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AB5334P

Sigma-Aldrich

Anti-Synuclein α Antibody

Chemicon®, from sheep

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About This Item

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

Source biologique

sheep

Niveau de qualité

Forme d'anticorps

affinity purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

polyclonal

Produit purifié par

affinity chromatography

Espèces réactives

rat, human

Fabricant/nom de marque

Chemicon®

Technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... SNCA(6622)

Spécificité

Recognizes alpha synuclein.

Immunogène

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

Liaison

Replaces: 04-1053

Forme physique

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.

Stockage et stabilité

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.

Informations légales

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

Clause de non-responsabilité

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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Code de la classe de stockage

13 - Non Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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
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
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
Haiyan Lou et al.
The Journal of biological chemistry, 285(23), 17648-17661 (2010-04-02)
Alpha-synuclein (a-Syn), a protein implicated in Parkinson disease, contributes significantly to dopamine metabolism. a-Syn binding inhibits the activity of tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis. Phosphorylation of TH stimulates its activity, an effect that is reversed by

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