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Merck

AB5464

Anti-Synuclein Antibody, pan

CHEMICON®, rabbit polyclonal

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About This Item

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

Key Documents

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Product Name

Anti-Synuclein Antibody, pan, serum, Chemicon®

biological source

rabbit

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human, rat

manufacturer/tradename

Chemicon®

technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

NCBI accession no.

NM_000345.2
NM_007308.1

UniProt accession no.

O76070
P37840
Q16143

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... SNCA(6622)

Application

Detect Synuclein using this Anti-Synuclein Antibody, pan validated for use in WB, IH(P).
Western blot: 1:1,000.

Immunohistochemistry: 1:1,000 on frozen and paraffin embedded tissue.

Optimal working dilutions must be determined by end user.

Biochem/physiol Actions

Pan synuclein. Initial testing by immunohistochemistry indicates that the antibody staining pattern overlaps alpha, beta, and gamma-synuclein maps.

Immunogen

Peptide corresponding to the amino acids 11-26 of human a, b, and g (82%)-synuclein protein. The peptide was chosen so that the antibody would recognize all three forms of synuclein.

Legal Information

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

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Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

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Li-Wen Ko et al.
Journal of neuropathology and experimental neurology, 67(11), 1084-1096 (2008-10-30)
Filamentous alpha-synuclein (alpha-syn) aggregates form Lewy bodies (LBs), the neuropathologic hallmarks of Parkinson disease and related alpha-synucleinopathies. To model Lewy body-associated neurodegeneration, we generated transfectant 3D5 of human neuronal-type in which expression of human wild-type alpha-syn is regulated by the
Peizhou Jiang et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 22(9), 3165-3174 (2008-05-22)
The accumulation of filamentous alpha-synuclein (alpha-S) is associated with Parkinson's disease. It remains controversial as to the mode (antiparallel or parallel) of alpha-S self-assembly and whether an exact alignment of the central hydrophobic region is essential. In the present study
Jochen Klucken et al.
Autophagy, 8(5), 754-766 (2012-06-01)
Synucleinopathies like Parkinson disease and dementia with Lewy bodies (DLB) are characterized by α-synuclein aggregates within neurons (Lewy bodies) and their processes (Lewy neurites). Whereas α-synuclein has been genetically linked to the disease process, the pathological relevance of α-synuclein aggregates

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