been implicated. A potential loss or change in the normal function of α-synuclein could play a role in

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