Application

Detect phospho-α-Synuclein using this Anti-phospho-α-Synuclein (Ser129) Antibody, clone 81A validated for use in Electron Microscopy, Immunocytochemistry, Immunofluorescence, Immunohistochemistry (Paraffin), Western Blotting.

Research Sub CategoryNeurodegenerative Diseases

Research CategoryNeuroscience

Immunohistochemistry Analysis: A 1:250-1,000 dilution from a representative lot detected α-synuclein pSer129 immunoreactivity associated with pathologic inclusions in M83 transgenic mouse brain and human PD brian.
Immunocytochemistry Analysis: A representative lot detected Ser129-phosphorylated α-synuclein in Lewy bodies-/LB- and Lewy-neurite-/LN-like inclusions in cultured embryonic hippocampal neurons from wild-type mice and mice carrying human mutant P301S tau transgene, but not Snca-/- mice, upon exposure to preformed α-synuclein fibrils (pffs) from C-terminally truncated, Myc-tagged α-synuclein (Guo, J.L., and Giasson, B.I. (2013). Cell. 154(1):103-117).
Electron Microscopy Analysis: A representative lot detected phosphorylated α-synuclein in close physical associations of tau in filamentous structures within neuronal processes of human P301S mutant tau transgenic mouse embryo hippocampal neurons exposed to α-synuclein fibrils formed by repeated rounds of self-seeding using C-terminally truncated, Myc-tagged α-synuclein (Guo, J.L., and Giasson, B.I. (2013). Cell. 154(1):103-117).
Western Blotting Analysis: A representative lot detected phosphorylation of the Triton-insoluble α-synuclein formed in cultured mouse embryonic hippocampal neurons upon exposure to preformed α-synuclein fibrils (pffs) from C-terminally truncated, Myc-tagged α-synuclein (Guo, J.L., and Giasson, B.I. (2013). Cell. 154(1):103-117).
Western Blotting Analysis: A representative lot detected Ser129 phosphorylation of Triton-insoluble, but not Triton-soluble, α-synuclein in the cingulate cortex extracts from DLB (dementia with Lewy bodies) patients and the cerebella extracts from patients with multiple systems atrophy (MSA) (Waxman, E.A., et al. (2008). J. Neuropathol. Exp. Neurol. 67(5):402-416).
Western Blotting Analysis: A representative lot detected CK1- and CK2-catalyzed alpha-synuclein Ser129 phosphorylation, but not CK1-catalyzed α-synuclein Ser87 phosphorylation, nor non-phosphorylated α-synuclein (Waxman, E.A., et al. (2008). J. Neuropathol. Exp. Neurol. 67(5):402-416).
Immunohistochemistry Analysis: A representative lot detected pathologic inclusions-associated α-synuclein Ser129 phosphorylation in paraffin-embedded brain tissue sections from patients with PD (Parkinson′s disease), DLB (dementia with Lewy bodies) and MSA (multiple systems atrophy), while clone 81A detected no α-synuclein Ser129 phosphorylation associated with neurofibrillary tangles in the hippocampus of a patient with Alzheimer′s disease (Waxman, E.A., et al. (2008). J. Neuropathol. Exp. Neurol. 67(5):402-416).
Immunofluorescence Analysis: A representative lot detected pathologic inclusions-associated α-synuclein Ser129 phosphorylation by fluorescent immunohistochemistry in paraffin-embedded cingulate cortex sections from a patient with LB variant of Alzheimer′s disease (LBVAD) and in the cerebellum sections from a patient with multiple systems atrophy (MSA) (Waxman, E.A., et al. (2008). J. Neuropathol. Exp. Neurol. 67(5):402-416).

Note: Incubating the transferred membrane with a combination of 4% paraformaldehyde and 0.01R01;~R01;0.1% glutaraldehyde is reported to produce an approximately 10-fold increase in the detection sensitivity of α-synuclein Ser129 phosphorylation by Western blotting. If not fixed, α-synuclein monomers can detach from the transferred membrane during incubation (Sasaki, A., et al. (2015). Sci. Rep. 5:14211).

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.

General description

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) Lewy bodies (LBs) in Parkinson's disease (PD) and dementia with LB (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). Both casein kinase-1 (CK-1) and CK-2 can catalyze the phosphorylation of alpha-synuclein on Ser129, and Ser129-phosphorylated alpha-synuclein is found in alpha-synuclein inclusions.

Immunogen

Epitope: pSer129

KLH-conjugated linear peptide corresponding a human α-synuclein sequence with the phosphorylated Ser129.

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Protein G Purified

Format: Purified

Purified mouse monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Quality

Identity Confirmation by Isotyping Test.

Isotyping Analysis: The identity of this monoclonal antibody is confirmed by isotyping test to be IgG2aκ.

Specificity

Clone 81A detected CK1- and CK2-catalyzed alpha-synuclein Ser129 phosphorylation, but not CK1-catalyzed alpha-synuclein Ser87 phosphorylation, nor non-phosphorylated alpha-synuclein (Waxman, E.A., et al. (2008). J. Neuropathol. Exp. Neurol. 67(5):402-416).

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Target description

14.46 kDa calculated.